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Histone H3.1 (Histone H3/a) (Histone H3/b) (Histone H3/c) (Histone H3/d) (Histone H3/f) (Histone H3/h) (Histone H3/i) (Histone H3/j) (Histone H3/k) (Histone H3/l)

 H31_HUMAN               Reviewed;         136 AA.
P68431; A0PJT7; A5PLR1; P02295; P02296; P16106; Q6ISV8; Q6NWP8;
Q6NWP9; Q6NXU4; Q71DJ3; Q93081;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-OCT-2017, entry version 155.
RecName: Full=Histone H3.1;
AltName: Full=Histone H3/a;
AltName: Full=Histone H3/b;
AltName: Full=Histone H3/c;
AltName: Full=Histone H3/d;
AltName: Full=Histone H3/f;
AltName: Full=Histone H3/h;
AltName: Full=Histone H3/i;
AltName: Full=Histone H3/j;
AltName: Full=Histone H3/k;
AltName: Full=Histone H3/l;
Name=HIST1H3A; Synonyms=H3FA;
and
Name=HIST1H3B; Synonyms=H3FL;
and
Name=HIST1H3C; Synonyms=H3FC;
and
Name=HIST1H3D; Synonyms=H3FB;
and
Name=HIST1H3E; Synonyms=H3FD;
and
Name=HIST1H3F; Synonyms=H3FI;
and
Name=HIST1H3G; Synonyms=H3FH;
and
Name=HIST1H3H; Synonyms=H3FK;
and
Name=HIST1H3I; Synonyms=H3FF;
and
Name=HIST1H3J; Synonyms=H3FJ;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3B).
PubMed=6647026; DOI=10.1093/nar/11.21.7409;
Zhong R., Roeder R.G., Heintz N.;
"The primary structure and expression of four cloned human histone
genes.";
Nucleic Acids Res. 11:7409-7425(1983).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3013246;
Marashi F., Helms S., Shiels A., Silverstein S., Greenspan D.S.,
Stein G., Stein J.;
"Enhancer-facilitated expression of prokaryotic and eukaryotic genes
using human histone gene 5' regulatory sequences.";
Biochem. Cell Biol. 64:277-289(1986).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (H3FD).
PubMed=1916825; DOI=10.1016/0888-7543(91)90183-F;
Albig W., Kardalinou E., Drabent B., Zimmer A., Doenecke D.;
"Isolation and characterization of two human H1 histone genes within
clusters of core histone genes.";
Genomics 10:940-948(1991).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8227173; DOI=10.1002/jcb.240520402;
Kardalinou E., Eick S., Albig W., Doenecke D.;
"Association of a human H1 histone gene with an H2A pseudogene and
genes encoding H2B.1 and H3.1 histones.";
J. Cell. Biochem. 52:375-383(1993).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Blood;
Runge D., Eick S., Doenecke D.;
"Expression of human histone h1.1 and the nearby core histones.";
Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3I).
PubMed=9031620; DOI=10.1016/S0378-1119(96)00582-3;
Albig W., Meergans T., Doenecke D.;
"Characterization of the H1.5 gene completes the set of human H1
subtype genes.";
Gene 184:141-148(1997).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3D; HIST1H3F AND HIST1H3G).
PubMed=9119399; DOI=10.1006/geno.1996.4592;
Albig W., Kioschis P., Poustka A., Meergans K., Doenecke D.;
"Human histone gene organization: nonregular arrangement within a
large cluster.";
Genomics 40:314-322(1997).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3H AND HIST1H3J).
PubMed=9439656; DOI=10.1007/s004390050630;
Albig W., Doenecke D.;
"The human histone gene cluster at the D6S105 locus.";
Hum. Genet. 101:284-294(1997).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3A; HIST1H3B; HIST1H3C;
HIST1H3D; HIST1H3E; HIST1H3F; HIST1H3G; HIST1H3H; HIST1H3I; HIST1H3J).
PubMed=12408966; DOI=10.1006/geno.2002.6850;
Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.;
"The human and mouse replication-dependent histone genes.";
Genomics 80:487-498(2002).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Caudate nucleus, Stomach, and Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[14]
PARTIAL PROTEIN SEQUENCE.
TISSUE=Spleen;
PubMed=7309716;
Ohe Y., Iwai K.;
"Human spleen histone H3. Isolation and amino acid sequence.";
J. Biochem. 90:1205-1211(1981).
[15]
PROTEIN SEQUENCE OF 2-20, METHYLATION AT LYS-10; LYS-28 AND LYS-37,
PHOSPHORYLATION AT THR-4; SER-11 AND SER-29, ACETYLATION AT LYS-10 AND
LYS-15, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16185088; DOI=10.1021/bi050906n;
Garcia B.A., Barber C.M., Hake S.B., Ptak C., Turner F.B., Busby S.A.,
Shabanowitz J., Moran R.G., Allis C.D., Hunt D.F.;
"Modifications of human histone H3 variants during mitosis.";
Biochemistry 44:13202-13213(2005).
[16]
PROTEIN SEQUENCE OF 58-64; 117-120 AND 124-135, AND PHOSPHORYLATION AT
SER-11 AND SER-29.
PubMed=10464286; DOI=10.1074/jbc.274.36.25543;
Goto H., Tomono Y., Ajiro K., Kosako H., Fujita M., Sakurai M.,
Okawa K., Iwamatsu A., Okigaki T., Takahashi T., Inagaki M.;
"Identification of a novel phosphorylation site on histone H3 coupled
with mitotic chromosome condensation.";
J. Biol. Chem. 274:25543-25549(1999).
[17]
METHYLATION AT LYS-10.
PubMed=11242053; DOI=10.1038/35065132;
Lachner M., O'Carroll D., Rea S., Mechtler K., Jenuwein T.;
"Methylation of histone H3 lysine 9 creates a binding site for HP1
proteins.";
Nature 410:116-120(2001).
[18]
PHOSPHORYLATION AT SER-11 AND SER-29.
PubMed=11856369; DOI=10.1046/j.1356-9597.2001.00498.x;
Goto H., Yasui Y., Nigg E.A., Inagaki M.;
"Aurora-B phosphorylates Histone H3 at serine28 with regard to the
mitotic chromosome condensation.";
Genes Cells 7:11-17(2002).
[19]
PHOSPHORYLATION AT SER-11 AND THR-12.
PubMed=12560483; DOI=10.1093/nar/gkg176;
Preuss U., Landsberg G., Scheidtmann K.H.;
"Novel mitosis-specific phosphorylation of histone H3 at Thr11
mediated by Dlk/ZIP kinase.";
Nucleic Acids Res. 31:878-885(2003).
[20]
METHYLATION AT ARG-18.
PubMed=15471871; DOI=10.1074/jbc.M410021200;
Ananthanarayanan M., Li S., Balasubramaniyan N., Suchy F.J.,
Walsh M.J.;
"Ligand-dependent activation of the farnesoid X-receptor directs
arginine methylation of histone H3 by CARM1.";
J. Biol. Chem. 279:54348-54357(2004).
[21]
METHYLATION AT LYS-80.
PubMed=15525939; DOI=10.1038/nature03114;
Huyen Y., Zgheib O., Ditullio R.A. Jr., Gorgoulis V.G., Zacharatos P.,
Petty T.J., Sheston E.A., Mellert H.S., Stavridi E.S.,
Halazonetis T.D.;
"Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand
breaks.";
Nature 432:406-411(2004).
[22]
CITRULLINATION AT ARG-9 AND ARG-18, AND METHYLATION AT ARG-18.
PubMed=15345777; DOI=10.1126/science.1101400;
Wang Y., Wysocka J., Sayegh J., Lee Y.-H., Perlin J.R., Leonelli L.,
Sonbuchner L.S., McDonald C.H., Cook R.G., Dou Y., Roeder R.G.,
Clarke S., Stallcup M.R., Allis C.D., Coonrod S.A.;
"Human PAD4 regulates histone arginine methylation levels via
demethylimination.";
Science 306:279-283(2004).
[23]
PHOSPHORYLATION AT THR-4; SER-11 AND SER-29.
PubMed=15681610; DOI=10.1101/gad.1267105;
Dai J., Sultan S., Taylor S.S., Higgins J.M.G.;
"The kinase haspin is required for mitotic histone H3 Thr 3
phosphorylation and normal metaphase chromosome alignment.";
Genes Dev. 19:472-488(2005).
[24]
PHOSPHORYLATION AT SER-29.
PubMed=15684425; DOI=10.1074/jbc.M410521200;
Choi H.S., Choi B.Y., Cho Y.-Y., Zhu F., Bode A.M., Dong Z.;
"Phosphorylation of Ser28 in histone H3 mediated by mixed lineage
kinase-like mitogen-activated protein triple kinase alpha.";
J. Biol. Chem. 280:13545-13553(2005).
[25]
METHYLATION AT LYS-37 AND LYS-38, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=15983376; DOI=10.1073/pnas.0503189102;
Coon J.J., Ueberheide B., Syka J.E.P., Dryhurst D.D., Ausio J.,
Shabanowitz J., Hunt D.F.;
"Protein identification using sequential ion/ion reactions and tandem
mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 102:9463-9468(2005).
[26]
ACETYLATION AT LYS-10; LYS-15; LYS-19 AND LYS-24, METHYLATION AT
LYS-5; LYS-10; LYS-19; LYS-28; LYS-37; LYS-65; LYS-80 AND LYS-123, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16267050; DOI=10.1074/jbc.M509266200;
Hake S.B., Garcia B.A., Duncan E.M., Kauer M., Dellaire G.,
Shabanowitz J., Bazett-Jones D.P., Allis C.D., Hunt D.F.;
"Expression patterns and post-translational modifications associated
with mammalian histone H3 variants.";
J. Biol. Chem. 281:559-568(2006).
[27]
METHYLATION AT LYS-5 AND LYS-10, ACETYLATION AT LYS-10; LYS-15 AND
LYS-24, PHOSPHORYLATION AT SER-11 AND SER-29, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=16457588; DOI=10.1021/pr050266a;
Thomas C.E., Kelleher N.L., Mizzen C.A.;
"Mass spectrometric characterization of human histone H3: a bird's eye
view.";
J. Proteome Res. 5:240-247(2006).
[28]
UBIQUITINATION.
PubMed=16678110; DOI=10.1016/j.molcel.2006.03.035;
Wang H., Zhai L., Xu J., Joo H.-Y., Jackson S., Erdjument-Bromage H.,
Tempst P., Xiong Y., Zhang Y.;
"Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin
ligase facilitates cellular response to DNA damage.";
Mol. Cell 22:383-394(2006).
[29]
ACETYLATION AT LYS-10; LYS-15; LYS-19; LYS-24 AND LYS-28, METHYLATION
AT LYS-28; LYS-37 AND LYS-80, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16627869; DOI=10.1074/mcp.M600007-MCP200;
Beck H.C., Nielsen E.C., Matthiesen R., Jensen L.H., Sehested M.,
Finn P., Grauslund M., Hansen A.M., Jensen O.N.;
"Quantitative proteomic analysis of post-translational modifications
of human histones.";
Mol. Cell. Proteomics 5:1314-1325(2006).
