H33_HUMAN
ID H33_HUMAN Reviewed; 136 AA.
AC P84243; P06351; P33155; Q5VV55; Q5VV56; Q66I33; Q9V3W4;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Histone H3.3;
GN Name=H3-3A {ECO:0000312|HGNC:HGNC:4764}; Synonyms=H3.3A, H3F3, H3F3A;
GN ORFNames=PP781;
GN and
GN Name=H3-3B {ECO:0000312|HGNC:HGNC:4765}; Synonyms=H3.3B, H3F3B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (H3-3A).
RC TISSUE=Fibroblast;
RX PubMed=2859593; DOI=10.1073/pnas.82.9.2834;
RA Wells D., Kedes L.;
RT "Structure of a human histone cDNA: evidence that basally expressed histone
RT genes have intervening sequences and encode polyadenylylated mRNAs.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:2834-2838(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (H3-3A).
RX PubMed=3031613; DOI=10.1093/nar/15.7.2871;
RA Wells D., Hoffman D., Kedes L.;
RT "Unusual structure, evolutionary conservation of non-coding sequences and
RT numerous pseudogenes characterize the human H3.3 histone multigene
RT family.";
RL Nucleic Acids Res. 15:2871-2889(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (H3-3B).
RC TISSUE=Testis;
RX PubMed=8586426; DOI=10.1006/geno.1995.9878;
RA Albig W., Bramlage B., Gruber K., Klobeck H.-G., Kunz J., Doenecke D.;
RT "The human replacement histone H3.3B gene (H3F3B).";
RL Genomics 30:264-272(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (H3-3B).
RC TISSUE=Retina;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (H3-3A AND H3-3B).
RC TISSUE=Bone marrow, Brain, Colon, Eye, Lung, Muscle, Spinal cord, Testis,
RC and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PARTIAL PROTEIN SEQUENCE, METHYLATION AT LYS-10; LYS-28 AND LYS-37, AND
RP ACETYLATION AT LYS-15 AND LYS-24.
RX PubMed=7309716; DOI=10.1093/oxfordjournals.jbchem.a133573;
RA Ohe Y., Iwai K.;
RT "Human spleen histone H3. Isolation and amino acid sequence.";
RL J. Biochem. 90:1205-1211(1981).
RN [9]
RP PROTEIN SEQUENCE OF 28-41, METHYLATION AT LYS-5; LYS-10; LYS-28 AND LYS-37,
RP PHOSPHORYLATION AT THR-4; SER-11; SER-29 AND SER-32, ACETYLATION AT LYS-10
RP AND 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 [10]
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., Okawa K.,
RA Iwamatsu A., Okigaki T., Takahashi T., Inagaki M.;
RT "Identification of a novel phosphorylation site on histone H3 coupled with
RT mitotic chromosome condensation.";
RL J. Biol. Chem. 274:25543-25549(1999).
RN [11]
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 [12]
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 mitotic
RT chromosome condensation.";
RL Genes Cells 7:11-17(2002).
RN [13]
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 mediated by
RT Dlk/ZIP kinase.";
RL Nucleic Acids Res. 31:878-885(2003).
RN [14]
RP FUNCTION, AND INTERACTION WITH HIRA.
RX PubMed=14718166; DOI=10.1016/s0092-8674(03)01064-x;
RA Tagami H., Ray-Gallet D., Almouzni G., Nakatani Y.;
RT "Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways
RT dependent or independent of DNA synthesis.";
RL Cell 116:51-61(2004).
RN [15]
RP METHYLATION AT ARG-18.
RX PubMed=15471871; DOI=10.1074/jbc.m410021200;
RA Ananthanarayanan M., Li S., Balasubramaniyan N., Suchy F.J., Walsh M.J.;
RT "Ligand-dependent activation of the farnesoid X-receptor directs arginine
RT methylation of histone H3 by CARM1.";
RL J. Biol. Chem. 279:54348-54357(2004).
RN [16]
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., 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 [17]
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., Clarke S.,
RA 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 [18]
RP FUNCTION.
RX PubMed=15776021; DOI=10.1038/sj.embor.7400366;
RA Chow C.-M., Georgiou A., Szutorisz H., Maia e Silva A., Pombo A.,
RA Barahona I., Dargelos E., Canzonetta C., Dillon N.;
RT "Variant histone H3.3 marks promoters of transcriptionally active genes
RT during mammalian cell division.";
RL EMBO Rep. 6:354-360(2005).
RN [19]
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 phosphorylation
RT and normal metaphase chromosome alignment.";
RL Genes Dev. 19:472-488(2005).
RN [20]
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 kinase-
RT like mitogen-activated protein triple kinase alpha.";
RL J. Biol. Chem. 280:13545-13553(2005).
RN [21]
RP PHOSPHORYLATION AT SER-11; SER-29 AND SER-32, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15851689; DOI=10.1073/pnas.0502413102;
RA Hake S.B., Garcia B.A., Kauer M., Baker S.P., Shabanowitz J., Hunt D.F.,
RA Allis C.D.;
RT "Serine 31 phosphorylation of histone variant H3.3 is specific to regions
RT bordering centromeres in metaphase chromosomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:6344-6349(2005).
RN [22]
RP FUNCTION.
RX PubMed=16258499; DOI=10.1038/sj.embor.7400561;
RA Daury L., Chailleux C., Bonvallet J., Trouche D.;
RT "Histone H3.3 deposition at E2F-regulated genes is linked to
RT transcription.";
RL EMBO Rep. 7:66-71(2006).
RN [23]
RP ACETYLATION AT LYS-10; LYS-15; LYS-19; LYS-24 AND LYS-28, 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., Shabanowitz J.,
RA Bazett-Jones D.P., Allis C.D., Hunt D.F.;
RT "Expression patterns and post-translational modifications associated with
RT mammalian histone H3 variants.";
RL J. Biol. Chem. 281:559-568(2006).
RN [24]
RP METHYLATION AT LYS-5 AND LYS-10, ACETYLATION AT LYS-10, AND IDENTIFICATION
RP BY 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 [25]
RP ACETYLATION AT LYS-10 AND LYS-15, METHYLATION AT ARG-18, AND CITRULLINATION
RP 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 histone H3
RT at arginine 17.";
RL Mol. Endocrinol. 20:1562-1573(2006).
RN [26]
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., Hsieh J.,
RA 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 [27]
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 [28]
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; LYS-28;
RP LYS-37; LYS-57; LYS-65; LYS-80 AND LYS-123, AND IDENTIFICATION BY MASS
RP 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 histones H3
RT and H4.";
RL J. Biol. Chem. 282:7641-7655(2007).
RN [29]
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., Shabanowitz J.,
RA Hunt D.F., Allis C.D., Lieb J.D., Strahl B.D.;
RT "Identification of histone H3 lysine 36 acetylation as a highly conserved
RT histone modification.";
RL J. Biol. Chem. 282:7632-7640(2007).
RN [30]
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 [31]
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., Richard S.,
RA Bedford M.T.;
RT "Arginine methylation of the histone H3 tail impedes effector binding.";
RL J. Biol. Chem. 283:3006-3010(2008).
RN [32]
RP PHOSPHORYLATION AT THR-12.
RX PubMed=18066052; DOI=10.1038/ncb1668;
RA Metzger E., Yin N., Wissmann M., Kunowska N., Fischer K., Friedrichs N.,
RA Patnaik D., Higgins J.M., Potier N., Scheidtmann K.H., Buettner R.,
RA 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 [33]
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., Edon A.,
RA 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 [34]
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 chromatin.";
RL Nature 461:819-822(2009).
RN [35]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [36]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-28, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [37]
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., Butter F.,
RA Lee K.K., Olsen J.V., Hyman A.A., Stunnenberg H.G., 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 [38]
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 at
RT histone H3K4.";
RL Nature 464:792-796(2010).
RN [39]
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., Wysocka J.,
RA Ye Y., Khochbin S., Ren B., Zhao Y.;
RT "Identification of 67 histone marks and histone lysine crotonylation as a
RT new type of histone modification.";
RL Cell 146:1016-1028(2011).
RN [40]
RP PHOSPHORYLATION AT THR-12.
