ID H32_HUMAN Reviewed; 136 AA. AC Q71DI3; A2BDF6; A6NFS4; Q6B053; DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 200. DE RecName: Full=Histone H3.2; DE AltName: Full=H3-clustered histone 13 {ECO:0000312|HGNC:HGNC:25311}; DE AltName: Full=H3-clustered histone 14 {ECO:0000312|HGNC:HGNC:20503}; DE AltName: Full=H3-clustered histone 15 {ECO:0000312|HGNC:HGNC:20505}; DE AltName: Full=Histone H3/m; DE AltName: Full=Histone H3/o; GN Name=H3C15 {ECO:0000312|HGNC:HGNC:20505}; GN Synonyms=HIST2H3A {ECO:0000312|HGNC:HGNC:20505}; GN and GN Name=H3C14 {ECO:0000312|HGNC:HGNC:20503}; GN Synonyms=H3F2, H3FM, HIST2H3C {ECO:0000312|HGNC:HGNC:20503}; GN and GN Name=H3C13 {ECO:0000312|HGNC:HGNC:25311}; GN Synonyms=HIST2H3D {ECO:0000312|HGNC:HGNC:25311}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=12408966; DOI=10.1016/s0888-7543(02)96850-3; RA Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.; RT "The human and mouse replication-dependent histone genes."; RL Genomics 80:487-498(2002). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=15527963; DOI=10.1016/j.gene.2004.07.036; RA Braastad C.D., Hovhannisyan H., van Wijnen A.J., Stein J.L., Stein G.S.; RT "Functional characterization of a human histone gene cluster duplication."; RL Gene 342:35-40(2004). RN [3] 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [5] RP PROTEIN SEQUENCE OF 28-41, METHYLATION AT LYS-10; LYS-28 AND LYS-37, RP PHOSPHORYLATION AT THR-4; SER-11 AND SER-29, ACETYLATION AT LYS-10 AND RP LYS-15, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=16185088; DOI=10.1021/bi050906n; RA Garcia B.A., Barber C.M., Hake S.B., Ptak C., Turner F.B., Busby S.A., RA Shabanowitz J., Moran R.G., Allis C.D., Hunt D.F.; RT "Modifications of human histone H3 variants during mitosis."; RL Biochemistry 44:13202-13213(2005). RN [6] 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 [7] RP PARTIAL PROTEIN SEQUENCE. RC TISSUE=Spleen; 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 [8] 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 [9] 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 [10] 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 [11] 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 [12] 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 [13] 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 [14] 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 [15] 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 [16] 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 [17] RP UBIQUITINATION. RX PubMed=16678110; DOI=10.1016/j.molcel.2006.03.035; RA Wang H., Zhai L., Xu J., Joo H.-Y., Jackson S., Erdjument-Bromage H., RA Tempst P., Xiong Y., Zhang Y.; RT "Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase RT facilitates cellular response to DNA damage."; RL Mol. Cell 22:383-394(2006). RN [18] RP ACETYLATION AT LYS-10; LYS-15; LYS-19; LYS-24 AND LYS-28, METHYLATION AT RP LYS-28; LYS-37 AND LYS-80, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=16627869; DOI=10.1074/mcp.m600007-mcp200; RA Beck H.C., Nielsen E.C., Matthiesen R., Jensen L.H., Sehested M., Finn P., RA Grauslund M., Hansen A.M., Jensen O.N.; RT "Quantitative proteomic analysis of post-translational modifications of RT human histones."; RL Mol. Cell. Proteomics 5:1314-1325(2006). RN [19] 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 [20] 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 [21] 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 [22] 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 [23] 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 [24] 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 [25] 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 [26] 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 [27] 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 [28] 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 [29] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-108, AND IDENTIFICATION BY RP 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 [30] 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 [31] 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 [32] 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 [33] RP PALMITOYLATION AT CYS-111, MUTAGENESIS OF CYS-111, AND IDENTIFICATION BY RP MASS SPECTROMETRY. RX PubMed=21076176; DOI=10.1074/mcp.m110.001198; RA Wilson J.P., Raghavan A.S., Yang Y.Y., Charron G., Hang H.C.; RT "Proteomic analysis of fatty-acylated proteins in mammalian cells with RT chemical reporters reveals S-acylation of histone H3 variants."; RL Mol. Cell. Proteomics 10:M110.001198-M110.001198(2011). RN [34] 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 [35] 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 [36] RP RETRACTED PAPER. 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 [37] RP RETRACTION NOTICE OF PUBMED:22483618. 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 [38] 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 [39] 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 [40] 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 [41] 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 [42] 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 [43] 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 [44] 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 [45] 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 [46] 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 [47] 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 [48] 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 [49] 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 [50] 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 [51] 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 [52] RP SEROTONYLATION AT 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 [53] 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 [54] 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 [55] RP ADP-RIBOSYLATION AT SER-11. RX PubMed=34874266; DOI=10.7554/elife.71502; RA Mohapatra J., Tashiro K., Beckner R.L., Sierra J., Kilgore J.A., RA Williams N.S., Liszczak G.; RT "Serine ADP-ribosylation marks nucleosomes for ALC1-dependent chromatin RT remodeling."; RL Elife 10:0-0(2021). RN [56] RP INTERACTION WITH DNAJC9; CHAF1A AND CHAF1B. 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 [57] RP ACETYLATION AT LYS-19, AND ACYLATION AT LYS-19. RX PubMed=35939806; DOI=10.1021/acschembio.2c00348; RA Kuznetsov V.I., Liu W.H., Klein M.A., Denu J.M.; RT "Potent Activation of NAD+-Dependent Deacetylase Sirt7 by Nucleosome RT Binding."; RL ACS Chem. Biol. 17:2248-2261(2022). RN [58] RP STRUCTURE BY NMR OF 121-136 IN COMPLEX WITH ASF1. RX PubMed=17292837; DOI=10.1016/j.str.2007.01.002; RA Agez M., Chen J., Guerois R., van Heijenoort C., Thuret J.