[30]
ACETYLATION AT LYS-10 AND LYS-15, METHYLATION AT ARG-18, AND
CITRULLINATION AT ARG-18.
PubMed=16497732; DOI=10.1210/me.2005-0365;
Miao F., Li S., Chavez V., Lanting L., Natarajan R.;
"Coactivator-associated arginine methyltransferase-1 enhances nuclear
factor-kappaB-mediated gene transcription through methylation of
histone H3 at arginine 17.";
Mol. Endocrinol. 20:1562-1573(2006).
[31]
CITRULLINATION AT ARG-3; ARG-9; ARG-18 AND ARG-27.
PubMed=16567635; DOI=10.1073/pnas.0509639103;
Arita K., Shimizu T., Hashimoto H., Hidaka Y., Yamada M., Sato M.;
"Structural basis for histone N-terminal recognition by human
peptidylarginine deiminase 4.";
Proc. Natl. Acad. Sci. U.S.A. 103:5291-5296(2006).
[32]
METHYLATION AT ARG-3 BY PRMT6.
PubMed=18079182; DOI=10.1101/gad.447007;
Hyllus D., Stein C., Schnabel K., Schiltz E., Imhof A., Dou Y.,
Hsieh J., Bauer U.M.;
"PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4
trimethylation.";
Genes Dev. 21:3369-3380(2007).
[33]
ACETYLATION AT LYS-5; LYS-10; LYS-15; LYS-19; LYS-24; LYS-28; LYS-37;
LYS-57 AND LYS-80, METHYLATION AT LYS-5; LYS-10; LYS-19; LYS-24;
LYS-28; LYS-37; LYS-57; LYS-65; LYS-80 AND LYS-123, AND IDENTIFICATION
BY MASS SPECTROMETRY.
PubMed=17194708; DOI=10.1074/jbc.M607900200;
Garcia B.A., Hake S.B., Diaz R.L., Kauer M., Morris S.A., Recht J.,
Shabanowitz J., Mishra N., Strahl B.D., Allis C.D., Hunt D.F.;
"Organismal differences in post-translational modifications in
histones H3 and H4.";
J. Biol. Chem. 282:7641-7655(2007).
[34]
ACETYLATION AT LYS-37.
PubMed=17189264; DOI=10.1074/jbc.M607909200;
Morris S.A., Rao B., Garcia B.A., Hake S.B., Diaz R.L.,
Shabanowitz J., Hunt D.F., Allis C.D., Lieb J.D., Strahl B.D.;
"Identification of histone H3 lysine 36 acetylation as a highly
conserved histone modification.";
J. Biol. Chem. 282:7632-7640(2007).
[35]
METHYLATION AT ARG-3 BY PRMT6.
PubMed=17898714; DOI=10.1038/nature06166;
Guccione E., Bassi C., Casadio F., Martinato F., Cesaroni M.,
Schuchlautz H., Luescher B., Amati B.;
"Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are
mutually exclusive.";
Nature 449:933-937(2007).
[36]
PHOSPHORYLATION AT THR-12 BY CHEK1.
PubMed=18243098; DOI=10.1016/j.cell.2007.12.013;
Shimada M., Niida H., Zineldeen D.H., Tagami H., Tanaka M., Saito H.,
Nakanishi M.;
"Chk1 is a histone H3 threonine 11 kinase that regulates DNA damage-
induced transcriptional repression.";
Cell 132:221-232(2008).
[37]
METHYLATION AT ARG-3 BY PRMT6.
PubMed=18077460; DOI=10.1074/jbc.C700192200;
Iberg A.N., Espejo A., Cheng D., Kim D., Michaud-Levesque J.,
Richard S., Bedford M.T.;
"Arginine methylation of the histone H3 tail impedes effector
binding.";
J. Biol. Chem. 283:3006-3010(2008).
[38]
PHOSPHORYLATION AT THR-12.
PubMed=18066052; DOI=10.1038/ncb1668;
Metzger E., Yin N., Wissmann M., Kunowska N., Fischer K.,
Friedrichs N., Patnaik D., Higgins J.M., Potier N., Scheidtmann K.H.,
Buettner R., Schule R.;
"Phosphorylation of histone H3 at threonine 11 establishes a novel
chromatin mark for transcriptional regulation.";
Nat. Cell Biol. 10:53-60(2008).
[39]
ACETYLATION AT LYS-116 AND LYS-123.
PubMed=19520870; DOI=10.1074/jbc.M109.003202;
Manohar M., Mooney A.M., North J.A., Nakkula R.J., Picking J.W.,
Edon A., Fishel R., Poirier M.G., Ottesen J.J.;
"Acetylation of histone H3 at the nucleosome dyad alters DNA-histone
binding.";
J. Biol. Chem. 284:23312-23321(2009).
[40]
PHOSPHORYLATION AT TYR-42.
PubMed=19783980; DOI=10.1038/nature08448;
Dawson M.A., Bannister A.J., Gottgens B., Foster S.D., Bartke T.,
Green A.R., Kouzarides T.;
"JAK2 phosphorylates histone H3Y41 and excludes HP1alpha from
chromatin.";
Nature 461:819-822(2009).
[41]
PHOSPHORYLATION AT SER-58 AND THR-81.
PubMed=20850016; DOI=10.1016/j.cell.2010.08.020;
Vermeulen M., Eberl H.C., Matarese F., Marks H., Denissov S.,
Butter F., Lee K.K., Olsen J.V., Hyman A.A., Stunnenberg H.G.,
Mann M.;
"Quantitative interaction proteomics and genome-wide profiling of
epigenetic histone marks and their readers.";
Cell 142:967-980(2010).
[42]
PHOSPHORYLATION AT THR-7.
PubMed=20228790; DOI=10.1038/nature08839;
Metzger E., Imhof A., Patel D., Kahl P., Hoffmeyer K., Friedrichs N.,
Muller J.M., Greschik H., Kirfel J., Ji S., Kunowska N.,
Beisenherz-Huss C., Gunther T., Buettner R., Schule R.;
"Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation
at histone H3K4.";
Nature 464:792-796(2010).
[43]
CROTONYLATION AT LYS-5; LYS-10; LYS-19; LYS-24; LYS-28 AND LYS-57.
PubMed=21925322; DOI=10.1016/j.cell.2011.08.008;
Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T.,
Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q.,
Wysocka J., Ye Y., Khochbin S., Ren B., Zhao Y.;
"Identification of 67 histone marks and histone lysine crotonylation
as a new type of histone modification.";
Cell 146:1016-1028(2011).
[44]
METHYLATION AT LYS-57.
PubMed=22387026; DOI=10.1016/j.molcel.2012.01.019;
Yu Y., Song C., Zhang Q., Dimaggio P.A., Garcia B.A., York A.,
Carey M.F., Grunstein M.;
"Histone H3 lysine 56 methylation regulates DNA replication through
its interaction with PCNA.";
Mol. Cell 46:7-17(2012).
[45]
ALLYSINE AT LYS-5.
PubMed=22483618; DOI=10.1016/j.molcel.2012.03.002;
Herranz N., Dave N., Millanes-Romero A., Morey L., Diaz V.M.,
Lorenz-Fonfria V., Gutierrez-Gallego R., Jeronimo C., Di Croce L.,
Garcia de Herreros A., Peiro S.;
"Lysyl oxidase-like 2 deaminates lysine 4 in histone H3.";
Mol. Cell 46:369-376(2012).
[46]
SUCCINYLATION AT LYS-15; LYS-57; LYS-80 AND LYS-123.
PubMed=22389435; DOI=10.1074/mcp.M111.015875;
Xie Z., Dai J., Dai L., Tan M., Cheng Z., Wu Y., Boeke J.D., Zhao Y.;
"Lysine succinylation and lysine malonylation in histones.";
Mol. Cell. Proteomics 11:100-107(2012).
[47]
INVOLVEMENT IN GLM, AND VARIANT GLM MET-28.
PubMed=22286216; DOI=10.1038/ng.1102;
St. Jude Children's Research Hospital-Washington University Pediatric Cancer Genome Project;
Wu G., Broniscer A., McEachron T.A., Lu C., Paugh B.S., Becksfort J.,
Qu C., Ding L., Huether R., Parker M., Zhang J., Gajjar A., Dyer M.A.,
Mullighan C.G., Gilbertson R.J., Mardis E.R., Wilson R.K.,
Downing J.R., Ellison D.W., Zhang J., Baker S.J.;
"Somatic histone H3 alterations in pediatric diffuse intrinsic pontine
gliomas and non-brainstem glioblastomas.";
Nat. Genet. 44:251-253(2012).
[48]
ACETYLATION AT LYS-123.
PubMed=23415232; DOI=10.1016/j.cell.2013.01.032;
Tropberger P., Pott S., Keller C., Kamieniarz-Gdula K., Caron M.,
Richter F., Li G., Mittler G., Liu E.T., Buhler M., Margueron R.,
Schneider R.;
"Regulation of transcription through acetylation of H3K122 on the
lateral surface of the histone octamer.";
Cell 152:859-872(2013).
[49]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[50]
BUTYRYLATION AT LYS-10; LYS-19 AND LYS-24.
PubMed=27105113; DOI=10.1016/j.molcel.2016.03.014;
Goudarzi A., Zhang D., Huang H., Barral S., Kwon O.K., Qi S., Tang Z.,
Buchou T., Vitte A.L., He T., Cheng Z., Montellier E., Gaucher J.,
Curtet S., Debernardi A., Charbonnier G., Puthier D., Petosa C.,
Panne D., Rousseaux S., Roeder R.G., Zhao Y., Khochbin S.;
"Dynamic competing histone H4 K5K8 acetylation and butyrylation are
hallmarks of highly active gene promoters.";
Mol. Cell 62:169-180(2016).
[51]
HYDROXYBUTYRYLATION AT LYS-5; LYS-10; LYS-15; LYS-19; LYS-24; LYS-28;
LYS-57; LYS-80 AND LYS-123.
PubMed=27105115; DOI=10.1016/j.molcel.2016.03.036;
Xie Z., Zhang D., Chung D., Tang Z., Huang H., Dai L., Qi S., Li J.,
Colak G., Chen Y., Xia C., Peng C., Ruan H., Kirkey M., Wang D.,
Jensen L.M., Kwon O.K., Lee S., Pletcher S.D., Tan M., Lombard D.B.,
White K.P., Zhao H., Li J., Roeder R.G., Yang X., Zhao Y.;
"Metabolic regulation of gene expression by histone lysine beta-
hydroxybutyrylation.";
Mol. Cell 62:194-206(2016).
[52]
HYDROXYBUTYRYLATION AT LYS-5; LYS-10; LYS-15; LYS-19; LYS-24; LYS-28;
LYS-37; LYS-57; LYS-65; LYS-80 AND LYS-123.