RX PubMed=22901803; DOI=10.1016/j.cell.2012.07.018;
RA Yang W., Xia Y., Hawke D., Li X., Liang J., Xing D., Aldape K., Hunter T.,
RA Alfred Yung W.K., Lu Z.;
RT "PKM2 phosphorylates histone H3 and promotes gene transcription and
RT tumorigenesis.";
RL Cell 150:685-696(2012).
RN [41]
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., Carey M.F.,
RA Grunstein M.;
RT "Histone H3 lysine 56 methylation regulates DNA replication through its
RT interaction with PCNA.";
RL Mol. Cell 46:7-17(2012).
RN [42]
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 [43]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [44]
RP METHYLATION [LARGE SCALE ANALYSIS] AT LYS-28, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [45]
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., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [46]
RP RETRACTION NOTICE OF PUBMED:25944712.
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 [47]
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 [48]
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., Downing J.R.,
RA 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 [49]
RP INVOLVEMENT IN GLM, AND VARIANTS GLM MET-28; ARG-35 AND VAL-35.
RX PubMed=22286061; DOI=10.1038/nature10833;
RA Schwartzentruber J., Korshunov A., Liu X.Y., Jones D.T., Pfaff E.,
RA Jacob K., Sturm D., Fontebasso A.M., Quang D.A., Toenjes M., Hovestadt V.,
RA Albrecht S., Kool M., Nantel A., Konermann C., Lindroth A., Jaeger N.,
RA Rausch T., Ryzhova M., Korbel J.O., Hielscher T., Hauser P., Garami M.,
RA Klekner A., Bognar L., Ebinger M., Schuhmann M.U., Scheurlen W., Pekrun A.,
RA Fruehwald M.C., Roggendorf W., Kramm C., Duerken M., Atkinson J.,
RA Lepage P., Montpetit A., Zakrzewska M., Zakrzewski K., Liberski P.P.,
RA Dong Z., Siegel P., Kulozik A.E., Zapatka M., Guha A., Malkin D.,
RA Felsberg J., Reifenberger G., von Deimling A., Ichimura K., Collins V.P.,
RA Witt H., Milde T., Witt O., Zhang C., Castelo-Branco P., Lichter P.,
RA Faury D., Tabori U., Plass C., Majewski J., Pfister S.M., Jabado N.;
RT "Driver mutations in histone H3.3 and chromatin remodelling genes in
RT paediatric glioblastoma.";
RL Nature 482:226-231(2012).
RN [50]
RP INVOLVEMENT IN GLM, AND CHARACTERIZATION OF VARIANT GLM VAL-35.
RX PubMed=23539269; DOI=10.1158/2159-8290.cd-12-0426;
RA Bjerke L., Mackay A., Nandhabalan M., Burford A., Jury A., Popov S.,
RA Bax D.A., Carvalho D., Taylor K.R., Vinci M., Bajrami I., McGonnell I.M.,
RA Lord C.J., Reis R.M., Hargrave D., Ashworth A., Workman P., Jones C.;
RT "Histone H3.3. mutations drive pediatric glioblastoma through upregulation
RT of MYCN.";
RL Cancer Discov. 3:512-519(2013).
RN [51]
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 lateral
RT surface of the histone octamer.";
RL Cell 152:859-872(2013).
RN [52]
RP INVOLVEMENT IN BONE AND CARTILAGE NEOPLASMS, AND VARIANTS TRP-35 AND
RP MET-37.
RX PubMed=24162739; DOI=10.1038/ng.2814;
RA Behjati S., Tarpey P.S., Presneau N., Scheipl S., Pillay N., Van Loo P.,
RA Wedge D.C., Cooke S.L., Gundem G., Davies H., Nik-Zainal S., Martin S.,
RA McLaren S., Goodie V., Robinson B., Butler A., Teague J.W., Halai D.,
RA Khatri B., Myklebost O., Baumhoer D., Jundt G., Hamoudi R., Tirabosco R.,
RA Amary M.F., Futreal P.A., Stratton M.R., Campbell P.J., Flanagan A.M.;
RT "Distinct H3F3A and H3F3B driver mutations define chondroblastoma and giant
RT cell tumor of bone.";
RL Nat. Genet. 45:1479-1482(2013).
RN [53]
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., Debernardi A.,
RA Buchou T., Rousseaux S., Jin F., Sabari B.R., Deng Z., Allis C.D., Ren B.,
RA Khochbin S., Zhao Y.;
RT "Lysine 2-hydroxyisobutyrylation is a widely distributed active histone
RT mark.";
RL Nat. Chem. Biol. 10:365-370(2014).
RN [54]
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 histone
RT H3.";
RL FEBS J. 283:4263-4273(2016).
RN [55]
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., Panne D.,
RA 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 [56]
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 [57]
RP SUCCINYLATION AT LYS-123, AND DESUSUCCINYLATION.
RX PubMed=27436229; DOI=10.1038/ncomms12235;
RA Li L., Shi L., Yang S., Yan R., Zhang D., Yang J., He L., Li W., Yi X.,
RA Sun L., Liang J., Cheng Z., Shi L., Shang Y., Yu W.;
RT "SIRT7 is a histone desuccinylase that functionally links to chromatin
RT compaction and genome stability.";
RL Nat. Commun. 7:12235-12235(2016).
RN [58]
RP MUTAGENESIS OF ARG-43.
RX PubMed=27016736; DOI=10.1093/nar/gkw202;
RA Kujirai T., Horikoshi N., Sato K., Maehara K., Machida S., Osakabe A.,
RA Kimura H., Ohkawa Y., Kurumizaka H.;
RT "Structure and function of human histone H3.Y nucleosome.";
RL Nucleic Acids Res. 44:6127-6141(2016).
RN [59]
RP CROTONYLATION AT LYS-5; LYS-10 AND LYS-24.
RX PubMed=28497810; DOI=10.1038/cr.2017.68;
RA Wei W., Liu X., Chen J., Gao S., Lu L., Zhang H., Ding G., Wang Z.,
RA Chen Z., Shi T., Li J., Yu J., Wong J.;
RT "Class I histone deacetylases are major histone decrotonylases: evidence
RT for critical and broad function of histone crotonylation in
RT transcription.";
RL Cell Res. 27:898-915(2017).
RN [60]
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 [61]
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., Xing D.,
RA 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 [62]
RP ADP-RIBOSYLATION AT SER-11.
RX PubMed=30257210; DOI=10.1016/j.celrep.2018.08.092;
RA Bartlett E., Bonfiglio J.J., Prokhorova E., Colby T., Zobel F., Ahel I.,
RA Matic I.;
RT "Interplay of histone marks with serine ADP-ribosylation.";
RL Cell Rep. 24:3488-3502(2018).
RN [63]
RP ADP-RIBOSYLATION AT SER-11 AND SER-29.
RX PubMed=29480802; DOI=10.7554/elife.34334;
RA Palazzo L., Leidecker O., Prokhorova E., Dauben H., Matic I., Ahel I.;
RT "Serine is the major residue for ADP-ribosylation upon DNA damage.";
RL Elife 7:0-0(2018).
RN [64]
RP GLUTARYLATION AT LYS-15; LYS-19; LYS-24; LYS-28; LYS-57; LYS-80; LYS-116
RP AND LYS-123.
RX PubMed=31542297; DOI=10.1016/j.molcel.2019.08.018;
RA Bao X., Liu Z., Zhang W., Gladysz K., Fung Y.M.E., Tian G., Xiong Y.,
RA Wong J.W.H., Yuen K.W.Y., Li X.D.;
RT "Glutarylation of histone H4 lysine 91 regulates chromatin dynamics.";
RL Mol. Cell 0:0-0(2019).
RN [65]
RP SEROTONYLATION AT GLN-6, AND MUTAGENESIS OF GLN-6.
