Full text data of HIST2H3A
HIST2H3A
(H3F2, H3FM)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Histone H3.2 (Histone H3/m; Histone H3/o)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Histone H3.2 (Histone H3/m; Histone H3/o)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q71DI3
ID H32_HUMAN Reviewed; 136 AA.
AC Q71DI3; A2BDF6; A6NFS4; Q6B053;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 116.
DE RecName: Full=Histone H3.2;
DE AltName: Full=Histone H3/m;
DE AltName: Full=Histone H3/o;
GN Name=HIST2H3A;
GN and
GN Name=HIST2H3C; Synonyms=H3F2, H3FM;
GN and
GN Name=HIST2H3D;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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.,
RA Stein G.S.;
RT "Functional characterization of a human histone gene cluster
RT 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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
RT project: 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 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.,
RA Okawa K., Iwamatsu A., Okigaki T., Takahashi T., Inagaki M.;
RT "Identification of a novel phosphorylation site on histone H3 coupled
RT with mitotic chromosome condensation.";
RL J. Biol. Chem. 274:25543-25549(1999).
RN [7]
RP PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Spleen;
RX PubMed=7309716;
RA Ohe Y., Iwai K.;
RT "Human spleen histone H3. Isolation and amino acid sequence.";
RL J. Biochem. 90:1205-1211(1981).
RN [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
RT mitotic 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
RT mediated by 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.,
RA Walsh M.J.;
RT "Ligand-dependent activation of the farnesoid X-receptor directs
RT arginine methylation of histone H3 by CARM1.";
RL J. Biol. Chem. 279:54348-54357(2004).
RN [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.,
RA Halazonetis T.D.;
RT "Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand
RT breaks.";
RL Nature 432:406-411(2004).
RN [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.,
RA Clarke S., Stallcup M.R., Allis C.D., Coonrod S.A.;
RT "Human PAD4 regulates histone arginine methylation levels via
RT demethylimination.";
RL Science 306:279-283(2004).
RN [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
RT phosphorylation 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
RT kinase-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
RP AT LYS-5; LYS-10; LYS-19; LYS-28; LYS-37; LYS-65; LYS-80 AND LYS-123,
RP AND MASS SPECTROMETRY.
RX PubMed=16267050; DOI=10.1074/jbc.M509266200;
RA Hake S.B., Garcia B.A., Duncan E.M., Kauer M., Dellaire G.,
RA Shabanowitz J., Bazett-Jones D.P., Allis C.D., Hunt D.F.;
RT "Expression patterns and post-translational modifications associated
RT with mammalian histone H3 variants.";
RL J. Biol. Chem. 281:559-568(2006).
RN [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
RT ligase 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
RP AT LYS-28; LYS-37 AND LYS-80, AND MASS SPECTROMETRY.
RX PubMed=16627869; DOI=10.1074/mcp.M600007-MCP200;
RA Beck H.C., Nielsen E.C., Matthiesen R., Jensen L.H., Sehested M.,
RA Finn P., Grauslund M., Hansen A.M., Jensen O.N.;
RT "Quantitative proteomic analysis of post-translational modifications
RT of human histones.";
RL Mol. Cell. Proteomics 5:1314-1325(2006).
RN [19]
RP ACETYLATION AT LYS-10 AND LYS-15, METHYLATION AT ARG-18, AND
RP CITRULLINATION AT ARG-18.
RX PubMed=16497732; DOI=10.1210/me.2005-0365;
RA Miao F., Li S., Chavez V., Lanting L., Natarajan R.;
RT "Coactivator-associated arginine methyltransferase-1 enhances nuclear
RT factor-kappaB-mediated gene transcription through methylation of
RT histone H3 at arginine 17.";
RL Mol. Endocrinol. 20:1562-1573(2006).
RN [20]
RP METHYLATION AT ARG-3 BY PRMT6.
RX PubMed=18079182; DOI=10.1101/gad.447007;
RA Hyllus D., Stein C., Schnabel K., Schiltz E., Imhof A., Dou Y.,
RA Hsieh J., Bauer U.M.;
RT "PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4
RT trimethylation.";
RL Genes Dev. 21:3369-3380(2007).
RN [21]
RP ACETYLATION AT LYS-5; LYS-10; LYS-15; LYS-19; LYS-24; LYS-28; LYS-37;
RP LYS-57 AND LYS-80, METHYLATION AT LYS-5; LYS-10; LYS-19; LYS-24;
RP LYS-28; LYS-37; LYS-57; LYS-65; LYS-80 AND LYS-123, AND 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
RT histones H3 and H4.";
RL J. Biol. Chem. 282:7641-7655(2007).
RN [22]
RP ACETYLATION AT LYS-37.
RX PubMed=17189264; DOI=10.1074/jbc.M607909200;
RA Morris S.A., Rao B., Garcia B.A., Hake S.B., Diaz R.L.,
RA Shabanowitz J., Hunt D.F., Allis C.D., Lieb J.D., Strahl B.D.;
RT "Identification of histone H3 lysine 36 acetylation as a highly
RT conserved histone modification.";
RL J. Biol. Chem. 282:7632-7640(2007).
RN [23]
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 [24]
RP METHYLATION AT ARG-3 BY PRMT6.
RX PubMed=18077460; DOI=10.1074/jbc.C700192200;
RA Iberg A.N., Espejo A., Cheng D., Kim D., Michaud-Levesque J.,
RA Richard S., Bedford M.T.;
RT "Arginine methylation of the histone H3 tail impedes effector
RT binding.";
RL J. Biol. Chem. 283:3006-3010(2008).
RN [25]
RP PHOSPHORYLATION AT THR-12.