PubMed=24681537; DOI=10.1038/nchembio.1497;
Dai L., Peng C., Montellier E., Lu Z., Chen Y., Ishii H.,
Debernardi A., Buchou T., Rousseaux S., Jin F., Sabari B.R., Deng Z.,
Allis C.D., Ren B., Khochbin S., Zhao Y.;
"Lysine 2-hydroxyisobutyrylation is a widely distributed active
histone mark.";
Nat. Chem. Biol. 10:365-370(2014).
[53]
INVOLVEMENT IN SOFT TISSUE SARCOMAS, VARIANTS ILE-37 AND MET-37, AND
CHARACTERIZATION OF VARIANTS ILE-37 AND MET-37.
PubMed=27174990; DOI=10.1126/science.aac7272;
Lu C., Jain S.U., Hoelper D., Bechet D., Molden R.C., Ran L.,
Murphy D., Venneti S., Hameed M., Pawel B.R., Wunder J.S.,
Dickson B.C., Lundgren S.M., Jani K.S., De Jay N.,
Papillon-Cavanagh S., Andrulis I.L., Sawyer S.L., Grynspan D.,
Turcotte R.E., Nadaf J., Fahiminiyah S., Muir T.W., Majewski J.,
Thompson C.B., Chi P., Garcia B.A., Allis C.D., Jabado N., Lewis P.W.;
"Histone H3K36 mutations promote sarcomagenesis through altered
histone methylation landscape.";
Science 352:844-849(2016).
[54]
ADP-RIBOSYLATION AT SER-11 AND SER-29.
PubMed=28190768; DOI=10.1016/j.molcel.2017.01.003;
Bonfiglio J.J., Fontana P., Zhang Q., Colby T., Gibbs-Seymour I.,
Atanassov I., Bartlett E., Zaja R., Ahel I., Matic I.;
"Serine ADP-ribosylation depends on HPF1.";
Mol. Cell 0:0-0(2017).
[55]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 8-15 IN COMPLEX WITH YWHAZ.
PubMed=16246723; DOI=10.1016/j.molcel.2005.08.032;
Macdonald N., Welburn J.P.I., Noble M.E.M., Nguyen A., Yaffe M.B.,
Clynes D., Moggs J.G., Orphanides G., Thomson S., Edmunds J.W.,
Clayton A.L., Endicott J.A., Mahadevan L.C.;
"Molecular basis for the recognition of phosphorylated and
phosphoacetylated histone h3 by 14-3-3.";
Mol. Cell 20:199-211(2005).
[56]
X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 2-20 IN COMPLEX WITH CHD1.
PubMed=16372014; DOI=10.1038/nature04290;
Flanagan J.F., Mi L.-Z., Chruszcz M., Cymborowski M., Clines K.L.,
Kim Y., Minor W., Rastinejad F., Khorasanizadeh S.;
"Double chromodomains cooperate to recognize the methylated histone H3
tail.";
Nature 438:1181-1185(2005).
[57]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
PubMed=15951514; DOI=10.1093/nar/gki663;
Tsunaka Y., Kajimura N., Tate S., Morikawa K.;
"Alteration of the nucleosomal DNA path in the crystal structure of a
human nucleosome core particle.";
Nucleic Acids Res. 33:3424-3434(2005).
[58]
CHARACTERIZATION OF VARIANT GLM MET-28.
PubMed=23603901; DOI=10.1101/gad.217778.113;
Chan K.M., Fang D., Gan H., Hashizume R., Yu C., Schroeder M.,
Gupta N., Mueller S., James C.D., Jenkins R., Sarkaria J., Zhang Z.;
"The histone H3.3K27M mutation in pediatric glioma reprograms H3K27
methylation and gene expression.";
Genes Dev. 27:985-990(2013).
[59]
VARIANT MET-37.
PubMed=28067913; DOI=10.1038/ng.3757;
Papillon-Cavanagh S., Lu C., Gayden T., Mikael L.G., Bechet D.,
Karamboulas C., Ailles L., Karamchandani J., Marchione D.M.,
Garcia B.A., Weinreb I., Goldstein D., Lewis P.W., Dancu O.M.,
Dhaliwal S., Stecho W., Howlett C.J., Mymryk J.S., Barrett J.W.,
Nichols A.C., Allis C.D., Majewski J., Jabado N.;
"Impaired H3K36 methylation defines a subset of head and neck squamous
cell carcinomas.";
Nat. Genet. 49:180-185(2017).
-!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and
compact DNA into chromatin, limiting DNA accessibility to the
cellular machineries which require DNA as a template. Histones
thereby play a central role in transcription regulation, DNA
repair, DNA replication and chromosomal stability. DNA
accessibility is regulated via a complex set of post-translational
modifications of histones, also called histone code, and
nucleosome remodeling.
-!- SUBUNIT: The nucleosome is a histone octamer containing two
molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4
heterotetramer and two H2A-H2B heterodimers. The octamer wraps
approximately 147 bp of DNA. {ECO:0000269|PubMed:16246723,
ECO:0000269|PubMed:16372014}.
-!- INTERACTION:
O43918:AIRE; NbExp=20; IntAct=EBI-79722, EBI-1753081;
Q9Y294:ASF1A; NbExp=5; IntAct=EBI-79722, EBI-749553;
P83916:CBX1; NbExp=9; IntAct=EBI-79722, EBI-78129;
Q13185:CBX3; NbExp=5; IntAct=EBI-79722, EBI-78176;
P45973:CBX5; NbExp=9; IntAct=EBI-79722, EBI-78219;
Q9Y232:CDYL; NbExp=5; IntAct=EBI-79722, EBI-1387386;
Q9UER7-1:DAXX; NbExp=6; IntAct=EBI-79722, EBI-287635;
Q8WUP2:FBLIM1; NbExp=11; IntAct=EBI-79722, EBI-3864120;
P62805:HIST2H4B; NbExp=6; IntAct=EBI-79722, EBI-302023;
P42858:HTT; NbExp=2; IntAct=EBI-79722, EBI-466029;
Q9UNL4:ING4; NbExp=3; IntAct=EBI-79722, EBI-2866661;
P38991:IPL1 (xeno); NbExp=2; IntAct=EBI-79722, EBI-9319;
O75164:KDM4A; NbExp=7; IntAct=EBI-79722, EBI-936709;
Q03164:KMT2A; NbExp=11; IntAct=EBI-79722, EBI-591370;
Q9Y468:L3MBTL1; NbExp=2; IntAct=EBI-79722, EBI-1265089;
P49736:MCM2; NbExp=5; IntAct=EBI-79722, EBI-374819;
Q99549:MPHOSPH8; NbExp=5; IntAct=EBI-79722, EBI-2653928;
P49321:NASP; NbExp=3; IntAct=EBI-79722, EBI-716205;
P49321-2:NASP; NbExp=12; IntAct=EBI-79722, EBI-7038920;
Q9BVI0:PHF20; NbExp=6; IntAct=EBI-79722, EBI-2560802;
A8MW92:PHF20L1; NbExp=2; IntAct=EBI-79722, EBI-2560834;
P14618-1:PKM; NbExp=3; IntAct=EBI-79722, EBI-4304679;
Q8WTS6:SETD7; NbExp=3; IntAct=EBI-79722, EBI-1268586;
P25554:SGF29 (xeno); NbExp=11; IntAct=EBI-79722, EBI-21678;
Q96ES7:SGF29; NbExp=25; IntAct=EBI-79722, EBI-743117;
Q12888:TP53BP1; NbExp=5; IntAct=EBI-79722, EBI-396540;
P61964:WDR5; NbExp=11; IntAct=EBI-79722, EBI-540834;
P63104:YWHAZ; NbExp=3; IntAct=EBI-79722, EBI-347088;
Q8R5C8:Zmynd11 (xeno); NbExp=4; IntAct=EBI-79722, EBI-647813;
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
-!- DEVELOPMENTAL STAGE: Expressed during S phase, then expression
strongly decreases as cell division slows down during the process
of differentiation.
-!- PTM: Acetylation is generally linked to gene activation.
Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9
(H3R8me2s). Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac)
favors methylation at Arg-18 (H3R17me). Acetylation at Lys-123
(H3K122ac) by EP300/p300 plays a central role in chromatin
structure: localizes at the surface of the histone octamer and
stimulates transcription, possibly by promoting nucleosome
instability. {ECO:0000269|PubMed:11242053,
ECO:0000269|PubMed:15345777, ECO:0000269|PubMed:15471871,
ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050,
ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:16497732,
ECO:0000269|PubMed:16627869, ECO:0000269|PubMed:17194708,
ECO:0000269|PubMed:19520870, ECO:0000269|PubMed:23415232}.
-!- PTM: Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by
PADI4 impairs methylation and represses transcription.
{ECO:0000269|PubMed:15345777, ECO:0000269|PubMed:15471871,
ECO:0000269|PubMed:16497732, ECO:0000269|PubMed:16567635}.
-!- PTM: Asymmetric dimethylation at Arg-18 (H3R17me2a) by CARM1 is
linked to gene activation. Symmetric dimethylation at Arg-9
(H3R8me2s) by PRMT5 is linked to gene repression. Asymmetric
dimethylation at Arg-3 (H3R2me2a) by PRMT6 is linked to gene
repression and is mutually exclusive with H3 Lys-5 methylation
(H3K4me2 and H3K4me3). H3R2me2a is present at the 3' of genes
regardless of their transcription state and is enriched on
inactive promoters, while it is absent on active promoters.
{ECO:0000269|PubMed:15345777, ECO:0000269|PubMed:15471871,
ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588,
ECO:0000269|PubMed:16497732, ECO:0000269|PubMed:17194708,
ECO:0000269|PubMed:17898714, ECO:0000269|PubMed:18077460,
ECO:0000269|PubMed:18079182}.
-!- PTM: Methylation at Lys-5 (H3K4me), Lys-37 (H3K36me) and Lys-80
(H3K79me) are linked to gene activation. Methylation at Lys-5
(H3K4me) facilitates subsequent acetylation of H3 and H4.
Methylation at Lys-80 (H3K79me) is associated with DNA double-
strand break (DSB) responses and is a specific target for TP53BP1.
Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are linked to
gene repression. Methylation at Lys-10 (H3K9me) is a specific
target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents
subsequent phosphorylation at Ser-11 (H3S10ph) and acetylation of
H3 and H4. Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me)
require preliminary monoubiquitination of H2B at 'Lys-120'.
Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched
in inactive X chromosome chromatin. Monomethylation at Lys-57
(H3K56me1) by EHMT2/G9A in G1 phase promotes interaction with PCNA
and is required for DNA replication. {ECO:0000269|PubMed:10464286,
ECO:0000269|PubMed:11242053, ECO:0000269|PubMed:11856369,
ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:15525939,
ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:15983376,
ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050,
ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:16497732,
ECO:0000269|PubMed:16627869, ECO:0000269|PubMed:17189264,
ECO:0000269|PubMed:17194708, ECO:0000269|PubMed:22387026}.