-Y., Mann C., RA Ochsenbein F.; RT "Structure of the histone chaperone ASF1 bound to the histone H3 C-terminal RT helix and functional insights."; RL Structure 15:191-199(2007). RN [59] {ECO:0007744|PDB:6Y5D} RP STRUCTURE BY ELECTRON MICROSCOPY (4.10 ANGSTROMS) OF 39-136 IN COMPLEX WITH RP NUCLEOSOME CORE AND CGAS. RX PubMed=32911482; DOI=10.1038/s41586-020-2750-6; RA Pathare G.R., Decout A., Glueck S., Cavadini S., Makasheva K., Hovius R., RA Kempf G., Weiss J., Kozicka Z., Guey B., Melenec P., Fierz B., Thomae N.H., RA Ablasser A.; RT "Structural mechanism of cGAS inhibition by the nucleosome."; RL Nature 587:668-672(2020). RN [60] {ECO:0007744|PDB:6X59, ECO:0007744|PDB:6X5A, ECO:0007744|PDB:6XJD} RP STRUCTURE BY ELECTRON MICROSCOPY (2.98 ANGSTROMS) OF 2-136 IN COMPLEX WITH RP NUCLEOSOME CORE AND CGAS. RX PubMed=32911481; DOI=10.1038/s41586-020-2749-z; RA Zhao B., Xu P., Rowlett C.M., Jing T., Shinde O., Lei Y., West A.P., RA Liu W.R., Li P.; RT "The molecular basis of tight nuclear tethering and inactivation of cGAS."; RL Nature 587:673-677(2020). RN [61] {ECO:0007744|PDB:7JO9, ECO:0007744|PDB:7JOA} RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS) IN COMPLEX WITH RP NUCLEOSOME CORE AND CGAS. RX PubMed=32913000; DOI=10.1126/science.abd0609; RA Boyer J.A., Spangler C.J., Strauss J.D., Cesmat A.P., Liu P., McGinty R.K., RA Zhang Q.; RT "Structural basis of nucleosome-dependent cGAS inhibition."; RL Science 370:450-454(2020). CC -!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact CC DNA into chromatin, limiting DNA accessibility to the cellular CC machineries which require DNA as a template. Histones thereby play a CC central role in transcription regulation, DNA repair, DNA replication CC and chromosomal stability. DNA accessibility is regulated via a complex CC set of post-translational modifications of histones, also called CC histone code, and nucleosome remodeling. 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. During nucleosome assembly the chaperone ASF1A interacts with the CC histone H3-H4 heterodimer. Interacts with DNAJC9, CHAF1A and CHAF1B CC (PubMed:33857403). {ECO:0000269|PubMed:17292837, CC ECO:0000269|PubMed:33857403}. CC -!- INTERACTION: CC Q71DI3; Q9UBB4: ATXN10; NbExp=3; IntAct=EBI-750650, EBI-702390; CC Q71DI3; Q12830-4: BPTF; NbExp=2; IntAct=EBI-750650, EBI-4288838; CC Q71DI3; Q13111: CHAF1A; NbExp=2; IntAct=EBI-750650, EBI-1020839; CC Q71DI3; Q9UER7-1: DAXX; NbExp=5; IntAct=EBI-750650, EBI-287635; CC Q71DI3; P09172: DBH; NbExp=3; IntAct=EBI-750650, EBI-8589586; CC Q71DI3; P14136: GFAP; NbExp=3; IntAct=EBI-750650, EBI-744302; CC Q71DI3; Q16695: H3-4; NbExp=2; IntAct=EBI-750650, EBI-358900; CC Q71DI3; P62805: H4C9; NbExp=4; IntAct=EBI-750650, EBI-302023; CC Q71DI3; P42858: HTT; NbExp=18; IntAct=EBI-750650, EBI-466029; CC Q71DI3; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-750650, EBI-1055254; CC Q71DI3; P02545: LMNA; NbExp=6; IntAct=EBI-750650, EBI-351935; CC Q71DI3; P02545-6: LMNA; NbExp=3; IntAct=EBI-750650, EBI-9034379; CC Q71DI3; P49321-2: NASP; NbExp=4; IntAct=EBI-750650, EBI-7038920; CC Q71DI3; P19404: NDUFV2; NbExp=3; IntAct=EBI-750650, EBI-713665; CC Q71DI3; P29474: NOS3; NbExp=3; IntAct=EBI-750650, EBI-1391623; CC Q71DI3; Q96CV9: OPTN; NbExp=3; IntAct=EBI-750650, EBI-748974; CC Q71DI3; P37840: SNCA; NbExp=3; IntAct=EBI-750650, EBI-985879; CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. CC -!- DEVELOPMENTAL STAGE: Expressed during S phase, then expression strongly CC decreases as cell division slows down during the process of CC differentiation. 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:16497732, ECO:0000269|PubMed:16627869, CC ECO:0000269|PubMed:17194708, ECO:0000269|PubMed:19520870, CC ECO:0000269|PubMed:23415232}. 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:16267050, ECO:0000269|PubMed:16497732, CC ECO:0000269|PubMed:17194708, ECO:0000269|PubMed:17898714, CC ECO:0000269|PubMed:18077460, ECO:0000269|PubMed:18079182}. CC -!