H32_HUMAN
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 03-AUG-2022, entry version 191.
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=10.1006/geno.2002.6850;
RA Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.;
RT "The human and mouse replication-dependent histone genes.";
RL Genomics 80:487-498(2002).
RN [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 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 [37]
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 [38]
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 [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 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 [56]
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 [57] {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 [58] {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 [59] {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 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 -!- 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}.
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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 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 AlphaFoldDB; Q71DI3; -.
DR SMR; Q71DI3; -.
DR BioGRID; 126025; 199.
DR BioGRID; 130616; 85.
DR BioGRID; 575920; 27.
DR ComplexPortal; CPX-5668; Nucleosome, variant H3.2-H2A.2-H2B.1.
DR DIP; DIP-48606N; -.
DR IntAct; Q71DI3; 105.
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; Q71DI3; -.
DR PeptideAtlas; Q71DI3; -.
DR PRIDE; Q71DI3; -.
DR ProteomicsDB; 68597; -.
DR TopDownProteomics; Q71DI3; -.
DR Antibodypedia; 53833; 184 antibodies from 15 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 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 (brain).
DR HPA; ENSG00000203811; Tissue enriched (brain).
DR HPA; ENSG00000203852; Tissue enriched (brain).
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; ENSGT01050000244889; -.
DR HOGENOM; CLU_078295_4_0_1; -.
DR InParanoid; Q71DI3; -.
DR OMA; LARRIXS; -.
DR OrthoDB; 1564596at2759; -.
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-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; Q71DI3; -.
DR SIGNOR; Q71DI3; -.
DR BioGRID-ORCS; 126961; 315 hits in 603 CRISPR screens.
DR BioGRID-ORCS; 333932; 478 hits in 931 CRISPR screens.
DR BioGRID-ORCS; 653604; 676 hits in 1004 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 93 other 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; TAS:Reactome.
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:0006334; P:nucleosome assembly; IDA:UniProtKB.
DR Gene3D; 1.10.20.10; -; 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; 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; 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"
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 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 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