-!- PTM: Phosphorylated at Thr-4 (H3T3ph) by HASPIN during prophase
and dephosphorylated during anaphase. Phosphorylation at Ser-11
(H3S10ph) by AURKB is crucial for chromosome condensation and
cell-cycle progression during mitosis and meiosis. In addition
phosphorylation at Ser-11 (H3S10ph) by RPS6KA4 and RPS6KA5 is
important during interphase because it enables the transcription
of genes following external stimulation, like mitogens, stress,
growth factors or UV irradiation and result in the activation of
genes, such as c-fos and c-jun. Phosphorylation at Ser-11
(H3S10ph), which is linked to gene activation, prevents
methylation at Lys-10 (H3K9me) but facilitates acetylation of H3
and H4. Phosphorylation at Ser-11 (H3S10ph) by AURKB mediates the
dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from
heterochromatin. Phosphorylation at Ser-11 (H3S10ph) is also an
essential regulatory mechanism for neoplastic cell transformation.
Phosphorylated at Ser-29 (H3S28ph) by MAP3K20 isoform 1, RPS6KA5
or AURKB during mitosis or upon ultraviolet B irradiation.
Phosphorylation at Thr-7 (H3T6ph) by PRKCB is a specific tag for
epigenetic transcriptional activation that prevents demethylation
of Lys-5 (H3K4me) by LSD1/KDM1A. At centromeres, specifically
phosphorylated at Thr-12 (H3T11ph) from prophase to early
anaphase, by DAPK3 and PKN1. Phosphorylation at Thr-12 (H3T11ph)
by PKN1 is a specific tag for epigenetic transcriptional
activation that promotes demethylation of Lys-10 (H3K9me) by
KDM4C/JMJD2C. Phosphorylation at Thr-12 (H3T11ph) by chromatin-
associated CHEK1 regulates the transcription of cell cycle
regulatory genes by modulating acetylation of Lys-10 (H3K9ac).
Phosphorylation at Tyr-42 (H3Y41ph) by JAK2 promotes exclusion of
CBX5 (HP1 alpha) from chromatin. {ECO:0000269|PubMed:10464286,
ECO:0000269|PubMed:11242053, ECO:0000269|PubMed:11856369,
ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:15681610,
ECO:0000269|PubMed:15684425, ECO:0000269|PubMed:16185088,
ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588,
ECO:0000269|PubMed:16497732, ECO:0000269|PubMed:16627869,
ECO:0000269|PubMed:17194708, ECO:0000269|PubMed:18066052,
ECO:0000269|PubMed:18243098, ECO:0000269|PubMed:19783980,
ECO:0000269|PubMed:20228790, ECO:0000269|PubMed:20850016}.
-!- PTM: Monoubiquitinated by RAG1 in lymphoid cells,
monoubiquitination is required for V(D)J recombination (By
similarity). Ubiquitinated by the CUL4-DDB-RBX1 complex in
response to ultraviolet irradiation. This may weaken the
interaction between histones and DNA and facilitate DNA
accessibility to repair proteins. {ECO:0000250|UniProtKB:Q6LED0,
ECO:0000269|PubMed:16678110}.
-!- PTM: Lysine deamination at Lys-5 (H3K4all) to form allysine is
mediated by LOXL2. Allysine formation by LOXL2 only takes place on
H3K4me3 and results in gene repression (PubMed:22483618).
{ECO:0000269|PubMed:22483618}.
-!- PTM: Crotonylation (Kcr) is specifically present in male germ
cells and marks testis-specific genes in post-meiotic cells,
including X-linked genes that escape sex chromosome inactivation
in haploid cells. Crotonylation marks active promoters and
enhancers and confers resistance to transcriptional repressors. It
is also associated with post-meiotically activated genes on
autosomes. {ECO:0000269|PubMed:21925322}.
-!- PTM: Butyrylation of histones marks active promoters and competes
with histone acetylation. It is present during late
spermatogenesis. {ECO:0000250|UniProtKB:P68433}.
-!- DISEASE: Glioma (GLM) [MIM:137800]: Gliomas are benign or
malignant central nervous system neoplasms derived from glial
cells. They comprise astrocytomas and glioblastoma multiforme that
are derived from astrocytes, oligodendrogliomas derived from
oligodendrocytes and ependymomas derived from ependymocytes.
{ECO:0000269|PubMed:22286216}. Note=The gene represented in this
entry is involved in disease pathogenesis. HIST1H3B mutations
affecting residue Lys-28 involved in post-translational
modifications of histone H3.1 are recurrent in malignant,
aggressive gliomas including pediatric non-brain stem glioblastoma
and diffuse intrinsic pontine glioma (DIPG) (PubMed:22286216). The
mechanism through which mutations lead to tumorigenesis involves
altered histone methylation, impaired regulation of Polycomb
repressive complex 2 (PRC2) activity, and aberrant epigenetic
regulation of gene expression (PubMed:23603901).
{ECO:0000269|PubMed:22286216, ECO:0000269|PubMed:23603901}.
-!- DISEASE: Note=HIST1H3B or HIST1H3C mutations affecting residue
Lys-37 of histone H3.1 are involved in the pathogenesis of
pediatric undifferentiated soft tissue sarcomas. The mechanism
through which mutations lead to tumorigenesis involves altered
histones methylation with gain of global H3K27 methylation,
altered Polycomb repressive complex 1 (PRC1) activity, aberrant
epigenetic regulation of gene expression and impaired
differentiation of mesenchimal progenitor cells.
{ECO:0000269|PubMed:27174990}.
-!- MISCELLANEOUS: This histone is only present in mammals and is
enriched in acetylation of Lys-15 and dimethylation of Lys-10
(H3K9me2).
-!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X00090; CAA24952.1; -; Genomic_DNA.
EMBL; M26150; AAA52651.1; -; Genomic_DNA.
EMBL; M60746; AAA63185.1; -; Genomic_DNA.
EMBL; X57128; CAA40407.1; -; Genomic_DNA.
EMBL; Z46261; CAA86403.1; -; Genomic_DNA.
EMBL; X83550; CAA58540.1; -; Genomic_DNA.
EMBL; Z80784; CAB02546.1; -; Genomic_DNA.
EMBL; Z80785; CAB02547.1; -; Genomic_DNA.
EMBL; Z80786; CAB02548.1; -; Genomic_DNA.
EMBL; Z83735; CAB06030.1; -; Genomic_DNA.
EMBL; Z83737; CAB06032.1; -; Genomic_DNA.
EMBL; AF531274; AAN10051.1; -; Genomic_DNA.
EMBL; AF531275; AAN10052.1; -; Genomic_DNA.
EMBL; AF531276; AAN10053.1; -; Genomic_DNA.
EMBL; AF531277; AAN10054.1; -; Genomic_DNA.
EMBL; AF531278; AAN10055.1; -; Genomic_DNA.
EMBL; AF531279; AAN10056.1; -; Genomic_DNA.
EMBL; AF531280; AAN10057.1; -; Genomic_DNA.
EMBL; AF531281; AAN10058.1; -; Genomic_DNA.
EMBL; AF531282; AAN10059.1; -; Genomic_DNA.
EMBL; AF531283; AAN10060.1; -; Genomic_DNA.
EMBL; AK311991; BAG34929.1; -; mRNA.
EMBL; AK313905; BAG36628.1; -; mRNA.
EMBL; AK314142; BAG36832.1; -; mRNA.
EMBL; AK316611; BAG38198.1; -; mRNA.
EMBL; CR542014; CAG46811.1; -; mRNA.
EMBL; CR542011; CAG46808.1; -; mRNA.
EMBL; CR541983; CAG46780.1; -; mRNA.
EMBL; CR541858; CAG46656.1; -; mRNA.
EMBL; Z98744; CAD24076.1; -; Genomic_DNA.
EMBL; Z98744; CAB11424.1; -; Genomic_DNA.
EMBL; AL009179; CAA15670.1; -; Genomic_DNA.
EMBL; AL031777; CAC03412.1; -; Genomic_DNA.
EMBL; AL031777; CAC03413.1; -; Genomic_DNA.
EMBL; AL031777; CAC03416.1; -; Genomic_DNA.
EMBL; AL031777; CAC03421.1; -; Genomic_DNA.
EMBL; BC031333; AAH31333.1; -; mRNA.
EMBL; BC066245; AAH66245.1; -; mRNA.
EMBL; BC066246; AAH66246.1; -; mRNA.
EMBL; BC066247; AAH66247.1; -; mRNA.
EMBL; BC066884; AAH66884.1; -; mRNA.
EMBL; BC067490; AAH67490.1; -; mRNA.
EMBL; BC067491; AAH67491.1; -; mRNA.
EMBL; BC067492; AAH67492.1; -; mRNA.
EMBL; BC067493; AAH67493.1; -; mRNA.
EMBL; BC069133; AAH69133.1; -; mRNA.
EMBL; BC069303; AAH69303.1; -; mRNA.
EMBL; BC069305; AAH69305.2; -; mRNA.
EMBL; BC069818; AAH69818.1; -; mRNA.
EMBL; BC096128; AAH96128.1; -; mRNA.
EMBL; BC096129; AAH96129.1; -; mRNA.
EMBL; BC096130; AAH96130.1; -; mRNA.
EMBL; BC096131; AAH96131.1; -; mRNA.
EMBL; BC096132; AAH96132.1; -; mRNA.
EMBL; BC096133; AAH96133.1; -; mRNA.
EMBL; BC096134; AAH96134.1; -; mRNA.
EMBL; BC099630; AAH99630.1; -; mRNA.
EMBL; BC127610; AAI27611.1; -; mRNA.
EMBL; BC143046; AAI43047.1; -; mRNA.
EMBL; BC148243; AAI48244.1; -; mRNA.
EMBL; BC148250; AAI48251.1; -; mRNA.
CCDS; CCDS4570.1; -.
CCDS; CCDS4573.1; -.
CCDS; CCDS4576.1; -.
CCDS; CCDS4590.1; -.
CCDS; CCDS4596.1; -.
CCDS; CCDS4600.1; -.
CCDS; CCDS4602.1; -.
CCDS; CCDS4627.1; -.
CCDS; CCDS4636.1; -.
CCDS; CCDS4638.1; -.
PIR; I37446; HSHU3.
RefSeq; NP_003520.1; NM_003529.2.
RefSeq; NP_003521.2; NM_003530.4.
RefSeq; NP_003522.1; NM_003531.2.
RefSeq; NP_003523.1; NM_003532.2.
RefSeq; NP_003524.1; NM_003533.2.
RefSeq; NP_003525.1; NM_003534.2.
RefSeq; NP_003526.1; NM_003535.2.
RefSeq; NP_003527.1; NM_003536.2.
RefSeq; NP_003528.1; NM_003537.3.
RefSeq; NP_066298.1; NM_021018.2.
UniGene; Hs.132854; -.
UniGene; Hs.247813; -.
UniGene; Hs.247814; -.
UniGene; Hs.248176; -.
UniGene; Hs.443021; -.
UniGene; Hs.484990; -.
UniGene; Hs.532144; -.
UniGene; Hs.533292; -.
UniGene; Hs.546315; -.
UniGene; Hs.586261; -.
UniGene; Hs.591778; -.
UniGene; Hs.626666; -.
PDB; 1CS9; NMR; -; A=131-136.