RX PubMed=18066052; DOI=10.1038/ncb1668;
RA Metzger E., Yin N., Wissmann M., Kunowska N., Fischer K.,
RA Friedrichs N., Patnaik D., Higgins J.M., Potier N., Scheidtmann K.H.,
RA Buettner R., Schule R.;
RT "Phosphorylation of histone H3 at threonine 11 establishes a novel
RT chromatin mark for transcriptional regulation.";
RL Nat. Cell Biol. 10:53-60(2008).
RN [26]
RP ACETYLATION AT LYS-116 AND LYS-123.
RX PubMed=19520870; DOI=10.1074/jbc.M109.003202;
RA Manohar M., Mooney A.M., North J.A., Nakkula R.J., Picking J.W.,
RA Edon A., Fishel R., Poirier M.G., Ottesen J.J.;
RT "Acetylation of histone H3 at the nucleosome dyad alters DNA-histone
RT binding.";
RL J. Biol. Chem. 284:23312-23321(2009).
RN [27]
RP PHOSPHORYLATION AT TYR-42.
RX PubMed=19783980; DOI=10.1038/nature08448;
RA Dawson M.A., Bannister A.J., Gottgens B., Foster S.D., Bartke T.,
RA Green A.R., Kouzarides T.;
RT "JAK2 phosphorylates histone H3Y41 and excludes HP1alpha from
RT chromatin.";
RL Nature 461:819-822(2009).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-108, AND MASS
RP SPECTROMETRY.
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 [29]
RP PHOSPHORYLATION AT SER-58 AND THR-81.
RX PubMed=20850016; DOI=10.1016/j.cell.2010.08.020;
RA Vermeulen M., Eberl H.C., Matarese F., Marks H., Denissov S.,
RA Butter F., Lee K.K., Olsen J.V., Hyman A.A., Stunnenberg H.G.,
RA Mann M.;
RT "Quantitative interaction proteomics and genome-wide profiling of
RT epigenetic histone marks and their readers.";
RL Cell 142:967-980(2010).
RN [30]
RP PHOSPHORYLATION AT THR-7.
RX PubMed=20228790; DOI=10.1038/nature08839;
RA Metzger E., Imhof A., Patel D., Kahl P., Hoffmeyer K., Friedrichs N.,
RA Muller J.M., Greschik H., Kirfel J., Ji S., Kunowska N.,
RA Beisenherz-Huss C., Gunther T., Buettner R., Schule R.;
RT "Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation
RT at histone H3K4.";
RL Nature 464:792-796(2010).
RN [31]
RP CROTONYLATION AT LYS-5; LYS-10; LYS-19; LYS-24; LYS-28 AND LYS-57.
RX PubMed=21925322; DOI=10.1016/j.cell.2011.08.008;
RA Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T.,
RA Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q.,
RA Wysocka J., Ye Y., Khochbin S., Ren B., Zhao Y.;
RT "Identification of 67 histone marks and histone lysine crotonylation
RT as a new type of histone modification.";
RL Cell 146:1016-1028(2011).
RN [32]
RP METHYLATION AT LYS-57.
RX PubMed=22387026; DOI=10.1016/j.molcel.2012.01.019;
RA Yu Y., Song C., Zhang Q., Dimaggio P.A., Garcia B.A., York A.,
RA Carey M.F., Grunstein M.;
RT "Histone H3 lysine 56 methylation regulates DNA replication through
RT its interaction with PCNA.";
RL Mol. Cell 46:7-17(2012).
RN [33]
RP ALLYSINE AT LYS-5.
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 [34]
RP ACETYLATION AT LYS-123.
RX PubMed=23415232; DOI=10.1016/j.cell.2013.01.032;
RA Tropberger P., Pott S., Keller C., Kamieniarz-Gdula K., Caron M.,
RA Richter F., Li G., Mittler G., Liu E.T., Buhler M., Margueron R.,
RA Schneider R.;
RT "Regulation of transcription through acetylation of H3K122 on the
RT lateral surface of the histone octamer.";
RL Cell 152:859-872(2013).
RN [35]
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.,
RA Mann C., Ochsenbein F.;
RT "Structure of the histone chaperone ASF1 bound to the histone H3 C-
RT terminal helix and functional insights.";
RL Structure 15:191-199(2007).
CC -!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and
CC compact DNA into chromatin, limiting DNA accessibility to the
CC cellular machineries which require DNA as a template. Histones
CC thereby play a central role in transcription regulation, DNA
CC repair, DNA replication and chromosomal stability. DNA
CC accessibility is regulated via a complex set of post-translational
CC modifications of histones, also called histone code, and
CC nucleosome remodeling.
CC -!- SUBUNIT: The nucleosome is a histone octamer containing two
CC molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4
CC heterotetramer and two H2A-H2B heterodimers. The octamer wraps
CC approximately 147 bp of DNA. During nucleosome assembly the
CC chaperone ASF1A interacts with the histone H3-H4 heterodimer.
CC -!- INTERACTION:
CC Q12830-4:BPTF; NbExp=2; IntAct=EBI-750650, EBI-4288838;
CC P02545:LMNA; NbExp=6; IntAct=EBI-750650, EBI-351935;
CC Q6UYC3:LMNA; NbExp=3; IntAct=EBI-750650, EBI-8042626;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- DEVELOPMENTAL STAGE: Expressed during S phase, then expression
CC strongly decreases as cell division slows down during the process
CC of differentiation.
CC -!- PTM: Acetylation is generally linked to gene activation.
CC Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9
CC (H3R8me2s). Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac)
CC favors methylation at Arg-18 (H3R17me). Acetylation at Lys-123
CC (H3K122ac) by EP300/p300 plays a central role in chromatin
CC structure: localizes at the surface of the histone octamer and
CC stimulates transcription, possibly by promoting nucleosome
CC instability.
CC -!- PTM: Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by
CC PADI4 impairs methylation and represses transcription.