- PTM: Methylation at Lys-5 (H3K4me), Lys-37 (H3K36me) and Lys-80 CC (H3K79me) are linked to gene activation. Methylation at Lys-5 (H3K4me) CC facilitates subsequent acetylation of H3 and H4. Methylation at Lys-80 CC (H3K79me) is associated with DNA double-strand break (DSB) responses CC and is a specific target for TP53BP1. Methylation at Lys-10 (H3K9me) CC and Lys-28 (H3K27me) are linked to gene repression. Methylation at Lys- CC 10 (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:16185088, CC ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16497732, CC ECO:0000269|PubMed:16627869, ECO:0000269|PubMed:17189264, CC ECO:0000269|PubMed:17194708, ECO:0000269|PubMed:22387026}. CC -!- PTM: Phosphorylated at Thr-4 (H3T3ph) by HASPIN during prophase 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. {ECO:0000269|PubMed:10464286, CC ECO:0000269|PubMed:11242053, ECO:0000269|PubMed:11856369, CC ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:15681610, CC ECO:0000269|PubMed:15684425, ECO:0000269|PubMed:16185088, CC ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16497732, CC ECO:0000269|PubMed:16627869, ECO:0000269|PubMed:17194708, CC ECO:0000269|PubMed:18066052, ECO:0000269|PubMed:19783980, CC ECO:0000269|PubMed:20228790, ECO:0000269|PubMed:22901803}. CC -!- PTM: Monoubiquitinated by RAG1 in lymphoid cells, monoubiquitination is CC required for V(D)J recombination. Ubiquitinated by the CUL4-DDB-RBX1 CC complex in response to ultraviolet irradiation. This may weaken the CC interaction between histones and DNA and facilitate DNA accessibility CC to repair proteins. {ECO:0000269|PubMed:16678110}. 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 by PARP1 or PARP2 constitutes the primary CC form of ADP-ribosylation of proteins in response to DNA damage CC (PubMed:29480802, PubMed:34874266). Serine ADP-ribosylation at Ser-11 CC (H3S10ADPr) promotes recruitment of CHD1L (PubMed:34874266). H3S10ADPr CC is mutually exclusive with phosphorylation at Ser-11 (H3S10ph) and CC impairs acetylation at Lys-10 (H3K9ac) (PubMed:30257210). CC {ECO:0000269|PubMed:29480802, ECO:0000269|PubMed:30257210, CC ECO:0000269|PubMed:34874266}. 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 -!- 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF531305; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AF531307; AAN39283.1; -; Genomic_DNA. DR EMBL; AY648851; AAT68254.1; -; Genomic_DNA. DR EMBL; AL591493; CAI12559.1; -; Genomic_DNA. DR EMBL; AL591493; CAI12561.1; -; Genomic_DNA. DR EMBL; AL591493; CAI12566.1; -; Genomic_DNA. DR EMBL; BC074969; AAH74969.2; -; mRNA. DR EMBL; BC130635; AAI30636.1; -; mRNA. DR EMBL; BC130637; AAI30638.1; -; mRNA. DR CCDS; CCDS30848.1; -. DR CCDS; CCDS30850.1; -. DR CCDS; CCDS41388.1; -. DR RefSeq; NP_001005464.1; NM_001005464.2. DR RefSeq; NP_001116847.1; NM_001123375.2. DR RefSeq; NP_066403.2; NM_021059.2. DR PDB; 2IIJ; NMR; -; B=121-136. DR PDB; 2X4W; X-ray; 1.50 A; B=23-43. DR PDB; 2X4X; X-ray; 1.85 A; B/D/F/H=23-43. DR PDB; 2X4Y; X-ray; 1.70 A; B/D/F/H/J/L/N/P=23-43. DR PDB; 3AV1; X-ray; 2.50 A; A/E=1-136. DR PDB; 3DB3; X-ray; 2.40 A; B=7-12. DR PDB; 3MO8; X-ray; 1.69 A; B=31-42. DR PDB; 3QO2; X-ray; 2.49 A; P/Q/R/S=2-16. DR PDB; 3R93; X-ray; 2.06 A; E/F/G/H=2-16. DR PDB; 4MZF; X-ray; 2.10 A; A=2-8. DR PDB; 4MZG; X-ray; 1.70 A; A/C=2-21. DR PDB; 4MZH; X-ray; 2.20 A; B=2-10. DR PDB; 4OUC; X-ray; 1.90 A; B=2-12. DR PDB; 5B0Y; X-ray; 2.56 A; A/E=1-136. DR PDB; 5B0Z; X-ray; 1.99 A; A/E=1-136. DR PDB; 5B40; X-ray; 3.33 A; A/E=1-136. DR