RX PubMed=30867594; DOI=10.1038/s41586-019-1024-7;
RA Farrelly L.A., Thompson R.E., Zhao S., Lepack A.E., Lyu Y., Bhanu N.V.,
RA Zhang B., Loh Y.E., Ramakrishnan A., Vadodaria K.C., Heard K.J.,
RA Erikson G., Nakadai T., Bastle R.M., Lukasak B.J., Zebroski H. III,
RA Alenina N., Bader M., Berton O., Roeder R.G., Molina H., Gage F.H.,
RA Shen L., Garcia B.A., Li H., Muir T.W., Maze I.;
RT "Histone serotonylation is a permissive modification that enhances TFIID
RT binding to H3K4me3.";
RL Nature 567:535-539(2019).
RN [66]
RP LACTYLATION AT LYS-9; LYS-19; LYS-24; LYS-28 AND LYS-80.
RX PubMed=31645732; DOI=10.1038/s41586-019-1678-1;
RA Zhang D., Tang Z., Huang H., Zhou G., Cui C., Weng Y., Liu W., Kim S.,
RA Lee S., Perez-Neut M., Ding J., Czyz D., Hu R., Ye Z., He M., Zheng Y.G.,
RA Shuman H.A., Dai L., Ren B., Roeder R.G., Becker L., Zhao Y.;
RT "Metabolic regulation of gene expression by histone lactylation.";
RL Nature 574:575-580(2019).
RN [67]
RP DOPAMINYLATION AT GLN-6.
RX PubMed=32273471; DOI=10.1126/science.aaw8806;
RA Lepack A.E., Werner C.T., Stewart A.F., Fulton S.L., Zhong P.,
RA Farrelly L.A., Smith A.C.W., Ramakrishnan A., Lyu Y., Bastle R.M.,
RA Martin J.A., Mitra S., O'Connor R.M., Wang Z.J., Molina H., Turecki G.,
RA Shen L., Yan Z., Calipari E.S., Dietz D.M., Kenny P.J., Maze I.;
RT "Dopaminylation of histone H3 in ventral tegmental area regulates cocaine
RT seeking.";
RL Science 368:197-201(2020).
RN [68]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 20-43 IN COMPLEX WITH ZMYND11.
RX PubMed=24590075; DOI=10.1038/nature13045;
RA Wen H., Li Y., Xi Y., Jiang S., Stratton S., Peng D., Tanaka K., Ren Y.,
RA Xia Z., Wu J., Li B., Barton M.C., Li W., Li H., Shi X.;
RT "ZMYND11 links histone H3.3K36me3 to transcription elongation and tumour
RT suppression.";
RL Nature 508:263-268(2014).
RN [69]
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., Gupta N.,
RA 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 [70]
RP CHARACTERIZATION OF VARIANTS GLM MET-28; ARG-35 AND VAL-35.
RX PubMed=23539183; DOI=10.1126/science.1232245;
RA Lewis P.W., Mueller M.M., Koletsky M.S., Cordero F., Lin S.,
RA Banaszynski L.A., Garcia B.A., Muir T.W., Becher O.J., Allis C.D.;
RT "Inhibition of PRC2 activity by a gain-of-function H3 mutation found in
RT pediatric glioblastoma.";
RL Science 340:857-861(2013).
RN [71]
RP CHARACTERIZATION OF VARIANT 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., Murphy D.,
RA Venneti S., Hameed M., Pawel B.R., Wunder J.S., Dickson B.C.,
RA Lundgren S.M., Jani K.S., De Jay N., Papillon-Cavanagh S., Andrulis I.L.,
RA Sawyer S.L., Grynspan D., Turcotte R.E., Nadaf J., Fahiminiyah S.,
RA Muir T.W., Majewski J., Thompson C.B., Chi P., Garcia B.A., Allis C.D.,
RA Jabado N., Lewis P.W.;
RT "Histone H3K36 mutations promote sarcomagenesis through altered histone
RT methylation landscape.";
RL Science 352:844-849(2016).
RN [72]
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., Garcia B.A.,
RA Weinreb I., Goldstein D., Lewis P.W., Dancu O.M., Dhaliwal S., Stecho W.,
RA Howlett C.J., Mymryk J.S., Barrett J.W., Nichols A.C., Allis C.D.,
RA Majewski J., Jabado N.;
RT "Impaired H3K36 methylation defines a subset of head and neck squamous cell
RT carcinomas.";
RL Nat. Genet. 49:180-185(2017).
RN [73] {ECO:0007744|PDB:7CIZ, ECO:0007744|PDB:7CJ0}
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 58-136 IN COMPLEX WITH DNJC9
RP 171-249 MUTANT CYS-243; MCM2 61-130 AND HISTONE H4, IDENTIFICATION IN A
RP CO-CHAPERONE COMPLEX WITH DNJC9; MCM2 AND HISTONE H4, INTERACTION WITH
RP DNJC9; ASF1A; MCM2; NASP AND SPT2, AND MUTAGENESIS OF 106-GLU-ASP-107.
RX PubMed=33857403; DOI=10.1016/j.molcel.2021.03.041;
RA Hammond C.M., Bao H., Hendriks I.A., Carraro M., Garcia-Nieto A., Liu Y.,
RA Reveron-Gomez N., Spanos C., Chen L., Rappsilber J., Nielsen M.L.,
RA Patel D.J., Huang H., Groth A.;
RT "DNAJC9 integrates heat shock molecular chaperones into the histone
RT chaperone network.";
RL Mol. Cell 0:0-0(2021).
RN [74] {ECO:0007744|PDB:7A08}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.11 ANGSTROMS) OF 2-136 IN COMPLEX WITH
RP NUCLEOSOME CORE AND CGAS.
RX PubMed=32911480; DOI=10.1038/s41586-020-2748-0;
RA Michalski S., de Oliveira Mann C.C., Stafford C.A., Witte G., Bartho J.,
RA Lammens K., Hornung V., Hopfner K.P.;
RT "Structural basis for sequestration and autoinhibition of cGAS by
RT chromatin.";
RL Nature 587:678-682(2020).
CC -!- FUNCTION: Variant histone H3 which replaces conventional H3 in a wide
CC range of nucleosomes in active genes. Constitutes the predominant form
CC of histone H3 in non-dividing cells and is incorporated into chromatin
CC independently of DNA synthesis. Deposited at sites of nucleosomal
CC displacement throughout transcribed genes, suggesting that it
CC represents an epigenetic imprint of transcriptionally active chromatin.
CC Nucleosomes wrap and compact DNA into chromatin, limiting DNA
CC accessibility to the cellular machineries which require DNA as a
CC template. Histones thereby play a central role in transcription
CC regulation, DNA 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 nucleosome
CC remodeling. {ECO:0000269|PubMed:14718166, ECO:0000269|PubMed:15776021,
CC ECO:0000269|PubMed:16258499}.
CC -!- SUBUNIT: The nucleosome is a histone octamer containing two molecules
CC each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and
CC two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of
CC DNA. Interacts with HIRA, a chaperone required for its incorporation
CC into nucleosomes. Interacts with ZMYND11; when trimethylated at 'Lys-
CC 36' (H3.3K36me3). Found in a co-chaperone complex with DNJC9, MCM2 and
CC histone H3.3-H4 dimers (PubMed:33857403). Within the complex, interacts
CC with DNJC9 (via C-terminus); the interaction is direct
CC (PubMed:33857403). Interacts with ASF1A, MCM2, NASP and SPT2
CC (PubMed:33857403). {ECO:0000269|PubMed:14718166,
CC ECO:0000269|PubMed:24590075, ECO:0000269|PubMed:33857403}.
CC -!- INTERACTION:
CC P84243; Q9NVP2: ASF1B; NbExp=4; IntAct=EBI-120658, EBI-1055650;
CC P84243; P45973: CBX5; NbExp=2; IntAct=EBI-120658, EBI-78219;
CC P84243; Q13111: CHAF1A; NbExp=2; IntAct=EBI-120658, EBI-1020839;
CC P84243; Q9UER7: DAXX; NbExp=6; IntAct=EBI-120658, EBI-77321;
CC P84243; Q9UER7-1: DAXX; NbExp=21; IntAct=EBI-120658, EBI-287635;
CC P84243; Q9Y6K1: DNMT3A; NbExp=7; IntAct=EBI-120658, EBI-923653;
CC P84243; P62805: H4C9; NbExp=12; IntAct=EBI-120658, EBI-302023;
CC P84243; P49321-2: NASP; NbExp=3; IntAct=EBI-120658, EBI-7038920;
CC P84243; Q8IZL8: PELP1; NbExp=11; IntAct=EBI-120658, EBI-716449;
CC P84243; Q5VWG9: TAF3; NbExp=3; IntAct=EBI-120658, EBI-1560087;
CC P84243; Q9VK33: Sfmbt; Xeno; NbExp=15; IntAct=EBI-120658, EBI-117801;
CC P84243; Q8R5C8: Zmynd11; Xeno; NbExp=6; IntAct=EBI-120658, EBI-647813;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout the cell cycle independently
CC of DNA synthesis.