CC -!- PTM: Asymmetric dimethylation at Arg-18 (H3R17me2a) by CARM1 is
CC linked to gene activation. Symmetric dimethylation at Arg-9
CC (H3R8me2s) by PRMT5 is linked to gene repression. Asymmetric
CC dimethylation at Arg-3 (H3R2me2a) by PRMT6 is linked to gene
CC repression and is mutually exclusive with H3 Lys-5 methylation
CC (H3K4me2 and H3K4me3). H3R2me2a is present at the 3' of genes
CC regardless of their transcription state and is enriched on
CC inactive promoters, while it is absent on active promoters.
CC -!- PTM: Methylation at Lys-5 (H3K4me), Lys-37 (H3K36me) and Lys-80
CC (H3K79me) are linked to gene activation. Methylation at Lys-5
CC (H3K4me) facilitates subsequent acetylation of H3 and H4.
CC Methylation at Lys-80 (H3K79me) is associated with DNA double-
CC strand break (DSB) responses and is a specific target for TP53BP1.
CC Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are linked to
CC gene repression. Methylation at Lys-10 (H3K9me) is a specific
CC target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents
CC subsequent phosphorylation at Ser-11 (H3S10ph) and acetylation of
CC H3 and H4. Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me)
CC require preliminary monoubiquitination of H2B at 'Lys-120'.
CC Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched
CC in inactive X chromosome chromatin. Monomethylation at Lys-57
CC (H3K56me1) by EHMT2/G9A in G1 phase promotes interaction with PCNA
CC and is required for DNA replication.
CC -!- PTM: Phosphorylated at Thr-4 (H3T3ph) by GSG2/haspin during
CC prophase and dephosphorylated during anaphase. Phosphorylation at
CC Ser-11 (H3S10ph) by AURKB is crucial for chromosome condensation
CC and cell-cycle progression during mitosis and meiosis. In addition
CC phosphorylation at Ser-11 (H3S10ph) by RPS6KA4 and RPS6KA5 is
CC important during interphase because it enables the transcription
CC of genes following external stimulation, like mitogens, stress,
CC growth factors or UV irradiation and result in the activation of
CC genes, such as c-fos and c-jun. Phosphorylation at Ser-11
CC (H3S10ph), which is linked to gene activation, prevents
CC methylation at Lys-10 (H3K9me) but facilitates acetylation of H3
CC and H4. Phosphorylation at Ser-11 (H3S10ph) by AURKB mediates the
CC dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from
CC heterochromatin. Phosphorylation at Ser-11 (H3S10ph) is also an
CC essential regulatory mechanism for neoplastic cell transformation.
CC Phosphorylated at Ser-29 (H3S28ph) by MLTK isoform 1, RPS6KA5 or
CC AURKB during mitosis or upon ultraviolet B irradiation.
CC Phosphorylation at Thr-7 (H3T6ph) by PRKCB is a specific tag for
CC epigenetic transcriptional activation that prevents demethylation
CC of Lys-5 (H3K4me) by LSD1/KDM1A. At centromeres, specifically
CC phosphorylated at Thr-12 (H3T11ph) from prophase to early
CC anaphase, by DAPK3 and PKN1. Phosphorylation at Thr-12 (H3T11ph)
CC by PKN1 is a specific tag for epigenetic transcriptional
CC activation that promotes demethylation of Lys-10 (H3K9me) by
CC KDM4C/JMJD2C. Phosphorylation at Tyr-42 (H3Y41ph) by JAK2 promotes
CC exclusion of CBX5 (HP1 alpha) from chromatin.
CC -!- PTM: Monoubiquitinated by RAG1 in lymphoid cells,
CC monoubiquitination is required for V(D)J recombination (By
CC similarity). Ubiquitinated by the CUL4-DDB-RBX1 complex in
CC response to ultraviolet irradiation. This may weaken the
CC interaction between histones and DNA and facilitate DNA
CC accessibility to repair proteins.
CC -!- PTM: Lysine deamination at Lys-5 (H3K4all) to form allysine is
CC mediated by LOXL2. Allysine formation by LOXL2 only takes place on
CC H3K4me3 and results in gene repression (PubMed:22483618).
CC -!- PTM: Crotonylation (Kcr) is specifically present in male germ
CC cells and marks testis-specific genes in post-meiotic cells,
CC including X-linked genes that escape sex chromosome inactivation
CC in haploid cells. Crotonylation marks active promoters and
CC enhancers and confers resistance to transcriptional repressors. It
CC is also associated with post-meiotically activated genes on
CC autosomes.
CC -!- SIMILARITY: Belongs to the histone H3 family.
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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 RefSeq; NP_001005464.1; NM_001005464.2.
DR RefSeq; NP_001116847.1; NM_001123375.2.
DR RefSeq; NP_066403.2; NM_021059.2.
DR UniGene; Hs.647745; -.
DR UniGene; Hs.706618; -.
DR UniGene; Hs.712062; -.
DR PDB; 2IIJ; NMR; -; B=123-136.
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 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 ProteinModelPortal; Q71DI3; -.
DR SMR; Q71DI3; 17-136.
DR DIP; DIP-48606N; -.
DR IntAct; Q71DI3; 9.
DR MINT; MINT-4828325; -.
DR STRING; 9606.ENSP00000333277; -.
DR PhosphoSite; Q71DI3; -.
DR PaxDb; Q71DI3; -.
DR PRIDE; Q71DI3; -.
DR DNASU; 126961; -.
DR Ensembl; ENST00000331491; ENSP00000333277; ENSG00000183598.
DR Ensembl; ENST00000369158; ENSP00000358154; ENSG00000203811.
DR Ensembl; ENST00000403683; ENSP00000385479; ENSG00000203852.
DR Ensembl; ENST00000578851; ENSP00000463798; ENSG00000265133.
DR Ensembl; ENST00000580481; ENSP00000463420; ENSG00000270263.
DR Ensembl; ENST00000585113; ENSP00000463995; ENSG00000270827.
DR GeneID; 126961; -.
DR GeneID; 333932; -.