PDB; 5BO0; X-ray; 2.91 A; A=57-136. DR PDB; 5CIU; X-ray; 2.24 A; C/D=29-43. DR PDB; 5VAC; X-ray; 1.95 A; C=19-37. DR PDB; 6ACE; X-ray; 1.98 A; B=119-126. DR PDB; 6FML; EM; 4.34 A; M/Q=2-136. DR PDB; 6T79; EM; 3.20 A; A/E=1-136. DR PDB; 6T7A; EM; 3.70 A; A/E=1-136. DR PDB; 6T7B; EM; 5.10 A; A/E=1-136. DR PDB; 6T7C; EM; 4.00 A; A/E=1-136. DR PDB; 6T7D; EM; 4.40 A; A/E=1-136. DR PDB; 6X59; EM; 2.98 A; A/E=2-136. DR PDB; 6X5A; EM; 4.36 A; A/E=2-136. DR PDB; 6XJD; EM; 6.80 A; A/E=2-136. DR PDB; 6Y5D; EM; 4.10 A; A/E/M/Q=39-136. DR PDB; 6Y5E; EM; 3.15 A; A/E=39-134. DR PDB; 7BQZ; X-ray; 3.10 A; B/D/F/H=2-16. DR PDB; 7BU9; X-ray; 3.50 A; B/D/F/H=2-16. DR PDB; 7JO9; EM; 3.30 A; A/E=1-136. DR PDB; 7JOA; EM; 3.30 A; A/E=1-136. DR PDB; 7JZV; EM; 3.90 A; P/p=2-136. DR PDB; 7PET; EM; 9.50 A; A/E/K/O/a/e/k/o=1-136. DR PDB; 7PEU; EM; 7.20 A; A/E/K/O/a/e=1-136. DR PDB; 7PEV; EM; 6.00 A; A/E/K/O=1-136. DR PDB; 7PEW; EM; 4.60 A; A/E=1-136. DR PDB; 7PEX; EM; 5.10 A; a/e=1-136. DR PDB; 7PEY; EM; 4.50 A; K/O=1-136. DR PDB; 7PEZ; EM; 7.90 A; k/o=1-136. DR PDB; 7PF0; EM; 11.00 A; A/E/K/O/a/e=1-136. DR PDB; 7PF2; EM; 5.10 A; A/E/K/O=1-136. DR PDB; 7PF3; EM; 4.00 A; k/o=1-136. DR PDB; 7PF4; EM; 4.00 A; K/O=1-136. DR PDB; 7PF5; EM; 3.80 A; a/e=1-136. DR PDB; 7PF6; EM; 4.00 A; A/E=1-136. DR PDB; 7PFA; EM; 9.70 A; A/E/K/O/a/e=1-136. DR PDB; 7PFC; EM; 6.40 A; A/E/K/O=1-136. DR PDB; 7PFD; EM; 4.40 A; A/E=1-136. DR PDB; 7PFE; EM; 4.40 A; a/e=1-136. DR PDB; 7PFF; EM; 4.30 A; K/O=1-136. DR PDB; 7PFT; EM; 9.80 A; A/E/K/O/a/e=1-136. DR PDB; 7PFU; EM; 5.00 A; A/E/K/O=1-136. DR PDB; 7PFV; EM; 4.40 A; A/E=1-136. DR PDB; 7PFW; EM; 5.20 A; a/e=1-136. DR PDB; 7PFX; EM; 4.30 A; K/O=1-136. DR PDB; 7TAN; EM; 3.00 A; A/E=2-136. DR PDB; 7U50; EM; 3.40 A; A/E=2-136. DR PDB; 7U51; EM; 3.10 A; A/E=2-136. DR PDB; 7U52; EM; 3.40 A; A/E=2-136. DR PDB; 7U53; EM; 4.00 A; A/E=2-136. DR PDB; 7UV9; EM; 3.20 A; A/E=2-136. DR PDB; 7UVA; X-ray; 1.98 A; C/F=30-42. DR PDB; 7XCR; EM; 2.57 A; A/E=38-136. DR PDB; 7XCT; EM; 2.72 A; A/E=38-136. DR PDB; 7XD0; EM; 3.48 A; A/E=38-136. DR PDB; 7YRD; EM; 3.20 A; A/E=34-136. DR PDB; 8AAG; EM; 10.00 A; A/E=1-136. DR PDB; 8ATF; EM; 3.45 A; M/Q=2-136. DR PDB; 8AV6; EM; 4.68 A; M/Q=2-136. DR PDB; 8JLB; EM; 2.36 A; A/E=2-136. DR PDB; 8JLD; EM; 2.48 A; A/E=2-136. DR PDBsum; 2IIJ; -. DR PDBsum; 2X4W; -. DR PDBsum; 2X4X; -. DR PDBsum; 2X4Y; -. DR PDBsum; 3AV1; -. DR PDBsum; 3DB3; -. DR PDBsum; 3MO8; -. DR PDBsum; 3QO2; -. DR PDBsum; 3R93; -. DR PDBsum; 4MZF; -. DR PDBsum; 4MZG; -. DR PDBsum; 4MZH; -. DR PDBsum; 4OUC; -. DR PDBsum; 5B0Y; -. DR PDBsum; 5B0Z; -. DR PDBsum; 5B40; -. DR PDBsum; 5BO0; -. DR PDBsum; 5CIU; -. DR PDBsum; 5VAC; -. DR PDBsum; 6ACE; -. DR PDBsum; 6FML; -. DR PDBsum; 6T79; -. DR PDBsum; 6T7A; -. DR PDBsum; 6T7B; -. DR PDBsum; 6T7C; -. DR PDBsum; 6T7D; -. DR PDBsum; 6X59; -. DR PDBsum; 6X5A; -. DR PDBsum; 6XJD; -. DR PDBsum; 6Y5D; -. DR PDBsum; 6Y5E; -. DR PDBsum; 7BQZ; -. DR PDBsum; 7BU9; -. DR PDBsum; 7JO9; -. DR PDBsum; 7JOA; -. DR PDBsum; 7JZV; -. DR PDBsum; 7PET; -. DR PDBsum; 7PEU; -. DR PDBsum; 7PEV; -. DR PDBsum; 7PEW; -. DR PDBsum; 7PEX; -. DR PDBsum; 7PEY; -. DR PDBsum; 7PEZ; -. DR PDBsum; 7PF0; -. DR PDBsum; 7PF2; -. DR PDBsum; 7PF3; -. DR PDBsum; 7PF4; -. DR PDBsum; 7PF5; -. DR PDBsum; 7PF6; -. DR PDBsum; 7PFA; -. DR PDBsum; 7PFC; -. DR PDBsum; 7PFD; -. DR PDBsum; 7PFE; -. DR PDBsum; 7PFF; -. DR PDBsum; 7PFT; -. DR PDBsum; 7PFU; -. DR PDBsum; 7PFV; -. DR PDBsum; 7PFW; -. DR PDBsum; 7PFX; -. DR PDBsum; 7TAN; -. DR PDBsum; 7U50; -. DR PDBsum; 7U51; -. DR PDBsum; 7U52; -. DR PDBsum; 7U53; -. DR PDBsum; 7UV9; -. DR PDBsum; 