CC -!- DOMAIN: Specific interaction of trimethylated form at 'Lys-36'
CC (H3.3K36me3) with ZMYND11 is mediated by the encapsulation of Ser-32
CC residue with a composite pocket formed by the tandem bromo-PWWP
CC domains. {ECO:0000269|PubMed:24590075}.
CC -!- PTM: Acetylation is generally linked to gene activation. Acetylation on
CC Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s). Acetylation on
CC Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18
CC (H3R17me). Acetylation at Lys-123 (H3K122ac) by EP300/p300 plays a
CC central role in chromatin structure: localizes at the surface of the
CC histone octamer and stimulates transcription, possibly by promoting
CC nucleosome 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:17194708, ECO:0000269|PubMed:19520870,
CC ECO:0000269|PubMed:23415232, ECO:0000269|PubMed:7309716}.
CC -!- PTM: Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4
CC 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 linked
CC to gene activation. Symmetric dimethylation at Arg-9 (H3R8me2s) by
CC PRMT5 is linked to gene repression. Asymmetric dimethylation at Arg-3
CC (H3R2me2a) by PRMT6 is linked to gene repression and is mutually
CC exclusive with H3 Lys-5 methylation (H3K4me2 and H3K4me3). H3R2me2a is
CC present at the 3' of genes regardless of their transcription state and
CC is enriched on inactive promoters, while it is absent on active
CC promoters. {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:17194708, ECO:0000269|PubMed:17898714,
CC ECO:0000269|PubMed:18077460, ECO:0000269|PubMed:18079182}.
CC -!- PTM: Specifically enriched in modifications associated with active
CC chromatin such as methylation at Lys-5 (H3K4me), Lys-37 and Lys-80.
CC Methylation at Lys-5 (H3K4me) facilitates subsequent acetylation of H3
CC and H4. 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), which are linked
CC to gene repression, are underrepresented. Methylation at Lys-10
CC (H3K9me) is a specific target for HP1 proteins (CBX1, CBX3 and CBX5)
CC and prevents subsequent phosphorylation at Ser-11 (H3S10ph) and
CC acetylation of H3 and H4. Methylation at Lys-5 (H3K4me) and Lys-80
CC (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120'.
CC Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched in
CC inactive X chromosome chromatin. Monomethylation at Lys-57 (H3K56me1)
CC by EHMT2/G9A in G1 phase promotes interaction with PCNA and is required
CC 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:15851689,
CC ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050,
CC ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:16497732,
CC ECO:0000269|PubMed:17189264, ECO:0000269|PubMed:17194708,
CC ECO:0000269|PubMed:22387026, ECO:0000269|PubMed:7309716}.
CC -!- PTM: Phosphorylated at Thr-4 (H3T3ph) by HASPIN during prophase and
CC dephosphorylated during anaphase. Phosphorylation at Ser-11 (H3S10ph)
CC by AURKB is crucial for chromosome condensation and cell-cycle
CC progression during mitosis and meiosis. In addition phosphorylation at
CC Ser-11 (H3S10ph) by RPS6KA4 and RPS6KA5 is important during interphase
CC because it enables the transcription of genes following external
CC stimulation, like mitogens, stress, growth factors or UV irradiation
CC and result in the activation of genes, such as c-fos and c-jun.
CC Phosphorylation at Ser-11 (H3S10ph), which is linked to gene
CC activation, prevents methylation at Lys-10 (H3K9me) but facilitates
CC acetylation of H3 and H4. Phosphorylation at Ser-11 (H3S10ph) by AURKB
CC mediates the 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 or
CC AURKB during mitosis or upon ultraviolet B irradiation. Phosphorylation
CC at Thr-7 (H3T6ph) by PRKCB is a specific tag for epigenetic
CC transcriptional activation that prevents demethylation of Lys-5
CC (H3K4me) by LSD1/KDM1A. At centromeres, specifically phosphorylated at
CC Thr-12 (H3T11ph) from prophase to early anaphase, by DAPK3 and PKN1.
CC Phosphorylation at Thr-12 (H3T11ph) by PKN1 or isoform M2 of PKM (PKM2)
CC is a specific tag for epigenetic transcriptional activation that
CC promotes demethylation of Lys-10 (H3K9me) by KDM4C/JMJD2C.
CC Phosphorylation at Tyr-42 (H3Y41ph) by JAK2 promotes exclusion of CBX5
CC (HP1 alpha) from chromatin. Phosphorylation on Ser-32 (H3S31ph) is
CC specific to regions bordering centromeres in metaphase chromosomes.
CC {ECO:0000269|PubMed:10464286, ECO:0000269|PubMed:11242053,
CC ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:12560483,
CC ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:15684425,
CC ECO:0000269|PubMed:15851689, ECO:0000269|PubMed:16185088,
CC ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588,
CC ECO:0000269|PubMed:16497732, ECO:0000269|PubMed:17194708,
CC ECO:0000269|PubMed:18066052, ECO:0000269|PubMed:19783980,
CC ECO:0000269|PubMed:20228790, ECO:0000269|PubMed:20850016,
CC ECO:0000269|PubMed:22901803, ECO:0000269|PubMed:7309716}.
CC -!- PTM: Ubiquitinated. Monoubiquitinated by RAG1 in lymphoid cells,
CC monoubiquitination is required for V(D)J recombination (By similarity).
CC {ECO:0000250|UniProtKB:P84245}.
CC -!- PTM: Lysine deamination at Lys-5 (H3K4all) to form allysine is mediated
CC by LOXL2. Allysine formation by LOXL2 only takes place on H3K4me3 and
CC results in gene repression. {ECO:0000269|PubMed:27735137}.
CC -!- PTM: Crotonylation (Kcr) is specifically present in male germ cells and
CC marks testis-specific genes in post-meiotic cells, including X-linked
CC genes that escape sex chromosome inactivation in haploid cells.
CC Crotonylation marks active promoters and enhancers and confers
CC resistance to transcriptional repressors. It is also associated with
CC post-meiotically activated genes on autosomes.
CC {ECO:0000269|PubMed:21925322}.
CC -!- PTM: Butyrylation of histones marks active promoters and competes with
CC histone acetylation. It is present during late spermatogenesis.
CC {ECO:0000250|UniProtKB:P68433}.
CC -!- PTM: Succinylation at Lys-80 (H3K79succ) by KAT2A takes place with a
CC maximum frequency around the transcription start sites of genes
CC (PubMed:29211711). It gives a specific tag for epigenetic transcription
CC activation (PubMed:29211711). Desuccinylation at Lys-123 (H3K122succ)
CC by SIRT7 in response to DNA damage promotes chromatin condensation and
CC double-strand breaks (DSBs) repair (PubMed:27436229).
CC {ECO:0000269|PubMed:27436229, ECO:0000269|PubMed:29211711}.
CC -!- PTM: Serine ADP-ribosylation constitutes the primary form of ADP-
CC ribosylation of proteins in response to DNA damage (PubMed:29480802).
CC Serine ADP-ribosylation at Ser-11 (H3S10ADPr) is mutually exclusive
CC with phosphorylation at Ser-11 (H3S10ph) and impairs acetylation at
CC Lys-10 (H3K9ac) (PubMed:30257210). {ECO:0000269|PubMed:29480802,
CC ECO:0000269|PubMed:30257210}.
CC -!- PTM: Serotonylated by TGM2 at Gln-6 (H3Q5ser) during serotonergic
CC neuron differentiation (PubMed:30867594). H3Q5ser is associated with
CC trimethylation of Lys-5 (H3K4me3) and enhances general transcription
CC factor IID (TFIID) complex-binding to H3K4me3, thereby facilitating
CC transcription (PubMed:30867594). {ECO:0000269|PubMed:30867594}.