PDB; 1CT6; NMR; -; A=131-136.
PDB; 1O9S; X-ray; 1.75 A; K/L=2-10.
PDB; 1Q3L; X-ray; 1.64 A; P=2-16.
PDB; 2B2T; X-ray; 2.45 A; D=2-20.
PDB; 2B2U; X-ray; 2.95 A; D=2-16.
PDB; 2B2V; X-ray; 2.65 A; D=2-16.
PDB; 2B2W; X-ray; 2.40 A; D=2-20.
PDB; 2C1J; X-ray; 2.60 A; C/D=8-15.
PDB; 2C1N; X-ray; 2.00 A; C/E=8-15.
PDB; 2CO0; X-ray; 2.25 A; B/D=2-16.
PDB; 2CV5; X-ray; 2.50 A; A/E=1-136.
PDB; 2KWJ; NMR; -; B=2-21.
PDB; 2KWK; NMR; -; B=2-21.
PDB; 2L75; NMR; -; B=2-14.
PDB; 2LBM; NMR; -; C=2-16.
PDB; 2M0O; NMR; -; B=32-42.
PDB; 2NDF; NMR; -; B=13-25.
PDB; 2NDG; NMR; -; B=13-25.
PDB; 2OQ6; X-ray; 2.00 A; C/D=8-15.
PDB; 2OT7; X-ray; 2.14 A; C/D=8-15.
PDB; 2OX0; X-ray; 1.95 A; C/D=8-15.
PDB; 2RI7; X-ray; 1.45 A; P=2-10.
PDB; 2UXN; X-ray; 2.72 A; E=2-22.
PDB; 2V85; X-ray; 2.00 A; D/E=2-13.
PDB; 2V89; X-ray; 1.10 A; D/E=2-10.
PDB; 2VNF; X-ray; 1.76 A; B/D=2-11.
PDB; 2VPG; X-ray; 1.60 A; P/R=2-19.
PDB; 2X0L; X-ray; 3.00 A; C=6-17.
PDB; 3A1B; X-ray; 2.29 A; A=2-21.
PDB; 3AFA; X-ray; 2.50 A; A/E=1-136.
PDB; 3AVR; X-ray; 1.80 A; B=18-39.
PDB; 3AYW; X-ray; 2.90 A; A/E=1-136.
PDB; 3AZE; X-ray; 3.00 A; A/E=1-136.
PDB; 3AZF; X-ray; 2.70 A; A/E=1-136.
PDB; 3AZG; X-ray; 2.40 A; A/E=1-136.
PDB; 3AZH; X-ray; 3.49 A; A/E=1-136.
PDB; 3AZI; X-ray; 2.70 A; A/E=1-136.
PDB; 3AZJ; X-ray; 2.89 A; A/E=1-136.
PDB; 3AZK; X-ray; 3.20 A; A/E=1-136.
PDB; 3AZL; X-ray; 2.70 A; A/E=1-136.
PDB; 3AZM; X-ray; 2.89 A; A/E=1-136.
PDB; 3AZN; X-ray; 3.00 A; A/E=1-136.
PDB; 3B95; X-ray; 2.99 A; P=2-16.
PDB; 3KMT; X-ray; 1.78 A; G/H/I=26-33.
PDB; 3KQI; X-ray; 1.78 A; B=2-13.
PDB; 3LQI; X-ray; 1.92 A; R/S/T=2-10.
PDB; 3LQJ; X-ray; 1.90 A; Q/T=2-10.
PDB; 3MP1; X-ray; 2.60 A; P=2-6.
PDB; 3O34; X-ray; 1.90 A; B=14-33.
PDB; 3O35; X-ray; 1.76 A; D/E=24-32.
PDB; 3O37; X-ray; 2.00 A; E/F/G/H=2-11.
PDB; 3QJ6; X-ray; 2.30 A; T=74-84.
PDB; 3RIG; X-ray; 2.00 A; C/D=5-16.
PDB; 3RIY; X-ray; 1.55 A; C/D=5-16.
PDB; 3SOU; X-ray; 1.80 A; D/E=2-10.
PDB; 3SOW; X-ray; 1.95 A; C/D=2-10.
PDB; 3U31; X-ray; 2.20 A; B=5-14.
PDB; 3U3D; X-ray; 2.40 A; B=5-14.
PDB; 3U4S; X-ray; 2.15 A; C/D=8-15.
PDB; 3U5N; X-ray; 1.95 A; C/D=2-21.
PDB; 3U5O; X-ray; 2.70 A; I/J/K/L/M/N/O/P=2-23.
PDB; 3U5P; X-ray; 2.80 A; I/J/K/L/M/N/O/P=2-29.
PDB; 3UEE; X-ray; 2.61 A; B/D=2-13.
PDB; 3UEF; X-ray; 2.45 A; B/D=2-13.
PDB; 3UIG; X-ray; 2.40 A; P/Q=2-16.
PDB; 3UII; X-ray; 2.60 A; P/Q=2-11.
PDB; 3UIK; X-ray; 2.70 A; P/Q=2-11.
PDB; 3V43; X-ray; 1.47 A; Q=2-19.
PDB; 3W96; X-ray; 3.00 A; A/E=1-136.
PDB; 3W97; X-ray; 3.20 A; A/E=1-136.
PDB; 3W98; X-ray; 3.42 A; A/E=29-136.
PDB; 3W99; X-ray; 3.00 A; A/E=1-136.
PDB; 3WA9; X-ray; 3.07 A; A/E=1-136.
PDB; 3WAA; X-ray; 3.20 A; A/E=1-136.
PDB; 3WKJ; X-ray; 2.80 A; A/E=1-136.
PDB; 3X1S; X-ray; 2.81 A; A/E=2-136.
PDB; 3X1T; X-ray; 2.81 A; A/E=2-136.
PDB; 3X1U; X-ray; 3.25 A; A/E=2-136.
PDB; 3X1V; X-ray; 2.92 A; A/E=2-136.
PDB; 3ZG6; X-ray; 2.20 A; F=5-14.
PDB; 3ZVY; X-ray; 1.95 A; C/D=2-9.
PDB; 4A0J; X-ray; 2.80 A; C/D=2-7.
PDB; 4A0N; X-ray; 2.74 A; C=2-7.
PDB; 4A7J; X-ray; 1.90 A; B=1-16.
PDB; 4BD3; NMR; -; B=32-42.
PDB; 4C1Q; X-ray; 2.30 A; C=2-10.
PDB; 4F4U; X-ray; 2.00 A; C/D=5-16.
PDB; 4F56; X-ray; 1.70 A; C/D=5-16.
PDB; 4FWF; X-ray; 2.70 A; E=2-21.
PDB; 4HON; X-ray; 1.80 A; F/G=7-16.
PDB; 4I51; X-ray; 1.90 A; C/D=4-12.
PDB; 4L7X; X-ray; 1.35 A; U=2-13.
PDB; 4LK9; X-ray; 1.60 A; B=2-22.
PDB; 4LKA; X-ray; 1.61 A; B=2-22.
PDB; 4LLB; X-ray; 2.50 A; C/D=2-22.
PDB; 4LXL; X-ray; 1.87 A; D=8-15.
PDB; 4N4H; X-ray; 2.30 A; B=22-43.
PDB; 4QBQ; X-ray; 2.41 A; P=2-9.
PDB; 4QBR; X-ray; 1.90 A; E/P=2-8.
PDB; 4QBS; X-ray; 1.80 A; P=2-8.
PDB; 4TN7; X-ray; 2.20 A; E/F=30-44.
PDB; 4U68; X-ray; 1.80 A; D/E/F=5-15.
PDB; 4UP0; X-ray; 1.28 A; F=2-16.
PDB; 4UY4; X-ray; 1.86 A; C/D=2-7.
PDB; 4X3K; X-ray; 1.45 A; C/D=24-30.
PDB; 4Y6L; X-ray; 1.60 A; C/D=7-13.
PDB; 4YHP; X-ray; 2.53 A; P/Q=2-17.
PDB; 4YHZ; X-ray; 2.30 A; P=2-13.
PDB; 4YM5; X-ray; 4.00 A; A/E=1-136.
PDB; 4YM6; X-ray; 3.51 A; A/E=1-136.
PDB; 4Z0R; X-ray; 1.75 A; D=2-16.
PDB; 4Z2M; X-ray; 2.98 A; G/I=35-136.
PDB; 5AV5; X-ray; 2.40 A; A/E=1-136.
PDB; 5AV6; X-ray; 2.20 A; A/E=1-136.
PDB; 5AV8; X-ray; 2.20 A; A/E=1-136.
PDB; 5AV9; X-ray; 2.20 A; A/E=1-136.
PDB; 5AVB; X-ray; 2.40 A; A/E=1-136.
PDB; 5AVC; X-ray; 2.40 A; A/E=1-136.
PDB; 5B24; X-ray; 3.60 A; A/E=1-136.
PDB; 5B2I; X-ray; 3.00 A; A/E=1-136.
PDB; 5B2J; X-ray; 2.60 A; A/E=1-136.
PDB; 5B31; X-ray; 2.20 A; A/E=1-136.
PDB; 5C11; X-ray; 2.80 A; B=2-11.
PDB; 5C13; X-ray; 2.10 A; D/F/H/P=2-11.
PDB; 5C3I; X-ray; 3.50 A; B/F/J/N/R/V=1-136.
PDB; 5CPI; X-ray; 2.90 A; A/E=1-136.
PDB; 5CPJ; X-ray; 3.15 A; A/E=1-136.
PDB; 5CPK; X-ray; 2.63 A; A/E=1-136.
PDB; 5D6Y; X-ray; 2.29 A; a/b/c/d=20-29.
PDB; 5DAH; X-ray; 2.61 A; C/D=20-30.
PDB; 5FB0; X-ray; 2.70 A; D/F=2-16.
PDB; 5FB1; X-ray; 2.10 A; C=2-16.
PDB; 5FFV; X-ray; 1.30 A; C/D=10-20.
PDB; 5GSE; X-ray; 3.14 A; A/E/K/O=1-136.
PDB; 5GSU; X-ray; 3.10 A; A/E=2-136.
PDB; 5GT0; X-ray; 2.82 A; A/E=2-136.
PDB; 5GT3; X-ray; 2.91 A; A/E=2-136.
PDB; 5GTC; X-ray; 2.70 A; A/E=1-136.
PDB; 5H6Q; X-ray; 2.53 A; C=2-21.
PDB; 5H6R; X-ray; 2.60 A; C=2-21.
PDB; 5HJB; X-ray; 2.70 A; B=4-9.
PDB; 5HJC; X-ray; 2.60 A; B=16-24.
PDB; 5HJD; X-ray; 2.81 A; B/D/F/H/I/J/L/M=15-21.
PDB; 5HYN; X-ray; 2.95 A; D/I/O/T=22-34.
PDB; 5IQL; X-ray; 2.10 A; B=25-32.
PDB; 5J3V; X-ray; 3.05 A; C/D=12-28.
PDB; 5J9S; X-ray; 2.70 A; B=16-40.