DR GeneID; 653604; -.
DR KEGG; hsa:126961; -.
DR KEGG; hsa:333932; -.
DR KEGG; hsa:653604; -.
DR UCSC; uc001esv.3; human.
DR CTD; 126961; -.
DR CTD; 333932; -.
DR CTD; 653604; -.
DR GeneCards; GC01M149784; -.
DR GeneCards; GC01M149812; -.
DR GeneCards; GC01P149824; -.
DR HGNC; HGNC:20505; HIST2H3A.
DR HGNC; HGNC:20503; HIST2H3C.
DR HGNC; HGNC:25311; HIST2H3D.
DR HPA; HPA042570; -.
DR MIM; 142780; gene.
DR neXtProt; NX_Q71DI3; -.
DR PharmGKB; PA145148728; -.
DR eggNOG; COG2036; -.
DR HOGENOM; HOG000155290; -.
DR HOVERGEN; HBG001172; -.
DR InParanoid; Q71DI3; -.
DR KO; K11253; -.
DR OMA; RISKMAR; -.
DR OrthoDB; EOG7HB5C2; -.
DR Reactome; REACT_111183; Meiosis.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_120956; Cellular responses to stress.
DR Reactome; REACT_604; Hemostasis.
DR ChiTaRS; HIST2H3C; human.
DR EvolutionaryTrace; Q71DI3; -.
DR GeneWiki; HIST2H3C; -.
DR NextBio; 81962; -.
DR Bgee; Q71DI3; -.
DR CleanEx; HS_HIST2H3A; -.
DR CleanEx; HS_HIST2H3C; -.
DR CleanEx; HS_HIST2H3D; -.
DR Genevestigator; Q71DI3; -.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0007596; P:blood coagulation; TAS:Reactome.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_core_D.
DR InterPro; IPR000164; Histone_H3.
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; Chromosome; Citrullination;
KW Complete proteome; Direct protein sequencing; DNA-binding;
KW Methylation; Nucleosome core; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 136 Histone H3.2.
FT /FTId=PRO_0000250357.
FT MOD_RES 3 3 Asymmetric dimethylarginine; by PRMT6.
FT MOD_RES 4 4 Phosphothreonine; by GSG2.
FT MOD_RES 5 5 Allysine; alternate.
FT MOD_RES 5 5 N6,N6,N6-trimethyllysine; alternate.
FT MOD_RES 5 5 N6,N6-dimethyllysine; alternate.
FT MOD_RES 5 5 N6-acetyllysine; alternate.
FT MOD_RES 5 5 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 5 5 N6-methyllysine; alternate.
FT MOD_RES 7 7 Phosphothreonine; by PKC.
FT MOD_RES 9 9 Citrulline; alternate.
FT MOD_RES 9 9 Symmetric dimethylarginine; by PRMT5;
FT alternate (By similarity).
FT MOD_RES 10 10 N6,N6,N6-trimethyllysine; alternate.
FT MOD_RES 10 10 N6,N6-dimethyllysine; alternate.
FT MOD_RES 10 10 N6-acetyllysine; alternate.
FT MOD_RES 10 10 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 10 10 N6-methyllysine; alternate.
FT MOD_RES 11 11 Phosphoserine; by AURKB, AURKC, RPS6KA3,
FT RPS6KA4 and RPS6KA5.
FT MOD_RES 12 12 Phosphothreonine; by PKC.
FT MOD_RES 15 15 N6-acetyllysine.
FT MOD_RES 18 18 Asymmetric dimethylarginine; by CARM1;
FT alternate.
FT MOD_RES 18 18 Citrulline; alternate.
FT MOD_RES 19 19 N6-acetyllysine; alternate.
FT MOD_RES 19 19 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 19 19 N6-methyllysine; alternate.
FT MOD_RES 24 24 N6-acetyllysine; alternate.
FT MOD_RES 24 24 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 24 24 N6-methyllysine; alternate.
FT MOD_RES 28 28 N6,N6,N6-trimethyllysine; alternate.
FT MOD_RES 28 28 N6,N6-dimethyllysine; alternate.
FT MOD_RES 28 28 N6-acetyllysine; alternate.
FT MOD_RES 28 28 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 28 28 N6-methyllysine; alternate.
FT MOD_RES 29 29 Phosphoserine; by AURKB, AURKC and
FT RPS6KA5.
FT MOD_RES 37 37 N6,N6,N6-trimethyllysine; alternate.
FT MOD_RES 37 37 N6,N6-dimethyllysine; alternate.
FT MOD_RES 37 37 N6-acetyllysine; alternate.
FT MOD_RES 37 37 N6-methyllysine; alternate.
FT MOD_RES 38 38 N6-methyllysine (By similarity).
FT MOD_RES 42 42 Phosphotyrosine.
FT MOD_RES 57 57 N6,N6,N6-trimethyllysine; alternate.
FT MOD_RES 57 57 N6-acetyllysine; alternate.
FT MOD_RES 57 57 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 57 57 N6-methyllysine; by EHMT2; alternate.
FT MOD_RES 58 58 Phosphoserine.
FT MOD_RES 65 65 N6-methyllysine.
FT MOD_RES 80 80 N6,N6,N6-trimethyllysine; alternate (By
FT similarity).
FT MOD_RES 80 80 N6,N6-dimethyllysine; alternate.
FT MOD_RES 80 80 N6-acetyllysine; alternate.
FT MOD_RES 80 80 N6-methyllysine; alternate.
FT MOD_RES 81 81 Phosphothreonine.
FT MOD_RES 108 108 Phosphothreonine.
FT MOD_RES 116 116 N6-acetyllysine.
FT MOD_RES 123 123 N6-acetyllysine; alternate.
FT MOD_RES 123 123 N6-methyllysine; alternate.
FT VARIANT 91 91 M -> T (in dbSNP:rs2664732).
FT /FTId=VAR_059313.