7UVA; -. DR PDBsum; 7XCR; -. DR PDBsum; 7XCT; -. DR PDBsum; 7XD0; -. DR PDBsum; 7YRD; -. DR PDBsum; 8AAG; -. DR PDBsum; 8ATF; -. DR PDBsum; 8AV6; -. DR PDBsum; 8JLB; -. DR PDBsum; 8JLD; -. DR AlphaFoldDB; Q71DI3; -. DR EMDB; EMD-10390; -. DR EMDB; EMD-10391; -. DR EMDB; EMD-10392; -. DR EMDB; EMD-10393; -. DR EMDB; EMD-10394; -. DR EMDB; EMD-10694; -. DR EMDB; EMD-10695; -. DR EMDB; EMD-11005; -. DR EMDB; EMD-11006; -. DR EMDB; EMD-13356; -. DR EMDB; EMD-13357; -. DR EMDB; EMD-13358; -. DR EMDB; EMD-13359; -. DR EMDB; EMD-13360; -. DR EMDB; EMD-13361; -. DR EMDB; EMD-13362; -. DR EMDB; EMD-13363; -. DR EMDB; EMD-13365; -. DR EMDB; EMD-13366; -. DR EMDB; EMD-13367; -. DR EMDB; EMD-13368; -. DR EMDB; EMD-13369; -. DR EMDB; EMD-13370; -. DR EMDB; EMD-13371; -. DR EMDB; EMD-13372; -. DR EMDB; EMD-13373; -. DR EMDB; EMD-13374; -. DR EMDB; EMD-13379; -. DR EMDB; EMD-13380; -. DR EMDB; EMD-13381; -. DR EMDB; EMD-13382; -. DR EMDB; EMD-13383; -. DR EMDB; EMD-15647; -. DR EMDB; EMD-22046; -. DR EMDB; EMD-22047; -. DR EMDB; EMD-22206; -. DR EMDB; EMD-22408; -. DR EMDB; EMD-22409; -. DR EMDB; EMD-22581; -. DR EMDB; EMD-25777; -. DR EMDB; EMD-25778; -. DR EMDB; EMD-26336; -. DR EMDB; EMD-26337; -. DR EMDB; EMD-26338; -. DR EMDB; EMD-26339; -. DR EMDB; EMD-26809; -. DR EMDB; EMD-26810; -. DR EMDB; EMD-33127; -. DR EMDB; EMD-33131; -. DR EMDB; EMD-34053; -. DR EMDB; EMD-34212; -. DR EMDB; EMD-36391; -. DR EMDB; EMD-36393; -. DR EMDB; EMD-4277; -. DR EMDB; EMD-4711; -. DR SMR; Q71DI3; -. DR BioGRID; 126025; 212. DR BioGRID; 130616; 104. DR BioGRID; 575920; 32. DR ComplexPortal; CPX-5668; Nucleosome, variant H3.2-H2A.2-H2B.1. DR DIP; DIP-48606N; -. DR IntAct; Q71DI3; 109. DR MINT; Q71DI3; -. DR STRING; 9606.ENSP00000333277; -. DR ChEMBL; CHEMBL4295875; -. DR GlyGen; Q71DI3; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q71DI3; -. DR MetOSite; Q71DI3; -. DR PhosphoSitePlus; Q71DI3; -. DR SwissPalm; Q71DI3; -. DR BioMuta; HIST2H3C; -. DR DMDM; 74758899; -. DR EPD; Q71DI3; -. DR jPOST; Q71DI3; -. DR MassIVE; Q71DI3; -. DR MaxQB; Q71DI3; -. DR PaxDb; 9606-ENSP00000333277; -. DR PeptideAtlas; Q71DI3; -. DR ProteomicsDB; 68597; -. DR Pumba; Q71DI3; -. DR TopDownProteomics; Q71DI3; -. DR Antibodypedia; 53833; 412 antibodies from 16 providers. DR Antibodypedia; 68017; 158 antibodies from 10 providers. DR Antibodypedia; 73939; 1496 antibodies from 6 providers. DR DNASU; 126961; -. DR Ensembl; ENST00000331491.2; ENSP00000333277.2; ENSG00000183598.4. DR Ensembl; ENST00000369158.2; ENSP00000358154.1; ENSG00000203811.2. DR Ensembl; ENST00000403683.2; ENSP00000385479.1; ENSG00000203852.4. DR GeneID; 126961; -. DR GeneID; 333932; -. DR GeneID; 653604; -. DR KEGG; hsa:126961; -. DR KEGG; hsa:333932; -. DR KEGG; hsa:653604; -. DR MANE-Select; ENST00000331491.2; ENSP00000333277.2; NM_001123375.3; NP_001116847.1. DR MANE-Select; ENST00000369158.2; ENSP00000358154.1; NM_021059.3; NP_066403.2. DR MANE-Select; ENST00000403683.2; ENSP00000385479.1; NM_001005464.3; NP_001005464.1. DR UCSC; uc001esv.4; human. DR AGR; HGNC:20503; -. DR AGR; HGNC:20505; -. DR AGR; HGNC:25311; -. DR CTD; 126961; -. DR CTD; 333932; -. DR CTD; 653604; -. DR DisGeNET; 126961; -. DR DisGeNET; 333932; -. DR DisGeNET; 653604; -. DR GeneCards; H3C13; -. DR GeneCards; H3C14; -. DR GeneCards; H3C15; -. DR HGNC; HGNC:25311; H3C13. DR HGNC; HGNC:20503; H3C14. DR HGNC; HGNC:20505; H3C15. DR HPA; ENSG00000183598; Tissue enhanced (bone). DR HPA; ENSG00000203811; Tissue enhanced (brain). DR HPA; ENSG00000203852; Tissue enhanced (bone). DR MIM; 142780; gene. DR neXtProt; NX_Q71DI3; -. DR OpenTargets; ENSG00000183598; -. DR OpenTargets; ENSG00000203811; -. DR VEuPathDB; HostDB:ENSG00000183598; -. DR VEuPathDB; HostDB:ENSG00000203811; -. DR VEuPathDB; HostDB:ENSG00000203852; -. DR eggNOG; KOG1745; Eukaryota. DR GeneTree; ENSGT01100000263559; -. DR HOGENOM; CLU_078295_4_0_1; -. DR InParanoid; Q71DI3; -. DR OMA; FLPMART; -. DR OrthoDB; 4687963at2759; -. DR PhylomeDB; Q71DI3; -. DR TreeFam; TF314241; -. DR PathwayCommons; Q71DI3; -. DR Reactome; R-HSA-1266695; Interleukin-7 signaling. 