PDB; 5JHN; X-ray; 1.67 A; F/G=4-14.
PDB; 5JIN; X-ray; 1.85 A; F/G=4-14.
PDB; 5JIY; X-ray; 1.48 A; F/G=4-14.
PDB; 5JJ0; X-ray; 1.72 A; F/G=4-14.
PDB; 5JRG; X-ray; 2.50 A; A/E=1-136.
PDB; 5KJH; X-ray; 2.27 A; D=23-33, E=19-38.
PDB; 5KJI; X-ray; 2.71 A; E=19-38.
PDB; 5KKL; X-ray; 2.94 A; B=23-27.
PDB; 5M5G; X-ray; 2.27 A; D=23-33.
PDB; 5SVX; X-ray; 1.56 A; B=2-12.
PDB; 5SVY; X-ray; 1.05 A; B=2-12.
PDB; 5T0K; X-ray; 1.70 A; P/Q=2-16.
PDB; 5T0M; X-ray; 1.90 A; C/P=2-16.
PDB; 5T1G; X-ray; 1.90 A; B=39-53.
PDB; 5T1I; X-ray; 1.60 A; C=39-53.
PDB; 5T8R; X-ray; 2.40 A; E/G=2-11.
PDB; 5TBN; NMR; -; C=2-12.
PDB; 5TDR; X-ray; 1.42 A; B=2-12.
PDB; 5TDW; X-ray; 1.70 A; B=2-12.
PDB; 5U2J; X-ray; 1.60 A; C/D=2-17.
PDB; 5V21; X-ray; 2.42 A; B=30-44.
PDB; 5V22; X-ray; 2.40 A; B=30-44.
PDB; 5VA6; X-ray; 2.40 A; C/D=20-37.
PDB; 5VAB; X-ray; 1.70 A; F=2-11.
PDB; 5VGE; X-ray; 2.60 A; C=41-49.
PDB; 5X60; X-ray; 2.69 A; C=2-21.
PDB; 5XFR; X-ray; 2.25 A; C/D=34-41.
PDBsum; 1CS9; -.
PDBsum; 1CT6; -.
PDBsum; 1O9S; -.
PDBsum; 1Q3L; -.
PDBsum; 2B2T; -.
PDBsum; 2B2U; -.
PDBsum; 2B2V; -.
PDBsum; 2B2W; -.
PDBsum; 2C1J; -.
PDBsum; 2C1N; -.
PDBsum; 2CO0; -.
PDBsum; 2CV5; -.
PDBsum; 2KWJ; -.
PDBsum; 2KWK; -.
PDBsum; 2L75; -.
PDBsum; 2LBM; -.
PDBsum; 2M0O; -.
PDBsum; 2NDF; -.
PDBsum; 2NDG; -.
PDBsum; 2OQ6; -.
PDBsum; 2OT7; -.
PDBsum; 2OX0; -.
PDBsum; 2RI7; -.
PDBsum; 2UXN; -.
PDBsum; 2V85; -.
PDBsum; 2V89; -.
PDBsum; 2VNF; -.
PDBsum; 2VPG; -.
PDBsum; 2X0L; -.
PDBsum; 3A1B; -.
PDBsum; 3AFA; -.
PDBsum; 3AVR; -.
PDBsum; 3AYW; -.
PDBsum; 3AZE; -.
PDBsum; 3AZF; -.
PDBsum; 3AZG; -.
PDBsum; 3AZH; -.
PDBsum; 3AZI; -.
PDBsum; 3AZJ; -.
PDBsum; 3AZK; -.
PDBsum; 3AZL; -.
PDBsum; 3AZM; -.
PDBsum; 3AZN; -.
PDBsum; 3B95; -.
PDBsum; 3KMT; -.
PDBsum; 3KQI; -.
PDBsum; 3LQI; -.
PDBsum; 3LQJ; -.
PDBsum; 3MP1; -.
PDBsum; 3O34; -.
PDBsum; 3O35; -.
PDBsum; 3O37; -.
PDBsum; 3QJ6; -.
PDBsum; 3RIG; -.
PDBsum; 3RIY; -.
PDBsum; 3SOU; -.
PDBsum; 3SOW; -.
PDBsum; 3U31; -.
PDBsum; 3U3D; -.
PDBsum; 3U4S; -.
PDBsum; 3U5N; -.
PDBsum; 3U5O; -.
PDBsum; 3U5P; -.
PDBsum; 3UEE; -.
PDBsum; 3UEF; -.
PDBsum; 3UIG; -.
PDBsum; 3UII; -.
PDBsum; 3UIK; -.
PDBsum; 3V43; -.
PDBsum; 3W96; -.
PDBsum; 3W97; -.
PDBsum; 3W98; -.
PDBsum; 3W99; -.
PDBsum; 3WA9; -.
PDBsum; 3WAA; -.
PDBsum; 3WKJ; -.
PDBsum; 3X1S; -.
PDBsum; 3X1T; -.
PDBsum; 3X1U; -.
PDBsum; 3X1V; -.
PDBsum; 3ZG6; -.
PDBsum; 3ZVY; -.
PDBsum; 4A0J; -.
PDBsum; 4A0N; -.
PDBsum; 4A7J; -.
PDBsum; 4BD3; -.
PDBsum; 4C1Q; -.
PDBsum; 4F4U; -.
PDBsum; 4F56; -.
PDBsum; 4FWF; -.
PDBsum; 4HON; -.
PDBsum; 4I51; -.
PDBsum; 4L7X; -.
PDBsum; 4LK9; -.
PDBsum; 4LKA; -.
PDBsum; 4LLB; -.
PDBsum; 4LXL; -.
PDBsum; 4N4H; -.
PDBsum; 4QBQ; -.
PDBsum; 4QBR; -.
PDBsum; 4QBS; -.
PDBsum; 4TN7; -.
PDBsum; 4U68; -.
PDBsum; 4UP0; -.
PDBsum; 4UY4; -.
PDBsum; 4X3K; -.
PDBsum; 4Y6L; -.
PDBsum; 4YHP; -.
PDBsum; 4YHZ; -.
PDBsum; 4YM5; -.
PDBsum; 4YM6; -.
PDBsum; 4Z0R; -.
PDBsum; 4Z2M; -.
PDBsum; 5AV5; -.
PDBsum; 5AV6; -.
PDBsum; 5AV8; -.
PDBsum; 5AV9; -.
PDBsum; 5AVB; -.
PDBsum; 5AVC; -.
PDBsum; 5B24; -.
PDBsum; 5B2I; -.
PDBsum; 5B2J; -.
PDBsum; 5B31; -.
PDBsum; 5C11; -.
PDBsum; 5C13; -.
PDBsum; 5C3I; -.
PDBsum; 5CPI; -.
PDBsum; 5CPJ; -.
PDBsum; 5CPK; -.
PDBsum; 5D6Y; -.
PDBsum; 5DAH; -.
PDBsum; 5FB0; -.
PDBsum; 5FB1; -.
PDBsum; 5FFV; -.
PDBsum; 5GSE; -.
PDBsum; 5GSU; -.
PDBsum; 5GT0; -.
PDBsum; 5GT3; -.
PDBsum; 5GTC; -.
PDBsum; 5H6Q; -.
PDBsum; 5H6R; -.
PDBsum; 5HJB; -.
PDBsum; 5HJC; -.
PDBsum; 5HJD; -.
PDBsum; 5HYN; -.
PDBsum; 5IQL; -.
PDBsum; 5J3V; -.
PDBsum; 5J9S; -.
PDBsum; 5JHN; -.
PDBsum; 5JIN; -.
PDBsum; 5JIY; -.
PDBsum; 5JJ0; -.
PDBsum; 5JRG; -.
PDBsum; 5KJH; -.
PDBsum; 5KJI; -.
PDBsum; 5KKL; -.
PDBsum; 5M5G; -.
PDBsum; 5SVX; -.
PDBsum; 5SVY; -.
PDBsum; 5T0K; -.
PDBsum; 5T0M; -.
PDBsum; 5T1G; -.
PDBsum; 5T1I; -.
PDBsum; 5T8R; -.
PDBsum; 5TBN; -.
PDBsum; 5TDR; -.
PDBsum; 5TDW; -.
PDBsum; 5U2J; -.
PDBsum; 5V21; -.
PDBsum; 5V22; -.
PDBsum; 5VA6; -.
PDBsum; 5VAB; -.
PDBsum; 5VGE; -.
PDBsum; 5X60; -.
PDBsum; 5XFR; -.
ProteinModelPortal; P68431; -.
SMR; P68431; -.
BioGrid; 113946; 290.
BioGrid; 113947; 5.
BioGrid; 113948; 10.
BioGrid; 113949; 200.
BioGrid; 113950; 5.
BioGrid; 113951; 6.
BioGrid; 113952; 4.
BioGrid; 113953; 8.
BioGrid; 113954; 23.
BioGrid; 114458; 8.
CORUM; P68431; -.
DIP; DIP-29371N; -.
ELM; P68431; -.
IntAct; P68431; 93.
MINT; MINT-256465; -.
STRING; 9606.ENSP00000444823; -.
iPTMnet; P68431; -.
PhosphoSitePlus; P68431; -.
SwissPalm; P68431; -.
BioMuta; HIST1H3A; -.
DMDM; 55977055; -.
EPD; P68431; -.
MaxQB; P68431; -.
PaxDb; P68431; -.
PeptideAtlas; P68431; -.
PRIDE; P68431; -.
TopDownProteomics; P68431; -.
DNASU; 8350; -.
DNASU; 8352; -.
DNASU; 8353; -.
DNASU; 8355; -.
DNASU; 8356; -.
DNASU; 8357; -.
Ensembl; ENST00000356476; ENSP00000366999; ENSG00000197409.
Ensembl; ENST00000359303; ENSP00000352252; ENSG00000197153.
Ensembl; ENST00000369163; ENSP00000358160; ENSG00000278828.
Ensembl; ENST00000612966; ENSP00000484658; ENSG00000278272.
Ensembl; ENST00000613854; ENSP00000480826; ENSG00000275714.
Ensembl; ENST00000614378; ENSP00000484638; ENSG00000273983.
Ensembl; ENST00000614911; ENSP00000482271; ENSG00000274750.
Ensembl; ENST00000616365; ENSP00000483283; ENSG00000275379.
Ensembl; ENST00000618052; ENSP00000484095; ENSG00000277775.
Ensembl; ENST00000621411; ENSP00000484841; ENSG00000274267.
Ensembl; ENST00000634733; ENSP00000489282; ENSG00000274750.
GeneID; 8350; -.
GeneID; 8351; -.
GeneID; 8352; -.
GeneID; 8353; -.
GeneID; 8354; -.
GeneID; 8355; -.
GeneID; 8356; -.
GeneID; 8357; -.
GeneID; 8358; -.
GeneID; 8968; -.
KEGG; hsa:8350; -.
KEGG; hsa:8351; -.
KEGG; hsa:8352; -.
KEGG; hsa:8353; -.
KEGG; hsa:8354; -.
KEGG; hsa:8355; -.