FT VARIANT 128 128 A -> V (in dbSNP:rs2664731).
FT /FTId=VAR_059314.
FT STRAND 7 9
FT HELIX 26 29
FT TURN 39 41
FT HELIX 46 57
FT HELIX 65 77
FT HELIX 87 114
FT STRAND 118 120
FT HELIX 122 131
SQ SEQUENCE 136 AA; 15388 MW; 6FD8508EA50A0EEC CRC64;
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE
LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEASEAY LVGLFEDTNL CAIHAKRVTI
MPKDIQLARR IRGERA
//
ID H32_HUMAN Reviewed; 136 AA.
AC Q71DI3; A2BDF6; A6NFS4; Q6B053;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 116.
DE RecName: Full=Histone H3.2;
DE AltName: Full=Histone H3/m;
DE AltName: Full=Histone H3/o;
GN Name=HIST2H3A;
GN and
GN Name=HIST2H3C; Synonyms=H3F2, H3FM;
GN and
GN Name=HIST2H3D;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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.,
RA Stein G.S.;
RT "Functional characterization of a human histone gene cluster
RT 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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
RT project: 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 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.,
RA Okawa K., Iwamatsu A., Okigaki T., Takahashi T., Inagaki M.;
RT "Identification of a novel phosphorylation site on histone H3 coupled
RT with mitotic chromosome condensation.";
RL J. Biol. Chem. 274:25543-25549(1999).
RN [7]
RP PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Spleen;
RX PubMed=7309716;
RA Ohe Y., Iwai K.;
RT "Human spleen histone H3. Isolation and amino acid sequence.";
RL J. Biochem. 90:1205-1211(1981).
RN [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
RT mitotic 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
RT mediated by 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.,
RA Walsh M.J.;
RT "Ligand-dependent activation of the farnesoid X-receptor directs
RT arginine methylation of histone H3 by CARM1.";
RL J. Biol. Chem. 279:54348-54357(2004).
RN [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.,
RA Halazonetis T.D.;
RT "Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand
RT breaks.";
RL Nature 432:406-411(2004).
RN [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.,
RA Clarke S., Stallcup M.R., Allis C.D., Coonrod S.A.;
RT "Human PAD4 regulates histone arginine methylation levels via
RT demethylimination.";
RL Science 306:279-283(2004).
RN [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
RT phosphorylation 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
RT kinase-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
RP AT LYS-5; LYS-10; LYS-19; LYS-28; LYS-37; LYS-65; LYS-80 AND LYS-123,
RP AND MASS SPECTROMETRY.
RX PubMed=16267050; DOI=10.1074/jbc.M509266200;
RA Hake S.B., Garcia B.A., Duncan E.M., Kauer M., Dellaire G.,
RA Shabanowitz J., Bazett-Jones D.P., Allis C.D., Hunt D.F.;
RT "Expression patterns and post-translational modifications associated
RT with mammalian histone H3 variants.";
RL J. Biol. Chem. 281:559-568(2006).
RN [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
RT ligase 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
RP AT LYS-28; LYS-37 AND LYS-80, AND MASS SPECTROMETRY.
RX PubMed=16627869; DOI=10.1074/mcp.M600007-MCP200;
RA Beck H.C., Nielsen E.C., Matthiesen R., Jensen L.H., Sehested M.,
RA Finn P., Grauslund M., Hansen A.M., Jensen O.N.;
RT "Quantitative proteomic analysis of post-translational modifications
RT of human histones.";
RL Mol. Cell. Proteomics 5:1314-1325(2006).
RN [19]
RP ACETYLATION AT LYS-10 AND LYS-15, METHYLATION AT ARG-18, AND
RP CITRULLINATION AT ARG-18.
RX PubMed=16497732; DOI=10.1210/me.2005-0365;
RA Miao F., Li S., Chavez V., Lanting L., Natarajan R.;
RT "Coactivator-associated arginine methyltransferase-1 enhances nuclear
RT factor-kappaB-mediated gene transcription through methylation of
RT histone H3 at arginine 17.";
RL Mol. Endocrinol. 20:1562-1573(2006).
RN [20]
RP METHYLATION AT ARG-3 BY PRMT6.
RX PubMed=18079182; DOI=10.1101/gad.447007;
RA Hyllus D., Stein C., Schnabel K., Schiltz E., Imhof A., Dou Y.,
RA Hsieh J., Bauer U.M.;
RT "PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4
RT trimethylation.";
RL Genes Dev. 21:3369-3380(2007).
RN [21]
RP ACETYLATION AT LYS-5; LYS-10; LYS-15; LYS-19; LYS-24; LYS-28; LYS-37;
RP LYS-57 AND LYS-80, METHYLATION AT LYS-5; LYS-10; LYS-19; LYS-24;
RP LYS-28; LYS-37; LYS-57; LYS-65; LYS-80 AND LYS-123, AND 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
RT histones H3 and H4.";
RL J. Biol. Chem. 282:7641-7655(2007).
RN [22]
RP ACETYLATION AT LYS-37.
RX PubMed=17189264; DOI=10.1074/jbc.M607909200;
RA Morris S.A., Rao B., Garcia B.A., Hake S.B., Diaz R.L.,
RA Shabanowitz J., Hunt D.F., Allis C.D., Lieb J.D., Strahl B.D.;
RT "Identification of histone H3 lysine 36 acetylation as a highly
RT conserved histone modification.";
RL J. Biol. Chem. 282:7632-7640(2007).
RN [23]
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 [24]
RP METHYLATION AT ARG-3 BY PRMT6.
RX PubMed=18077460; DOI=10.1074/jbc.C700192200;
RA Iberg A.N., Espejo A., Cheng D., Kim D., Michaud-Levesque J.,
RA Richard S., Bedford M.T.;
RT "Arginine methylation of the histone H3 tail impedes effector
RT binding.";
RL J. Biol. Chem. 283:3006-3010(2008).