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-3214815; HDACs deacetylate histones. DR Reactome; R-HSA-3214841; PKMTs methylate histone lysines. DR Reactome; R-HSA-3214842; HDMs demethylate histones. DR Reactome; R-HSA-3214847; HATs acetylate histones. DR Reactome; R-HSA-3214858; RMTs methylate histone arginines. DR Reactome; R-HSA-3247509; Chromatin modifying enzymes. DR Reactome; R-HSA-427359; SIRT1 negatively regulates rRNA expression. DR Reactome; R-HSA-427389; ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression. DR Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression. DR Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression. DR Reactome; R-HSA-5334118; DNA methylation. DR Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs. DR Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis. DR Reactome; R-HSA-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3. DR Reactome; R-HSA-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-9609690; HCMV Early Events. DR Reactome; R-HSA-9610379; HCMV Late Events. DR Reactome; R-HSA-9616222; Transcriptional regulation of granulopoiesis. DR Reactome; R-HSA-9710421; Defective pyroptosis. DR Reactome; R-HSA-977225; Amyloid fiber formation. DR Reactome; R-HSA-9821002; Chromatin modifications during the maternal to zygotic transition (MZT). DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production. DR SignaLink; Q71DI3; -. DR SIGNOR; Q71DI3; -. DR BioGRID-ORCS; 126961; 322 hits in 639 CRISPR screens. DR BioGRID-ORCS; 333932; 489 hits in 985 CRISPR screens. DR BioGRID-ORCS; 653604; 683 hits in 1055 CRISPR screens. DR ChiTaRS; HIST2H3C; human. DR EvolutionaryTrace; Q71DI3; -. DR GeneWiki; HIST2H3C; -. DR Pharos; Q71DI3; Tbio. DR PRO; PR:Q71DI3; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q71DI3; Protein. DR Bgee; ENSG00000183598; Expressed in bone marrow cell and 94 other cell types or tissues. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0000786; C:nucleosome; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro. DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro. DR GO; GO:0006325; P:chromatin organization; NAS:ComplexPortal. DR GO; GO:0006334; P:nucleosome assembly; IDA:UniProtKB. DR Gene3D; 1.10.20.10; Histone, subunit A; 1. DR IDEAL; IID00088; -. DR InterPro; IPR009072; Histone-fold. DR InterPro; IPR007125; Histone_H2A/H2B/H3. DR InterPro; IPR000164; Histone_H3/CENP-A. DR PANTHER; PTHR11426; HISTONE H3; 1. DR PANTHER; PTHR11426:SF274; HISTONE H3.1T; 1. DR Pfam; PF00125; Histone; 1. DR PRINTS; PR00622; HISTONEH3. DR SMART; SM00428; H3; 1. DR SUPFAM; SSF47113; Histone-fold; 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; DNA-binding; Hydroxylation; Lipoprotein; KW Methylation; Nucleosome core; Nucleus; Palmitate; Phosphoprotein; KW Reference proteome; Ubl conjugation. FT CHAIN 1..136 FT /note="Histone H3.2" FT /id="PRO_0000250357" FT REGION 1..43 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" 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:16267050, FT ECO:0000269|PubMed:17194708" FT MOD_RES 5 