KEGG; hsa:8356; -.
KEGG; hsa:8357; -.
KEGG; hsa:8358; -.
KEGG; hsa:8968; -.
UCSC; uc003nfp.2; human.
CTD; 8350; -.
CTD; 8351; -.
CTD; 8352; -.
CTD; 8353; -.
CTD; 8354; -.
CTD; 8355; -.
CTD; 8356; -.
CTD; 8357; -.
CTD; 8358; -.
CTD; 8968; -.
DisGeNET; 8350; -.
DisGeNET; 8351; -.
DisGeNET; 8352; -.
DisGeNET; 8353; -.
DisGeNET; 8354; -.
DisGeNET; 8355; -.
DisGeNET; 8356; -.
DisGeNET; 8357; -.
DisGeNET; 8358; -.
DisGeNET; 8968; -.
EuPathDB; HostDB:ENSG00000197153.4; -.
EuPathDB; HostDB:ENSG00000197409.7; -.
EuPathDB; HostDB:ENSG00000273983.1; -.
EuPathDB; HostDB:ENSG00000274267.1; -.
EuPathDB; HostDB:ENSG00000274750.2; -.
EuPathDB; HostDB:ENSG00000275379.1; -.
EuPathDB; HostDB:ENSG00000275714.1; -.
EuPathDB; HostDB:ENSG00000277775.1; -.
EuPathDB; HostDB:ENSG00000278272.1; -.
EuPathDB; HostDB:ENSG00000278828.1; -.
GeneCards; HIST1H3A; -.
GeneCards; HIST1H3B; -.
GeneCards; HIST1H3C; -.
GeneCards; HIST1H3D; -.
GeneCards; HIST1H3E; -.
GeneCards; HIST1H3F; -.
GeneCards; HIST1H3G; -.
GeneCards; HIST1H3H; -.
GeneCards; HIST1H3I; -.
GeneCards; HIST1H3J; -.
HGNC; HGNC:4766; HIST1H3A.
HGNC; HGNC:4776; HIST1H3B.
HGNC; HGNC:4768; HIST1H3C.
HGNC; HGNC:4767; HIST1H3D.
HGNC; HGNC:4769; HIST1H3E.
HGNC; HGNC:4773; HIST1H3F.
HGNC; HGNC:4772; HIST1H3G.
HGNC; HGNC:4775; HIST1H3H.
HGNC; HGNC:4771; HIST1H3I.
HGNC; HGNC:4774; HIST1H3J.
HPA; CAB070190; -.
HPA; HPA042570; -.
MIM; 137800; phenotype.
MIM; 602810; gene.
MIM; 602811; gene.
MIM; 602812; gene.
MIM; 602813; gene.
MIM; 602814; gene.
MIM; 602815; gene.
MIM; 602816; gene.
MIM; 602817; gene.
MIM; 602818; gene.
MIM; 602819; gene.
neXtProt; NX_P68431; -.
OpenTargets; ENSG00000197153; -.
OpenTargets; ENSG00000197409; -.
OpenTargets; ENSG00000273983; -.
OpenTargets; ENSG00000274267; -.
OpenTargets; ENSG00000274750; -.
OpenTargets; ENSG00000275379; -.
OpenTargets; ENSG00000275714; -.
OpenTargets; ENSG00000277775; -.
OpenTargets; ENSG00000278272; -.
OpenTargets; ENSG00000278828; -.
PharmGKB; PA29148; -.
eggNOG; KOG1745; Eukaryota.
eggNOG; COG2036; LUCA.
GeneTree; ENSGT00760000118967; -.
HOVERGEN; HBG001172; -.
InParanoid; P68431; -.
KO; K11253; -.
OMA; ASEAYYL; -.
OrthoDB; EOG09370ZG5; -.
PhylomeDB; P68431; -.
TreeFam; TF314241; -.
Reactome; R-HSA-1266695; Interleukin-7 signaling.
Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
Reactome; R-HSA-212300; PRC2 methylates histones and DNA.
Reactome; R-HSA-2299718; Condensation of Prophase Chromosomes.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-HSA-3214815; HDACs deacetylate histones.
Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
Reactome; R-HSA-3214842; HDMs demethylate histones.
Reactome; R-HSA-3214847; HATs acetylate histones.
Reactome; R-HSA-3214858; RMTs methylate histone arginines.
Reactome; R-HSA-3247509; Chromatin modifying enzymes.
Reactome; R-HSA-427359; SIRT1 negatively regulates rRNA Expression.
Reactome; R-HSA-427389; ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression.
Reactome; R-HSA-5334118; DNA methylation.
Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs.
Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
Reactome; R-HSA-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
Reactome; R-HSA-73728; RNA Polymerase I Promoter Opening.
Reactome; R-HSA-73777; RNA Polymerase I Chain Elongation.
Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
Reactome; R-HSA-912446; Meiotic recombination.
Reactome; R-HSA-977225; Amyloid fiber formation.
Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
SIGNOR; P68431; -.
ChiTaRS; HIST1H3B; human.
ChiTaRS; HIST1H3F; human.
EvolutionaryTrace; P68431; -.
GeneWiki; HIST1H3A; -.
GeneWiki; HIST1H3B; -.
GeneWiki; HIST1H3C; -.
GeneWiki; HIST1H3D; -.
GeneWiki; HIST1H3E; -.
GeneWiki; HIST1H3F; -.
GeneWiki; HIST1H3G; -.
GeneWiki; HIST1H3H; -.
GeneWiki; HIST1H3I; -.
GeneWiki; HIST1H3J; -.
PRO; PR:P68431; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000197153; -.
CleanEx; HS_HIST1H3A; -.
CleanEx; HS_HIST1H3B; -.
CleanEx; HS_HIST1H3C; -.
CleanEx; HS_HIST1H3D; -.
CleanEx; HS_HIST1H3E; -.
CleanEx; HS_HIST1H3F; -.
CleanEx; HS_HIST1H3G; -.
CleanEx; HS_HIST1H3H; -.
CleanEx; HS_HIST1H3I; -.
Genevisible; P68431; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0000228; C:nuclear chromosome; IDA:UniProtKB.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IDA:BHF-UCL.
GO; GO:0000788; C:nuclear nucleosome; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0000786; C:nucleosome; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0042393; F:histone binding; IPI:UniProtKB.
GO; GO:0031492; F:nucleosomal DNA binding; IBA:GO_Central.
GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
GO; GO:0007596; P:blood coagulation; TAS:Reactome.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0006325; P:chromatin organization; TAS:Reactome.
GO; GO:0000183; P:chromatin silencing at rDNA; TAS:Reactome.
GO; GO:0006335; P:DNA replication-dependent nucleosome assembly; IDA:UniProtKB.
GO; GO:0038111; P:interleukin-7-mediated signaling pathway; TAS:Reactome.
GO; GO:0045814; P:negative regulation of gene expression, epigenetic; TAS:Reactome.
GO; GO:0006334; P:nucleosome assembly; IDA:UniProtKB.
GO; GO:0045815; P:positive regulation of gene expression, epigenetic; TAS:Reactome.
GO; GO:0051290; P:protein heterotetramerization; IDA:UniProtKB.
GO; GO:0060968; P:regulation of gene silencing; IDA:BHF-UCL.
GO; GO:0060964; P:regulation of gene silencing by miRNA; TAS:Reactome.
GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; TAS:Reactome.
GO; GO:0045652; P:regulation of megakaryocyte differentiation; TAS:Reactome.
GO; GO:0032200; P:telomere organization; TAS:BHF-UCL.
InterPro; IPR009072; Histone-fold.
InterPro; IPR007125; Histone_H2A/H2B/H3.
InterPro; IPR000164; Histone_H3/CENP-A.
PANTHER; PTHR11426; PTHR11426; 1.
Pfam; PF00125; Histone; 1.
PRINTS; PR00622; HISTONEH3.
SMART; SM00428; H3; 1.
SUPFAM; SSF47113; SSF47113; 1.
PROSITE; PS00322; HISTONE_H3_1; 1.
PROSITE; PS00959; HISTONE_H3_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ADP-ribosylation; Chromosome;
Citrullination; Complete proteome; Direct protein sequencing;
Disease mutation; DNA-binding; Hydroxylation; Methylation;
Nucleosome core; Nucleus; Phosphoprotein; Reference proteome;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:16185088}.
CHAIN 2 136 Histone H3.1.
/FTId=PRO_0000221245.
MOD_RES 3 3 Asymmetric dimethylarginine; by PRMT6;
alternate. {ECO:0000269|PubMed:17898714,
ECO:0000269|PubMed:18077460,
ECO:0000269|PubMed:18079182}.
MOD_RES 3 3 Citrulline; alternate.
{ECO:0000269|PubMed:16567635}.
MOD_RES 4 4 Phosphothreonine; by HASPIN.
{ECO:0000269|PubMed:15681610,
ECO:0000269|PubMed:16185088}.
MOD_RES 5 5 Allysine; alternate.
{ECO:0000269|PubMed:22483618}.
MOD_RES 5 5 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000269|PubMed:16267050,
ECO:0000269|PubMed:16457588,
ECO:0000269|PubMed:17194708}.
MOD_RES 5 5 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:16267050,
ECO:0000269|PubMed:16457588,
ECO:0000269|PubMed:17194708}.
MOD_RES 5 5 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 5 5 N6-(beta-hydroxybutyryl)lysine;
alternate. {ECO:0000269|PubMed:27105115}.
MOD_RES 5 5 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:17194708}.
MOD_RES 5 5 N6-crotonyllysine; alternate.
{ECO:0000269|PubMed:21925322}.
MOD_RES 5 5 N6-methyllysine; alternate.
{ECO:0000269|PubMed:16267050,
ECO:0000269|PubMed:16457588,
ECO:0000269|PubMed:17194708}.
MOD_RES 7 7 Phosphothreonine; by PKC.
{ECO:0000269|PubMed:20228790}.
MOD_RES 9 9 Citrulline; alternate.
{ECO:0000269|PubMed:15345777,
ECO:0000269|PubMed:16567635}.
MOD_RES 9 9 Symmetric dimethylarginine; by PRMT5;
alternate.
{ECO:0000250|UniProtKB:P68433}.
MOD_RES 10 10 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000269|PubMed:11242053,
ECO:0000269|PubMed:16185088,
ECO:0000269|PubMed:16267050,
ECO:0000269|PubMed:16457588,
ECO:0000269|PubMed:17194708}.
MOD_RES 10 10 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:11242053,
ECO:0000269|PubMed:16185088,
ECO:0000269|PubMed:16267050,
ECO:0000269|PubMed:16457588,
ECO:0000269|PubMed:17194708}.
MOD_RES 10 10 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 10 10 N6-(beta-hydroxybutyryl)lysine;
alternate. {ECO:0000269|PubMed:27105115}.
MOD_RES 10 10 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:16185088,
ECO:0000269|PubMed:16267050,
ECO:0000269|PubMed:16457588,
ECO:0000269|PubMed:16497732,
ECO:0000269|PubMed:16627869,
ECO:0000269|PubMed:17194708}.