CC -!- PTM: Dopaminylated by TGM2 at Gln-6 (H3Q5dop) in ventral tegmental area
CC (VTA) neurons (PubMed:32273471). H3Q5dop mediates neurotransmission-
CC independent role of nuclear dopamine by regulating relapse-related
CC transcriptional plasticity in the reward system (By similarity).
CC {ECO:0000250|UniProtKB:P84245, ECO:0000269|PubMed:32273471}.
CC -!- PTM: Lactylated in macrophages by EP300/P300 by using lactoyl-CoA
CC directly derived from endogenous or exogenous lactate, leading to
CC stimulates gene transcription. {ECO:0000269|PubMed:31645732}.
CC -!- DISEASE: Glioma (GLM) [MIM:137800]: Gliomas are benign or malignant
CC central nervous system neoplasms derived from glial cells. They
CC comprise astrocytomas and glioblastoma multiforme that are derived from
CC astrocytes, oligodendrogliomas derived from oligodendrocytes and
CC ependymomas derived from ependymocytes. {ECO:0000269|PubMed:22286061,
CC ECO:0000269|PubMed:22286216, ECO:0000269|PubMed:23539269}. Note=The
CC gene represented in this entry is involved in disease pathogenesis.
CC H3F3A mutations affecting residues involved in post-translational
CC modifications of histone H3.3 are recurrent in malignant, aggressive
CC gliomas including glioblastoma multiforme (GBM) and diffuse intrinsic
CC pontine glioma (DIPG) (PubMed:22286061, PubMed:22286216). The mechanism
CC through which mutations lead to tumorigenesis involves altered histones
CC methylation, impaired regulation of Polycomb repressive complex 2
CC (PRC2) activity, and aberrant epigenetic regulation of gene expression
CC (PubMed:23539269, PubMed:23539183, PubMed:23603901).
CC {ECO:0000269|PubMed:22286061, ECO:0000269|PubMed:22286216,
CC ECO:0000269|PubMed:23539183, ECO:0000269|PubMed:23539269,
CC ECO:0000269|PubMed:23603901}.
CC -!- DISEASE: Note=H3F3A and H3F3B mutations affecting residues involved in
CC post-translational modifications of histone H3.3 are implicated in the
CC pathogenesis of some bone and cartilage neoplasms. Mutations have been
CC found with high prevalence in chondroblastoma and giant cell tumors of
CC bone, and with low frequency in osteosarcoma, conventional
CC chondrosarcoma and clear cell chondrosarcoma. Chondroblastoma samples
CC frequently carry a H3F3B mutation affecting residue Lys-37 (H3K36),
CC although H3F3A is mutated in some cases. Most giant cell tumors of bone
CC harbor H3F3A mutations affecting residue Gly-35 (H3G34).
CC {ECO:0000269|PubMed:24162739}.
CC -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
CC -!- CAUTION: The original paper reporting lysine deamination at Lys-5 by
CC LOXL2 has been retracted due to inappropriate manipulation of figure
CC data (PubMed:22483618, PubMed:27392148). However, this modification was
CC confirmed in a subsequent publication (PubMed:27735137).
CC {ECO:0000269|PubMed:27735137, ECO:0000305|PubMed:22483618,
CC ECO:0000305|PubMed:27392148}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Histone H3 entry;
CC URL="https://en.wikipedia.org/wiki/Histone_H3";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
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DR EMBL; M11354; AAA52653.1; -; mRNA.
DR EMBL; M11353; AAA52654.1; -; mRNA.
DR EMBL; Z48950; CAA88778.1; -; Genomic_DNA.
DR EMBL; X05855; CAA29288.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X05856; CAA29288.1; JOINED; Genomic_DNA.
DR EMBL; X05857; CAA29288.1; JOINED; Genomic_DNA.
DR EMBL; AF218029; AAG17271.1; -; mRNA.
DR EMBL; BX537379; CAD97621.1; -; mRNA.
DR EMBL; AL512343; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001124; AAH01124.1; -; mRNA.
DR EMBL; BC006497; AAH06497.1; -; mRNA.
DR EMBL; BC012813; AAH12813.1; -; mRNA.
DR EMBL; BC017558; AAH17558.1; -; mRNA.
DR EMBL; BC029405; AAH29405.1; -; mRNA.
DR EMBL; BC038989; AAH38989.1; -; mRNA.
DR EMBL; BC066901; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC067757; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC081560; AAH81560.1; -; mRNA.
DR EMBL; BC081561; AAH81561.1; -; mRNA.
DR EMBL; BC095447; AAH95447.1; -; mRNA.
DR EMBL; BC108701; AAI08702.1; -; mRNA.
DR CCDS; CCDS11729.1; -.
DR CCDS; CCDS1550.1; -.
DR PIR; A27501; HSHU33.
DR RefSeq; NP_002098.1; NM_002107.4.
DR RefSeq; NP_005315.1; NM_005324.4.
DR PDB; 2L43; NMR; -; A=2-13.
DR PDB; 3ASK; X-ray; 2.90 A; P/Q/R=2-14.
DR PDB; 3ASL; X-ray; 1.41 A; B=2-12.
DR PDB; 3AV2; X-ray; 2.80 A; A/E=1-136.
DR PDB; 3JVK; X-ray; 1.80 A; C=13-20.
DR PDB; 3MUK; X-ray; 1.75 A; D=22-29.
DR PDB; 3MUL; X-ray; 1.65 A; D=13-20.
DR PDB; 3QL9; X-ray; 0.93 A; C=2-16.
DR PDB; 3QLA; X-ray; 1.60 A; C/F=2-16.
DR PDB; 3QLC; X-ray; 2.50 A; C/D=2-16.
DR PDB; 3WTP; X-ray; 2.67 A; E=1-136.
DR PDB; 4GNE; X-ray; 1.47 A; B=2-8.
DR PDB; 4GNF; X-ray; 1.55 A; C=2-16.
DR PDB; 4GNG; X-ray; 1.73 A; B/F=2-16.
DR PDB; 4GU0; X-ray; 3.10 A; E/F=2-27.
DR PDB; 4GUR; X-ray; 2.51 A; C=2-22.
DR PDB; 4GUS; X-ray; 2.23 A; C=2-22.
DR PDB; 4GY5; X-ray; 2.96 A; E/F=2-18.
DR PDB; 4H9N; X-ray; 1.95 A; A=2-136.
DR PDB; 4H9O; X-ray; 2.05 A; A=2-136.
DR PDB; 4H9P; X-ray; 2.20 A; A=2-136.
DR PDB; 4H9Q; X-ray; 1.95 A; A=2-136.
DR PDB; 4H9R; X-ray; 2.20 A; A=2-136.
DR PDB; 4H9S; X-ray; 2.60 A; A/B=2-136.
DR PDB; 4HGA; X-ray; 2.80 A; B=1-136.
DR PDB; 4L58; X-ray; 1.48 A; B=2-13.
DR PDB; 4N4I; X-ray; 2.00 A; B=20-43.
DR PDB; 4O62; X-ray; 1.78 A; D=2-12.
DR PDB; 4QQ4; X-ray; 1.75 A; C/D=2-16.
DR PDB; 4TMP; X-ray; 2.30 A; B/D=2-12.
DR PDB; 4U7T; X-ray; 2.90 A; F/G=2-13.
DR PDB; 4W5A; X-ray; 2.60 A; C/D/F=2-16.
DR PDB; 5B32; X-ray; 2.35 A; A/E=1-136.
DR PDB; 5B33; X-ray; 2.92 A; A/E=1-136.
DR PDB; 5BNV; X-ray; 2.79 A; A/D=58-136.
DR PDB; 5BNX; X-ray; 2.31 A; A=58-136.
DR PDB; 5DWQ; X-ray; 2.36 A; F/G=14-31.
DR PDB; 5DX0; X-ray; 2.05 A; F/G/H/I=14-31.
DR PDB; 5JA4; X-ray; 2.42 A; A=58-136.