RN [25]
RP PHOSPHORYLATION AT THR-12.
RX PubMed=18066052; DOI=10.1038/ncb1668;
RA Metzger E., Yin N., Wissmann M., Kunowska N., Fischer K.,
RA Friedrichs N., Patnaik D., Higgins J.M., Potier N., Scheidtmann K.H.,
RA Buettner R., Schule R.;
RT "Phosphorylation of histone H3 at threonine 11 establishes a novel
RT chromatin mark for transcriptional regulation.";
RL Nat. Cell Biol. 10:53-60(2008).
RN [26]
RP ACETYLATION AT LYS-116 AND LYS-123.
RX PubMed=19520870; DOI=10.1074/jbc.M109.003202;
RA Manohar M., Mooney A.M., North J.A., Nakkula R.J., Picking J.W.,
RA Edon A., Fishel R., Poirier M.G., Ottesen J.J.;
RT "Acetylation of histone H3 at the nucleosome dyad alters DNA-histone
RT binding.";
RL J. Biol. Chem. 284:23312-23321(2009).
RN [27]
RP PHOSPHORYLATION AT TYR-42.
RX PubMed=19783980; DOI=10.1038/nature08448;
RA Dawson M.A., Bannister A.J., Gottgens B., Foster S.D., Bartke T.,
RA Green A.R., Kouzarides T.;
RT "JAK2 phosphorylates histone H3Y41 and excludes HP1alpha from
RT chromatin.";
RL Nature 461:819-822(2009).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-108, AND MASS
RP SPECTROMETRY.
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 [29]
RP PHOSPHORYLATION AT SER-58 AND THR-81.
RX PubMed=20850016; DOI=10.1016/j.cell.2010.08.020;
RA Vermeulen M., Eberl H.C., Matarese F., Marks H., Denissov S.,
RA Butter F., Lee K.K., Olsen J.V., Hyman A.A., Stunnenberg H.G.,
RA Mann M.;
RT "Quantitative interaction proteomics and genome-wide profiling of
RT epigenetic histone marks and their readers.";
RL Cell 142:967-980(2010).
RN [30]
RP PHOSPHORYLATION AT THR-7.
RX PubMed=20228790; DOI=10.1038/nature08839;
RA Metzger E., Imhof A., Patel D., Kahl P., Hoffmeyer K., Friedrichs N.,
RA Muller J.M., Greschik H., Kirfel J., Ji S., Kunowska N.,
RA Beisenherz-Huss C., Gunther T., Buettner R., Schule R.;
RT "Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation
RT at histone H3K4.";
RL Nature 464:792-796(2010).
RN [31]
RP CROTONYLATION AT LYS-5; LYS-10; LYS-19; LYS-24; LYS-28 AND LYS-57.
RX PubMed=21925322; DOI=10.1016/j.cell.2011.08.008;
RA Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T.,
RA Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q.,
RA Wysocka J., Ye Y., Khochbin S., Ren B., Zhao Y.;
RT "Identification of 67 histone marks and histone lysine crotonylation
RT as a new type of histone modification.";
RL Cell 146:1016-1028(2011).
RN [32]
RP METHYLATION AT LYS-57.
RX PubMed=22387026; DOI=10.1016/j.molcel.2012.01.019;
RA Yu Y., Song C., Zhang Q., Dimaggio P.A., Garcia B.A., York A.,
RA Carey M.F., Grunstein M.;
RT "Histone H3 lysine 56 methylation regulates DNA replication through
RT its interaction with PCNA.";
RL Mol. Cell 46:7-17(2012).
RN [33]
RP ALLYSINE AT LYS-5.
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 [34]
RP ACETYLATION AT LYS-123.
RX PubMed=23415232; DOI=10.1016/j.cell.2013.01.032;
RA Tropberger P., Pott S., Keller C., Kamieniarz-Gdula K., Caron M.,
RA Richter F., Li G., Mittler G., Liu E.T., Buhler M., Margueron R.,
RA Schneider R.;
RT "Regulation of transcription through acetylation of H3K122 on the
RT lateral surface of the histone octamer.";
RL Cell 152:859-872(2013).
RN [35]
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.,
RA Mann C., Ochsenbein F.;
RT "Structure of the histone chaperone ASF1 bound to the histone H3 C-
RT terminal helix and functional insights.";
RL Structure 15:191-199(2007).
CC -!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and
CC compact DNA into chromatin, limiting DNA accessibility to the
CC cellular machineries which require DNA as a template. Histones
CC thereby play a central role in transcription regulation, DNA
CC repair, DNA replication and chromosomal stability. DNA
CC accessibility is regulated via a complex set of post-translational
CC modifications of histones, also called histone code, and
CC nucleosome remodeling.
CC -!- SUBUNIT: The nucleosome is a histone octamer containing two
CC molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4
CC heterotetramer and two H2A-H2B heterodimers. The octamer wraps
CC approximately 147 bp of DNA. During nucleosome assembly the
CC chaperone ASF1A interacts with the histone H3-H4 heterodimer.
CC -!- INTERACTION:
CC Q12830-4:BPTF; NbExp=2; IntAct=EBI-750650, EBI-4288838;
CC P02545:LMNA; NbExp=6; IntAct=EBI-750650, EBI-351935;
CC Q6UYC3:LMNA; NbExp=3; IntAct=EBI-750650, EBI-8042626;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- DEVELOPMENTAL STAGE: Expressed during S phase, then expression
CC strongly decreases as cell division slows down during the process
CC of differentiation.
CC -!- PTM: Acetylation is generally linked to gene activation.
CC Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9
CC (H3R8me2s). Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac)
CC favors methylation at Arg-18 (H3R17me). Acetylation at Lys-123
CC (H3K122ac) by EP300/p300 plays a central role in chromatin
CC structure: localizes at the surface of the histone octamer and
CC stimulates transcription, possibly by promoting nucleosome
CC instability.