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000269|PubMed:16267050, 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:16267050, 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:P84228" 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:17194708" 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:17194708" 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:16497732, FT ECO:0000269|PubMed:16627869, 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:17194708" FT MOD_RES 11 FT /note="ADP-ribosylserine; alternate" FT /evidence="ECO:0000269|PubMed:28190768, FT ECO:0000269|PubMed:29480802, ECO:0000269|PubMed:34874266" 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: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:16627869, ECO:0000269|PubMed:17194708" 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:P84228" 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:16627869, ECO:0000269|PubMed:17194708, FT ECO:0000269|PubMed:35939806" 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:16627869, ECO:0000269|PubMed:17194708" 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:16627869, FT ECO:0000269|PubMed:17194708" FT MOD_RES 28 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000269|PubMed:16185088, FT ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16627869, FT ECO:0000269|PubMed:17194708" 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:16627869, ECO:0000269|PubMed:17194708" 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:16627869, FT ECO:0000269|PubMed:17194708" 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: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:16627869, FT ECO:0000269|PubMed:17194708" FT MOD_RES 37 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000269|PubMed:16185088, FT ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16627869, FT ECO:0000269|PubMed:17194708" 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:16627869, FT ECO:0000269|PubMed:17194708" 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:P84228" 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:P84228" FT MOD_RES 80 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000269|PubMed:15525939, FT ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16627869, FT 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:16627869, FT 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:0000250|UniProtKB:P84243" FT MOD_RES 108 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332" 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 LIPID 19 FT /note="N6-decanoyllysine" FT /evidence="ECO:0000269|PubMed:35939806" FT LIPID 111 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000269|PubMed:21076176" FT VARIANT 91 FT /note="M -> T (in dbSNP:rs2664732)" FT /id="VAR_059313" FT VARIANT 128 FT /note="A -> V (in dbSNP:rs2664731)" FT /id="VAR_059314" FT MUTAGEN 111 FT /note="C->A: Abolishes S-palmitoylation." FT /evidence="ECO:0000269|PubMed:21076176" FT STRAND 7..9 FT /evidence="ECO:0007829|PDB:3R93" FT HELIX 26..29 FT /evidence="ECO:0007829|PDB:2X4Y" FT STRAND 32..34 FT /evidence="ECO:0007829|PDB:5VAC" FT HELIX 46..57 FT /evidence="ECO:0007829|PDB:5B0Z" FT HELIX 65..77 FT /evidence="ECO:0007829|PDB:5B0Z" FT STRAND 80..82 FT /evidence="ECO:0007829|PDB:5B0Y" FT HELIX 87..114 FT /evidence="ECO:0007829|PDB:5B0Z" FT STRAND 118..120 FT /evidence="ECO:0007829|PDB:5B0Z" FT STRAND 123..125 FT /evidence="ECO:0007829|PDB:6ACE" SQ SEQUENCE 136 AA; 15388 MW; 6FD8508EA50A0EEC CRC64; MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEASEAY LVGLFEDTNL CAIHAKRVTI MPKDIQLARR IRGERA //