DR PDB; 5JJY; X-ray; 2.05 A; B=30-43.
DR PDB; 5JLB; X-ray; 1.50 A; B=30-43.
DR PDB; 5KDM; X-ray; 3.50 A; A=2-136.
DR PDB; 5X7X; X-ray; 2.18 A; A/E=1-136.
DR PDB; 6A5L; EM; 5.60 A; a/e=1-136.
DR PDB; 6A5O; EM; 9.90 A; a/e=1-136.
DR PDB; 6A5P; EM; 7.00 A; a/e=1-136.
DR PDB; 6A5R; EM; 8.70 A; a/e=1-136.
DR PDB; 6A5T; EM; 6.70 A; a/e=1-136.
DR PDB; 6A5U; EM; 7.60 A; a/e=1-136.
DR PDB; 6HGT; X-ray; 2.33 A; E/F/G/H=4-18.
DR PDB; 6INQ; EM; 6.90 A; a/e=1-136.
DR PDB; 6IR9; EM; 3.80 A; a/e=1-136.
DR PDB; 6J4W; EM; 7.90 A; a/e=1-136.
DR PDB; 6J4X; EM; 4.30 A; a/e=1-136.
DR PDB; 6J4Y; EM; 4.30 A; a/e=1-136.
DR PDB; 6J4Z; EM; 4.10 A; a/e=1-136.
DR PDB; 6J50; EM; 4.70 A; a/e=1-136.
DR PDB; 6J51; EM; 4.20 A; a/e=1-136.
DR PDB; 6J9J; X-ray; 1.78 A; B=30-43.
DR PDB; 6PZV; X-ray; 3.01 A; D/H=2-27.
DR PDB; 6QXZ; NMR; -; B=2-10.
DR PDB; 6R0C; EM; 4.20 A; A/E=1-136.
DR PDB; 6RNY; EM; 3.90 A; A/E=1-136.
DR PDB; 6U04; X-ray; 2.20 A; A=2-13.
DR PDB; 7A08; EM; 3.11 A; d/h=2-136.
DR PDB; 7CIZ; X-ray; 1.80 A; A/E/I=58-136.
DR PDB; 7CJ0; X-ray; 2.50 A; B/E=58-136.
DR PDB; 7CWH; NMR; -; A=32-42.
DR PDB; 7OKP; X-ray; 2.20 A; E/F/G/H=14-23.
DR PDBsum; 2L43; -.
DR PDBsum; 3ASK; -.
DR PDBsum; 3ASL; -.
DR PDBsum; 3AV2; -.
DR PDBsum; 3JVK; -.
DR PDBsum; 3MUK; -.
DR PDBsum; 3MUL; -.
DR PDBsum; 3QL9; -.
DR PDBsum; 3QLA; -.
DR PDBsum; 3QLC; -.
DR PDBsum; 3WTP; -.
DR PDBsum; 4GNE; -.
DR PDBsum; 4GNF; -.
DR PDBsum; 4GNG; -.
DR PDBsum; 4GU0; -.
DR PDBsum; 4GUR; -.
DR PDBsum; 4GUS; -.
DR PDBsum; 4GY5; -.
DR PDBsum; 4H9N; -.
DR PDBsum; 4H9O; -.
DR PDBsum; 4H9P; -.
DR PDBsum; 4H9Q; -.
DR PDBsum; 4H9R; -.
DR PDBsum; 4H9S; -.
DR PDBsum; 4HGA; -.
DR PDBsum; 4L58; -.
DR PDBsum; 4N4I; -.
DR PDBsum; 4O62; -.
DR PDBsum; 4QQ4; -.
DR PDBsum; 4TMP; -.
DR PDBsum; 4U7T; -.
DR PDBsum; 4W5A; -.
DR PDBsum; 5B32; -.
DR PDBsum; 5B33; -.
DR PDBsum; 5BNV; -.
DR PDBsum; 5BNX; -.
DR PDBsum; 5DWQ; -.
DR PDBsum; 5DX0; -.
DR PDBsum; 5JA4; -.
DR PDBsum; 5JJY; -.
DR PDBsum; 5JLB; -.
DR PDBsum; 5KDM; -.
DR PDBsum; 5X7X; -.
DR PDBsum; 6A5L; -.
DR PDBsum; 6A5O; -.
DR PDBsum; 6A5P; -.
DR PDBsum; 6A5R; -.
DR PDBsum; 6A5T; -.
DR PDBsum; 6A5U; -.
DR PDBsum; 6HGT; -.
DR PDBsum; 6INQ; -.
DR PDBsum; 6IR9; -.
DR PDBsum; 6J4W; -.
DR PDBsum; 6J4X; -.
DR PDBsum; 6J4Y; -.
DR PDBsum; 6J4Z; -.
DR PDBsum; 6J50; -.
DR PDBsum; 6J51; -.
DR PDBsum; 6J9J; -.
DR PDBsum; 6PZV; -.
DR PDBsum; 6QXZ; -.
DR PDBsum; 6R0C; -.
DR PDBsum; 6RNY; -.
DR PDBsum; 6U04; -.
DR PDBsum; 7A08; -.
DR PDBsum; 7CIZ; -.
DR PDBsum; 7CJ0; -.
DR PDBsum; 7CWH; -.
DR PDBsum; 7OKP; -.
DR AlphaFoldDB; P84243; -.
DR SMR; P84243; -.
DR BioGRID; 109272; 177.
DR BioGRID; 109273; 92.
DR CORUM; P84243; -.
DR DIP; DIP-40046N; -.
DR IntAct; P84243; 85.
DR MINT; P84243; -.
DR STRING; 9606.ENSP00000254810; -.
DR GlyGen; P84243; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P84243; -.
DR MetOSite; P84243; -.
DR PhosphoSitePlus; P84243; -.
DR SwissPalm; P84243; -.
DR BioMuta; H3F3A; -.
DR DMDM; 55977062; -.
DR EPD; P84243; -.
DR jPOST; P84243; -.
DR MassIVE; P84243; -.
DR MaxQB; P84243; -.
DR PaxDb; P84243; -.
DR PeptideAtlas; P84243; -.
DR PRIDE; P84243; -.
DR ProteomicsDB; 57757; -.
DR TopDownProteomics; P84243; -.
DR Antibodypedia; 32264; 713 antibodies from 40 providers.
DR Antibodypedia; 54014; 609 antibodies from 19 providers.
DR DNASU; 3020; -.
DR Ensembl; ENST00000254810.8; ENSP00000254810.3; ENSG00000132475.10.
DR Ensembl; ENST00000366813.1; ENSP00000355778.1; ENSG00000163041.13.
DR Ensembl; ENST00000366815.10; ENSP00000355780.3; ENSG00000163041.13.
DR Ensembl; ENST00000366816.5; ENSP00000355781.1; ENSG00000163041.13.
DR Ensembl; ENST00000586607.5; ENSP00000466020.1; ENSG00000132475.10.
DR Ensembl; ENST00000587560.5; ENSP00000468714.1; ENSG00000132475.10.
DR Ensembl; ENST00000589599.5; ENSP00000465813.1; ENSG00000132475.10.
DR Ensembl; ENST00000655399.1; ENSP00000499800.1; ENSG00000163041.13.
DR Ensembl; ENST00000661429.1; ENSP00000499385.1; ENSG00000163041.13.
DR Ensembl; ENST00000666609.1; ENSP00000499275.1; ENSG00000163041.13.
DR GeneID; 3020; -.
DR GeneID; 3021; -.
DR KEGG; hsa:3020; -.
DR KEGG; hsa:3021; -.
DR MANE-Select; ENST00000254810.8; ENSP00000254810.3; NM_005324.5; NP_005315.1.
DR MANE-Select; ENST00000366815.10; ENSP00000355780.3; NM_002107.7; NP_002098.1.
DR UCSC; uc001hpw.4; human.
DR CTD; 3020; -.
DR CTD; 3021; -.
DR DisGeNET; 3020; -.
DR DisGeNET; 3021; -.
DR GeneCards; H3-3A; -.
DR GeneCards; H3-3B; -.
DR HGNC; HGNC:4764; H3-3A.