CC -!- PTM: Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by
CC PADI4 impairs methylation and represses transcription.
CC -!- PTM: Asymmetric dimethylation at Arg-18 (H3R17me2a) by CARM1 is
CC linked to gene activation. Symmetric dimethylation at Arg-9
CC (H3R8me2s) by PRMT5 is linked to gene repression. Asymmetric
CC dimethylation at Arg-3 (H3R2me2a) by PRMT6 is linked to gene
CC repression and is mutually exclusive with H3 Lys-5 methylation
CC (H3K4me2 and H3K4me3). H3R2me2a is present at the 3' of genes
CC regardless of their transcription state and is enriched on
CC inactive promoters, while it is absent on active promoters.
CC -!- PTM: Methylation at Lys-5 (H3K4me), Lys-37 (H3K36me) and Lys-80
CC (H3K79me) are linked to gene activation. Methylation at Lys-5
CC (H3K4me) facilitates subsequent acetylation of H3 and H4.
CC Methylation at Lys-80 (H3K79me) is associated with DNA double-
CC strand break (DSB) responses and is a specific target for TP53BP1.
CC Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are linked to
CC gene repression. Methylation at Lys-10 (H3K9me) is a specific
CC target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents
CC subsequent phosphorylation at Ser-11 (H3S10ph) and acetylation of
CC H3 and H4. Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me)
CC require preliminary monoubiquitination of H2B at 'Lys-120'.
CC Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched
CC in inactive X chromosome chromatin. Monomethylation at Lys-57
CC (H3K56me1) by EHMT2/G9A in G1 phase promotes interaction with PCNA
CC and is required for DNA replication.
CC -!- PTM: Phosphorylated at Thr-4 (H3T3ph) by GSG2/haspin during
CC prophase and dephosphorylated during anaphase. Phosphorylation at
CC Ser-11 (H3S10ph) by AURKB is crucial for chromosome condensation
CC and cell-cycle progression during mitosis and meiosis. In addition
CC phosphorylation at Ser-11 (H3S10ph) by RPS6KA4 and RPS6KA5 is
CC important during interphase because it enables the transcription
CC of genes following external stimulation, like mitogens, stress,
CC growth factors or UV irradiation and result in the activation of
CC genes, such as c-fos and c-jun. Phosphorylation at Ser-11
CC (H3S10ph), which is linked to gene activation, prevents
CC methylation at Lys-10 (H3K9me) but facilitates acetylation of H3
CC and H4. Phosphorylation at Ser-11 (H3S10ph) by AURKB mediates the
CC dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from
CC heterochromatin. Phosphorylation at Ser-11 (H3S10ph) is also an
CC essential regulatory mechanism for neoplastic cell transformation.
CC Phosphorylated at Ser-29 (H3S28ph) by MLTK isoform 1, RPS6KA5 or
CC AURKB during mitosis or upon ultraviolet B irradiation.
CC Phosphorylation at Thr-7 (H3T6ph) by PRKCB is a specific tag for
CC epigenetic transcriptional activation that prevents demethylation
CC of Lys-5 (H3K4me) by LSD1/KDM1A. At centromeres, specifically
CC phosphorylated at Thr-12 (H3T11ph) from prophase to early
CC anaphase, by DAPK3 and PKN1. Phosphorylation at Thr-12 (H3T11ph)
CC by PKN1 is a specific tag for epigenetic transcriptional
CC activation that promotes demethylation of Lys-10 (H3K9me) by
CC KDM4C/JMJD2C. Phosphorylation at Tyr-42 (H3Y41ph) by JAK2 promotes
CC exclusion of CBX5 (HP1 alpha) from chromatin.
CC -!- PTM: Monoubiquitinated by RAG1 in lymphoid cells,
CC monoubiquitination is required for V(D)J recombination (By
CC similarity). Ubiquitinated by the CUL4-DDB-RBX1 complex in
CC response to ultraviolet irradiation. This may weaken the
CC interaction between histones and DNA and facilitate DNA
CC accessibility to repair proteins.
CC -!- PTM: Lysine deamination at Lys-5 (H3K4all) to form allysine is
CC mediated by LOXL2. Allysine formation by LOXL2 only takes place on
CC H3K4me3 and results in gene repression (PubMed:22483618).
CC -!- PTM: Crotonylation (Kcr) is specifically present in male germ
CC cells and marks testis-specific genes in post-meiotic cells,
CC including X-linked genes that escape sex chromosome inactivation
CC in haploid cells. Crotonylation marks active promoters and
CC enhancers and confers resistance to transcriptional repressors. It
CC is also associated with post-meiotically activated genes on
CC autosomes.
CC -!- SIMILARITY: Belongs to the histone H3 family.
CC -----------------------------------------------------------------------
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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 RefSeq; NP_001005464.1; NM_001005464.2.
DR RefSeq; NP_001116847.1; NM_001123375.2.
DR RefSeq; NP_066403.2; NM_021059.2.
DR UniGene; Hs.647745; -.
DR UniGene; Hs.706618; -.
DR UniGene; Hs.712062; -.
DR PDB; 2IIJ; NMR; -; B=123-136.
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 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 ProteinModelPortal; Q71DI3; -.
DR SMR; Q71DI3; 17-136.
DR DIP; DIP-48606N; -.
DR IntAct; Q71DI3; 9.
DR MINT; MINT-4828325; -.
DR STRING; 9606.ENSP00000333277; -.
DR PhosphoSite; Q71DI3; -.
DR PaxDb; Q71DI3; -.
DR PRIDE; Q71DI3; -.
DR DNASU; 126961; -.
DR Ensembl; ENST00000331491; ENSP00000333277; ENSG00000183598.
DR Ensembl; ENST00000369158; ENSP00000358154; ENSG00000203811.
DR Ensembl; ENST00000403683; ENSP00000385479; ENSG00000203852.