MOD_RES 10 10 N6-butyryllysine; alternate.
{ECO:0000269|PubMed:27105113}.
MOD_RES 10 10 N6-crotonyllysine; alternate.
{ECO:0000269|PubMed:21925322}.
MOD_RES 10 10 N6-methyllysine; alternate.
{ECO:0000269|PubMed:11242053,
ECO:0000269|PubMed:16185088,
ECO:0000269|PubMed:16267050,
ECO:0000269|PubMed:16457588,
ECO:0000269|PubMed:17194708}.
MOD_RES 11 11 ADP-ribosylserine; alternate.
{ECO:0000269|PubMed:28190768}.
MOD_RES 11 11 Phosphoserine; alternate; by AURKB,
AURKC, RPS6KA3, RPS6KA4 and RPS6KA5.
{ECO:0000269|PubMed:10464286,
ECO:0000269|PubMed:11856369,
ECO:0000269|PubMed:12560483,
ECO:0000269|PubMed:15681610,
ECO:0000269|PubMed:16185088,
ECO:0000269|PubMed:16457588}.
MOD_RES 12 12 Phosphothreonine; by PKC and CHEK1.
{ECO:0000269|PubMed:12560483,
ECO:0000269|PubMed:18066052,
ECO:0000269|PubMed:18243098}.
MOD_RES 15 15 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 15 15 N6-(beta-hydroxybutyryl)lysine;
alternate. {ECO:0000269|PubMed:27105115}.
MOD_RES 15 15 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:16185088,
ECO:0000269|PubMed:16267050,
ECO:0000269|PubMed:16457588,
ECO:0000269|PubMed:16497732,
ECO:0000269|PubMed:16627869,
ECO:0000269|PubMed:17194708}.
MOD_RES 15 15 N6-succinyllysine; alternate.
{ECO:0000269|PubMed:22389435}.
MOD_RES 18 18 Asymmetric dimethylarginine; by CARM1;
alternate. {ECO:0000269|PubMed:15345777,
ECO:0000269|PubMed:15471871,
ECO:0000269|PubMed:16497732}.
MOD_RES 18 18 Citrulline; alternate.
{ECO:0000269|PubMed:15345777,
ECO:0000269|PubMed:16497732,
ECO:0000269|PubMed:16567635}.
MOD_RES 19 19 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 19 19 N6-(beta-hydroxybutyryl)lysine;
alternate. {ECO:0000269|PubMed:27105115}.
MOD_RES 19 19 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:16267050,
ECO:0000269|PubMed:16627869,
ECO:0000269|PubMed:17194708}.
MOD_RES 19 19 N6-butyryllysine; alternate.
{ECO:0000269|PubMed:27105113}.
MOD_RES 19 19 N6-crotonyllysine; alternate.
{ECO:0000269|PubMed:21925322}.
MOD_RES 19 19 N6-methyllysine; alternate.
{ECO:0000269|PubMed:16267050,
ECO:0000269|PubMed:17194708}.
MOD_RES 24 24 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 24 24 N6-(beta-hydroxybutyryl)lysine;
alternate. {ECO:0000269|PubMed:27105115}.
MOD_RES 24 24 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:16267050,
ECO:0000269|PubMed:16457588,
ECO:0000269|PubMed:16627869,
ECO:0000269|PubMed:17194708}.
MOD_RES 24 24 N6-butyryllysine; alternate.
{ECO:0000269|PubMed:27105113}.
MOD_RES 24 24 N6-crotonyllysine; alternate.
{ECO:0000269|PubMed:21925322}.
MOD_RES 24 24 N6-methyllysine; alternate.
{ECO:0000269|PubMed:17194708}.
MOD_RES 27 27 Citrulline.
{ECO:0000269|PubMed:16567635}.
MOD_RES 28 28 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000269|PubMed:16185088,
ECO:0000269|PubMed:16267050,
ECO:0000269|PubMed:16627869,
ECO:0000269|PubMed:17194708}.
MOD_RES 28 28 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:16185088,
ECO:0000269|PubMed:16267050,
ECO:0000269|PubMed:16627869,
ECO:0000269|PubMed:17194708}.
MOD_RES 28 28 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 28 28 N6-(beta-hydroxybutyryl)lysine;
alternate. {ECO:0000269|PubMed:27105115}.
MOD_RES 28 28 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:16627869,
ECO:0000269|PubMed:17194708}.
MOD_RES 28 28 N6-crotonyllysine; alternate.
{ECO:0000269|PubMed:21925322}.
MOD_RES 28 28 N6-methyllysine; alternate.
{ECO:0000269|PubMed:16185088,
ECO:0000269|PubMed:16267050,
ECO:0000269|PubMed:16627869,
ECO:0000269|PubMed:17194708}.
MOD_RES 29 29 ADP-ribosylserine; alternate.
{ECO:0000269|PubMed:28190768}.
MOD_RES 29 29 Phosphoserine; alternate; by AURKB, AURKC
and RPS6KA5.
{ECO:0000269|PubMed:10464286,
ECO:0000269|PubMed:11856369,
ECO:0000269|PubMed:15681610,
ECO:0000269|PubMed:15684425,
ECO:0000269|PubMed:16185088,
ECO:0000269|PubMed:16457588}.
MOD_RES 37 37 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000269|PubMed:15983376,
ECO:0000269|PubMed:16185088,
ECO:0000269|PubMed:16267050,
ECO:0000269|PubMed:16627869,
ECO:0000269|PubMed:17194708}.
MOD_RES 37 37 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:15983376,
ECO:0000269|PubMed:16185088,
ECO:0000269|PubMed:16267050,
ECO:0000269|PubMed:16627869,
ECO:0000269|PubMed:17194708}.
MOD_RES 37 37 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 37 37 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:17189264,
ECO:0000269|PubMed:17194708}.
MOD_RES 37 37 N6-methyllysine; alternate.
{ECO:0000269|PubMed:15983376,
ECO:0000269|PubMed:16185088,
ECO:0000269|PubMed:16267050,
ECO:0000269|PubMed:16627869,
ECO:0000269|PubMed:17194708}.
MOD_RES 38 38 N6-methyllysine.
{ECO:0000269|PubMed:15983376}.
MOD_RES 42 42 Phosphotyrosine.
{ECO:0000269|PubMed:19783980}.
MOD_RES 57 57 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000269|PubMed:17194708,
ECO:0000269|PubMed:22387026}.
MOD_RES 57 57 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 57 57 N6-(beta-hydroxybutyryl)lysine;
alternate. {ECO:0000269|PubMed:27105115}.
MOD_RES 57 57 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:17194708}.
MOD_RES 57 57 N6-crotonyllysine; alternate.
{ECO:0000269|PubMed:21925322}.
MOD_RES 57 57 N6-methyllysine; by EHMT2; alternate.
{ECO:0000269|PubMed:17194708,
ECO:0000269|PubMed:22387026}.
MOD_RES 57 57 N6-succinyllysine; alternate.
{ECO:0000269|PubMed:22389435}.
MOD_RES 58 58 Phosphoserine.
{ECO:0000269|PubMed:20850016}.
MOD_RES 65 65 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 65 65 N6-methyllysine; alternate.
{ECO:0000269|PubMed:16267050,
ECO:0000269|PubMed:17194708}.
MOD_RES 80 80 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000250|UniProtKB:P68433}.
MOD_RES 80 80 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:15525939,
ECO:0000269|PubMed:16267050,
ECO:0000269|PubMed:16627869,
ECO:0000269|PubMed:17194708}.
MOD_RES 80 80 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 80 80 N6-(beta-hydroxybutyryl)lysine;
alternate. {ECO:0000269|PubMed:27105115}.
MOD_RES 80 80 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:17194708}.
MOD_RES 80 80 N6-methyllysine; alternate.
{ECO:0000269|PubMed:15525939,
ECO:0000269|PubMed:16267050,
ECO:0000269|PubMed:16627869,
ECO:0000269|PubMed:17194708}.
MOD_RES 80 80 N6-succinyllysine; alternate.
{ECO:0000269|PubMed:22389435}.
MOD_RES 81 81 Phosphothreonine.
{ECO:0000269|PubMed:20850016}.
MOD_RES 87 87 Phosphoserine.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 108 108 Phosphothreonine.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 116 116 N6-acetyllysine.
{ECO:0000269|PubMed:19520870}.
MOD_RES 123 123 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 123 123 N6-(beta-hydroxybutyryl)lysine;
alternate. {ECO:0000269|PubMed:27105115}.
MOD_RES 123 123 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:19520870,
ECO:0000269|PubMed:23415232}.
MOD_RES 123 123 N6-methyllysine; alternate.
{ECO:0000269|PubMed:16267050,
ECO:0000269|PubMed:17194708}.
MOD_RES 123 123 N6-succinyllysine; alternate.
{ECO:0000269|PubMed:22389435}.
VARIANT 28 28 K -> M (in GLM; non-brain stem pediatric
glioblastoma and diffuse intrinsic
pontine glioma; somatic mutation; results
in a global decrease of H3K27me3 levels).
{ECO:0000269|PubMed:22286216,
ECO:0000269|PubMed:23603901}.
/FTId=VAR_079018.
VARIANT 37 37 K -> I (probable disease-associated
mutation found in pediatric
undifferentiated soft tissue sarcoma
samples; somatic mutation; results in
global decrease of H3K36me2 and H3K36me3
levels and increased H3K27me3 levels).
{ECO:0000269|PubMed:27174990}.
/FTId=VAR_079019.
VARIANT 37 37 K -> M (probable disease-associated
mutation found in pediatric
undifferentiated soft tissue sarcoma
samples; somatic mutation; also found in
a subset of human papillomavirus-negative
head and neck squamous cell carcinomas;
results in global decrease of H3K36me2
and H3K36me3 levels and increased
H3K27me3 levels).
{ECO:0000269|PubMed:27174990,
ECO:0000269|PubMed:28067913}.
/FTId=VAR_079020.
CONFLICT 70 70 R -> C (in Ref. 13; AAH67493).
{ECO:0000305}.
CONFLICT 100 100 Y -> T (in Ref. 7; CAB02546).
{ECO:0000305}.
CONFLICT 122 122 P -> L (in Ref. 13; AAH66884).
{ECO:0000305}.
CONFLICT 135 135 Missing (in Ref. 2; AAA52651).
{ECO:0000305}.
STRAND 4 7 {ECO:0000244|PDB:5SVY}.
HELIX 13 15 {ECO:0000244|PDB:3U5N}.
STRAND 25 27 {ECO:0000244|PDB:4X3K}.
STRAND 45 49 {ECO:0000244|PDB:5T1I}.
HELIX 50 58 {ECO:0000244|PDB:5C3I}.
HELIX 65 77 {ECO:0000244|PDB:5AV6}.
STRAND 80 82 {ECO:0000244|PDB:5AV6}.
HELIX 87 114 {ECO:0000244|PDB:5AV6}.
STRAND 118 120 {ECO:0000244|PDB:5AV6}.
HELIX 122 132 {ECO:0000244|PDB:5AV6}.
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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