DR HGNC; HGNC:4765; H3-3B.
DR HPA; ENSG00000132475; Tissue enhanced (bone).
DR HPA; ENSG00000163041; Low tissue specificity.
DR MalaCards; H3-3A; -.
DR MIM; 137800; phenotype.
DR MIM; 601058; gene.
DR MIM; 601128; gene.
DR neXtProt; NX_P84243; -.
DR OpenTargets; ENSG00000132475; -.
DR OpenTargets; ENSG00000163041; -.
DR PharmGKB; PA29140; -.
DR VEuPathDB; HostDB:ENSG00000132475; -.
DR VEuPathDB; HostDB:ENSG00000163041; -.
DR eggNOG; KOG1745; Eukaryota.
DR GeneTree; ENSGT01050000244918; -.
DR HOGENOM; CLU_078295_4_0_1; -.
DR InParanoid; P84243; -.
DR OMA; HIVMART; -.
DR OrthoDB; 1564596at2759; -.
DR PhylomeDB; P84243; -.
DR TreeFam; TF314241; -.
DR PathwayCommons; P84243; -.
DR Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation.
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-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-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-HSA-73728; RNA Polymerase I Promoter Opening.
DR Reactome; R-HSA-73772; RNA Polymerase I Promoter Escape.
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-9616222; Transcriptional regulation of granulopoiesis.
DR Reactome; R-HSA-9670095; Inhibition of DNA recombination at telomere.
DR Reactome; R-HSA-9710421; Defective pyroptosis.
DR Reactome; R-HSA-977225; Amyloid fiber formation.
DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; P84243; -.
DR SIGNOR; P84243; -.
DR BioGRID-ORCS; 3020; 251 hits in 667 CRISPR screens.
DR BioGRID-ORCS; 3021; 147 hits in 1060 CRISPR screens.
DR ChiTaRS; H3F3A; human.
DR ChiTaRS; H3F3B; human.
DR EvolutionaryTrace; P84243; -.
DR GeneWiki; H3F3A; -.
DR Pharos; P84243; Tbio.
DR PRO; PR:P84243; -.
DR Proteomes; UP000005640; Chromosome 1.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P84243; protein.
DR Bgee; ENSG00000132475; Expressed in oocyte and 222 other tissues.
DR ExpressionAtlas; P84243; baseline and differential.
DR Genevisible; P84243; HS.
DR GO; GO:0001740; C:Barr body; IEA:Ensembl.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:BHF-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0000939; C:inner kinetochore; IEA:Ensembl.
DR GO; GO:0000228; C:nuclear chromosome; 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:0031492; F:nucleosomal DNA binding; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:0006336; P:DNA replication-independent chromatin assembly; IDA:UniProtKB.
DR GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
DR GO; GO:0043987; P:histone H3-S10 phosphorylation; IEA:Ensembl.
DR GO; GO:2000751; P:histone H3-T3 phosphorylation involved in chromosome passenger complex localization to kinetochore; IEA:Ensembl.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:0042692; P:muscle cell differentiation; IEA:Ensembl.
DR GO; GO:1902340; P:negative regulation of chromosome condensation; IEA:Ensembl.
DR GO; GO:0006334; P:nucleosome assembly; IDA:UniProtKB.
DR GO; GO:0006997; P:nucleus organization; IEA:Ensembl.
DR GO; GO:0001556; P:oocyte maturation; IEA:Ensembl.
DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0031508; P:pericentric heterochromatin assembly; IEA:Ensembl.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0090230; P:regulation of centromere complex assembly; IEA:Ensembl.
DR GO; GO:0007338; P:single fertilization; IEA:Ensembl.
DR GO; GO:0007286; P:spermatid development; IEA:Ensembl.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IEA:Ensembl.
DR GO; GO:0032200; P:telomere organization; TAS:BHF-UCL.
DR Gene3D; 1.10.20.10; -; 1.
DR IDEAL; IID00239; -.
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; Citrullination;
KW Direct protein sequencing; Disease variant; DNA-binding; Hydroxylation;
KW Methylation; Nucleosome core; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..136
FT /note="Histone H3.3"
FT /id="PRO_0000221247"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 32
FT /note="Interaction with ZMYND11"
FT /evidence="ECO:0000269|PubMed:24590075"
FT MOD_RES 3
FT /note="Asymmetric dimethylarginine; by PRMT6; alternate"
FT /evidence="ECO:0000269|PubMed:17898714,
FT ECO:0000269|PubMed:18077460, ECO:0000269|PubMed:18079182"
FT MOD_RES 3
FT /note="Citrulline; alternate"
FT /evidence="ECO:0000269|PubMed:16567635"
FT MOD_RES 4
FT /note="Phosphothreonine; by HASPIN"
FT /evidence="ECO:0000269|PubMed:15681610,
FT ECO:0000269|PubMed:16185088"
FT MOD_RES 5
FT /note="Allysine; alternate"
FT /evidence="ECO:0000269|PubMed:27735137"
FT MOD_RES 5
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16185088,
FT ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588,
FT ECO:0000269|PubMed:17194708"
FT MOD_RES 5
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16185088,
FT ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588,
FT ECO:0000269|PubMed:17194708"
FT MOD_RES 5
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 5
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 5
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17194708"
FT MOD_RES 5
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322,
FT ECO:0000269|PubMed:28497810"
FT MOD_RES 5
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16185088,
FT ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588,
FT ECO:0000269|PubMed:17194708"
FT MOD_RES 6
FT /note="5-glutamyl dopamine; alternate"
FT /evidence="ECO:0000269|PubMed:32273471"
FT MOD_RES 6
FT /note="5-glutamyl serotonin; alternate"
FT /evidence="ECO:0000269|PubMed:30867594"
FT MOD_RES 7
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000269|PubMed:20228790"
FT MOD_RES 9
FT /note="Citrulline; alternate"
FT /evidence="ECO:0000269|PubMed:15345777,
FT ECO:0000269|PubMed:16567635"
FT MOD_RES 9
FT /note="Symmetric dimethylarginine; by PRMT5; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84244"
FT MOD_RES 10
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:11242053,
FT ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050,
FT ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708,
FT ECO:0000269|PubMed:7309716"
FT MOD_RES 10
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:11242053,
FT ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050,
FT ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708,
FT ECO:0000269|PubMed:7309716"
FT MOD_RES 10
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 10
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 10
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16185088,
FT ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588,
FT ECO:0000269|PubMed:16497732, ECO:0000269|PubMed:17194708"
FT MOD_RES 10
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105113"
FT MOD_RES 10
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322,
FT ECO:0000269|PubMed:28497810"
FT MOD_RES 10
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31645732"
FT MOD_RES 10
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:11242053,
FT ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050,
FT ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708,
FT ECO:0000269|PubMed:7309716"
FT MOD_RES 11
FT /note="ADP-ribosylserine; alternate"
FT /evidence="ECO:0000269|PubMed:28190768,
FT ECO:0000269|PubMed:29480802"
FT MOD_RES 11
FT /note="Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3,
FT RPS6KA4 and RPS6KA5"
FT /evidence="ECO:0000269|PubMed:10464286,
FT ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:12560483,
FT ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:15851689,
FT ECO:0000269|PubMed:16185088"
FT MOD_RES 12
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000269|PubMed:12560483,
FT ECO:0000269|PubMed:18066052, ECO:0000269|PubMed:22901803"
FT MOD_RES 15
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 15
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 15
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16185088,
FT ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16497732,
FT ECO:0000269|PubMed:17194708, ECO:0000269|PubMed:7309716"
FT MOD_RES 15
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31542297"
FT MOD_RES 15
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84244"
FT MOD_RES 15
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:22389435"
FT MOD_RES 18
FT /note="Asymmetric dimethylarginine; by CARM1; alternate"
FT /evidence="ECO:0000269|PubMed:15345777,
FT ECO:0000269|PubMed:15471871, ECO:0000269|PubMed:16497732"
FT MOD_RES 18
FT /note="Citrulline; alternate"
FT /evidence="ECO:0000269|PubMed:15345777,
FT ECO:0000269|PubMed:16497732, ECO:0000269|PubMed:16567635"
FT MOD_RES 19
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 19
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 19
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16267050,
FT ECO:0000269|PubMed:17194708"
FT MOD_RES 19
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105113"
FT MOD_RES 19
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
FT MOD_RES 19
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31542297"
FT MOD_RES 19
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31645732"
FT MOD_RES 19
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16267050,
FT ECO:0000269|PubMed:17194708"
FT MOD_RES 24
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 24
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 24
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16267050,
FT ECO:0000269|PubMed:17194708, ECO:0000269|PubMed:7309716"
FT MOD_RES 24
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105113"
FT MOD_RES 24
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322,
FT ECO:0000269|PubMed:28497810"
FT MOD_RES 24
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31542297"
FT MOD_RES 24
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31645732"
FT MOD_RES 24
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17194708"
FT MOD_RES 27
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:16567635"
FT MOD_RES 28
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16185088,
FT ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:17194708,
FT ECO:0000269|PubMed:7309716"
FT MOD_RES 28
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16185088,
FT ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:17194708,
FT ECO:0000269|PubMed:7309716, ECO:0007744|PubMed:24129315"
FT MOD_RES 28
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 28
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 28
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16267050,
FT ECO:0000269|PubMed:17194708, ECO:0007744|PubMed:19608861"
FT MOD_RES 28
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
FT MOD_RES 28
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31542297"
FT MOD_RES 28
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31645732"
FT MOD_RES 28
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16185088,
FT ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:17194708,
FT ECO:0000269|PubMed:7309716"
FT MOD_RES 29
FT /note="ADP-ribosylserine; alternate"
FT /evidence="ECO:0000269|PubMed:28190768,
FT ECO:0000269|PubMed:29480802"
FT MOD_RES 29
FT /note="Phosphoserine; alternate; by AURKB, AURKC and
FT RPS6KA5"
FT /evidence="ECO:0000269|PubMed:10464286,
FT ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:15681610,
FT ECO:0000269|PubMed:15684425, ECO:0000269|PubMed:15851689,
FT ECO:0000269|PubMed:16185088"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15851689,
FT ECO:0000269|PubMed:16185088"
FT MOD_RES 37
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16185088,
FT ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:17194708,
FT ECO:0000269|PubMed:7309716"
FT MOD_RES 37
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16185088,
FT ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:17194708,
FT ECO:0000269|PubMed:7309716"
FT MOD_RES 37
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 37
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17189264,
FT ECO:0000269|PubMed:17194708"
FT MOD_RES 37
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16185088,
FT ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:17194708,
FT ECO:0000269|PubMed:7309716"
FT MOD_RES 38
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 42
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:19783980"
FT MOD_RES 57
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17194708,
FT ECO:0000269|PubMed:22387026"
FT MOD_RES 57
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 57
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 57
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17194708"
FT MOD_RES 57
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
FT MOD_RES 57
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31542297"
FT MOD_RES 57
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84244"
FT MOD_RES 57
FT /note="N6-methyllysine; by EHMT2; alternate"
FT /evidence="ECO:0000269|PubMed:17194708,
FT ECO:0000269|PubMed:22387026"
FT MOD_RES 57
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:22389435"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20850016"
FT MOD_RES 65
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 65
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16267050,
FT ECO:0000269|PubMed:17194708"
FT MOD_RES 80
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84244"
FT MOD_RES 80
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:15525939,
FT ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:17194708"
FT MOD_RES 80
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 80
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 80
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17194708"
FT MOD_RES 80
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31542297"
FT MOD_RES 80
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31645732"
FT MOD_RES 80
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:15525939,
FT ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:17194708"
FT MOD_RES 80
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:22389435,
FT ECO:0000269|PubMed:29211711"
FT MOD_RES 81
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:20850016"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 108
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q71DI3"
FT MOD_RES 116
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:19520870"
FT MOD_RES 116
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31542297"
FT MOD_RES 123
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 123
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 123
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:19520870,
FT ECO:0000269|PubMed:23415232"
FT MOD_RES 123
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31542297"
FT MOD_RES 123
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16267050,
FT ECO:0000269|PubMed:17194708"
FT MOD_RES 123
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:22389435,
FT ECO:0000269|PubMed:27436229"
FT VARIANT 28
FT /note="K -> M (in GLM; glioblastoma multiforme samples and
FT diffuse intrinsic pontine glioma; somatic mutation; more
FT prevalent in pediatric than adult malignancies; results in
FT reduced allosteric activation of PRC2 causing a global
FT decrease of H3K27me3 levels; has no effect on H3K4me3 or
FT H3K36me3 levels; dbSNP:rs1057519903)"
FT /evidence="ECO:0000269|PubMed:22286061,
FT ECO:0000269|PubMed:22286216, ECO:0000269|PubMed:23539183"
FT /id="VAR_079021"
FT VARIANT 35
FT /note="G -> R (in GLM; glioblastoma multiforme samples;
FT somatic mutation; also found in osteosarcoma samples;
FT results in global decrease of H3K36me2 and H3K36me3 levels;
FT has no effect on H3K27me3 levels; dbSNP:rs1553260624)"
FT /evidence="ECO:0000269|PubMed:22286061,
FT ECO:0000269|PubMed:23539183"
FT /id="VAR_079022"
FT VARIANT 35
FT /note="G -> V (in GLM; glioblastoma multiforme samples;
FT somatic mutation; affects regulation of gene expression and
FT results in up-regulation of MYCN; results in global
FT decrease of H3K36me2 and H3K36me3 levels; has no effect on
FT H3K27me3 levels)"
FT /evidence="ECO:0000269|PubMed:22286061,
FT ECO:0000269|PubMed:23539183, ECO:0000269|PubMed:23539269"
FT /id="VAR_079023"
FT VARIANT 35
FT /note="G -> W (probable disease-associated variant found in
FT giant cell tumors of bone; somatic mutation)"
FT /evidence="ECO:0000269|PubMed:24162739"
FT /id="VAR_079024"
FT VARIANT 37
FT /note="K -> M (probable disease-associated variant found in
FT chondroblastoma and clear cell chondrosarcoma; somatic
FT mutation; also found in a subset of human papillomavirus-
FT negative head and neck squamous cell carcinomas; results in
FT global decrease of H3K36me2 and H3K36me3 levels and
FT increased H3K27me3 levels)"
FT /evidence="ECO:0000269|PubMed:24162739,
FT ECO:0000269|PubMed:27174990, ECO:0000269|PubMed:28067913"
FT /id="VAR_079025"
FT MUTAGEN 6
FT /note="Q->A: Abolished serotonylation by TGM2."
FT /evidence="ECO:0000269|PubMed:30867594"
FT MUTAGEN 43
FT /note="R->K: Reduced binding of histone H1 to histone H3.3-
FT containing nucleosomes."
FT /evidence="ECO:0000269|PubMed:27016736"
FT MUTAGEN 106..107
FT /note="ED->AA: Loss of interaction with DNAJC9, but not
FT with other histone chaperones, such as ASF1A, MCCM2, NASP
FT or SPT2."
FT /evidence="ECO:0000269|PubMed:33857403"
FT CONFLICT 9
FT /note="R -> L (in Ref. 7; AAH81561)"
FT /evidence="ECO:0000305"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:3QL9"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:4GY5"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:6PZV"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:5DX0"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:5JLB"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:4H9N"
FT HELIX 49..59
FT /evidence="ECO:0007829|PDB:4H9N"
FT HELIX 65..77
FT /evidence="ECO:0007829|PDB:7CIZ"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:5X7X"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:4H9N"
FT HELIX 87..114
FT /evidence="ECO:0007829|PDB:7CIZ"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:7CIZ"
FT HELIX 122..131
FT /evidence="ECO:0007829|PDB:7CIZ"
SQ SEQUENCE 136 AA; 15328 MW; 5158ED279E6F9E1C CRC64;
MARTKQTARK STGGKAPRKQ LATKAARKSA PSTGGVKKPH RYRPGTVALR EIRRYQKSTE
LLIRKLPFQR LVREIAQDFK TDLRFQSAAI GALQEASEAY LVGLFEDTNL CAIHAKRVTI
MPKDIQLARR IRGERA