DR Ensembl; ENST00000578851; ENSP00000463798; ENSG00000265133.
DR Ensembl; ENST00000580481; ENSP00000463420; ENSG00000270263.
DR Ensembl; ENST00000585113; ENSP00000463995; ENSG00000270827.
DR GeneID; 126961; -.
DR GeneID; 333932; -.
DR GeneID; 653604; -.
DR KEGG; hsa:126961; -.
DR KEGG; hsa:333932; -.
DR KEGG; hsa:653604; -.
DR UCSC; uc001esv.3; human.
DR CTD; 126961; -.
DR CTD; 333932; -.
DR CTD; 653604; -.
DR GeneCards; GC01M149784; -.
DR GeneCards; GC01M149812; -.
DR GeneCards; GC01P149824; -.
DR HGNC; HGNC:20505; HIST2H3A.
DR HGNC; HGNC:20503; HIST2H3C.
DR HGNC; HGNC:25311; HIST2H3D.
DR HPA; HPA042570; -.
DR MIM; 142780; gene.
DR neXtProt; NX_Q71DI3; -.
DR PharmGKB; PA145148728; -.
DR eggNOG; COG2036; -.
DR HOGENOM; HOG000155290; -.
DR HOVERGEN; HBG001172; -.
DR InParanoid; Q71DI3; -.
DR KO; K11253; -.
DR OMA; RISKMAR; -.
DR OrthoDB; EOG7HB5C2; -.
DR Reactome; REACT_111183; Meiosis.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_120956; Cellular responses to stress.
DR Reactome; REACT_604; Hemostasis.
DR ChiTaRS; HIST2H3C; human.
DR EvolutionaryTrace; Q71DI3; -.
DR GeneWiki; HIST2H3C; -.
DR NextBio; 81962; -.
DR Bgee; Q71DI3; -.
DR CleanEx; HS_HIST2H3A; -.
DR CleanEx; HS_HIST2H3C; -.
DR CleanEx; HS_HIST2H3D; -.
DR Genevestigator; Q71DI3; -.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0007596; P:blood coagulation; TAS:Reactome.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_core_D.
DR InterPro; IPR000164; Histone_H3.
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; Chromosome; Citrullination;
KW Complete proteome; Direct protein sequencing; DNA-binding;
KW Methylation; Nucleosome core; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 136 Histone H3.2.
FT /FTId=PRO_0000250357.
FT MOD_RES 3 3 Asymmetric dimethylarginine; by PRMT6.
FT MOD_RES 4 4 Phosphothreonine; by GSG2.
FT MOD_RES 5 5 Allysine; alternate.
FT MOD_RES 5 5 N6,N6,N6-trimethyllysine; alternate.
FT MOD_RES 5 5 N6,N6-dimethyllysine; alternate.
FT MOD_RES 5 5 N6-acetyllysine; alternate.
FT MOD_RES 5 5 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 5 5 N6-methyllysine; alternate.
FT MOD_RES 7 7 Phosphothreonine; by PKC.
FT MOD_RES 9 9 Citrulline; alternate.
FT MOD_RES 9 9 Symmetric dimethylarginine; by PRMT5;
FT alternate (By similarity).
FT MOD_RES 10 10 N6,N6,N6-trimethyllysine; alternate.
FT MOD_RES 10 10 N6,N6-dimethyllysine; alternate.
FT MOD_RES 10 10 N6-acetyllysine; alternate.
FT MOD_RES 10 10 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 10 10 N6-methyllysine; alternate.
FT MOD_RES 11 11 Phosphoserine; by AURKB, AURKC, RPS6KA3,
FT RPS6KA4 and RPS6KA5.
FT MOD_RES 12 12 Phosphothreonine; by PKC.
FT MOD_RES 15 15 N6-acetyllysine.
FT MOD_RES 18 18 Asymmetric dimethylarginine; by CARM1;
FT alternate.
FT MOD_RES 18 18 Citrulline; alternate.
FT MOD_RES 19 19 N6-acetyllysine; alternate.
FT MOD_RES 19 19 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 19 19 N6-methyllysine; alternate.
FT MOD_RES 24 24 N6-acetyllysine; alternate.
FT MOD_RES 24 24 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 24 24 N6-methyllysine; alternate.
FT MOD_RES 28 28 N6,N6,N6-trimethyllysine; alternate.
FT MOD_RES 28 28 N6,N6-dimethyllysine; alternate.
FT MOD_RES 28 28 N6-acetyllysine; alternate.
FT MOD_RES 28 28 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 28 28 N6-methyllysine; alternate.
FT MOD_RES 29 29 Phosphoserine; by AURKB, AURKC and
FT RPS6KA5.
FT MOD_RES 37 37 N6,N6,N6-trimethyllysine; alternate.
FT MOD_RES 37 37 N6,N6-dimethyllysine; alternate.
FT MOD_RES 37 37 N6-acetyllysine; alternate.
FT MOD_RES 37 37 N6-methyllysine; alternate.
FT MOD_RES 38 38 N6-methyllysine (By similarity).
FT MOD_RES 42 42 Phosphotyrosine.
FT MOD_RES 57 57 N6,N6,N6-trimethyllysine; alternate.
FT MOD_RES 57 57 N6-acetyllysine; alternate.
FT MOD_RES 57 57 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 57 57 N6-methyllysine; by EHMT2; alternate.
FT MOD_RES 58 58 Phosphoserine.
FT MOD_RES 65 65 N6-methyllysine.
FT MOD_RES 80 80 N6,N6,N6-trimethyllysine; alternate (By
FT similarity).
FT MOD_RES 80 80 N6,N6-dimethyllysine; alternate.
FT MOD_RES 80 80 N6-acetyllysine; alternate.
FT MOD_RES 80 80 N6-methyllysine; alternate.
FT MOD_RES 81 81 Phosphothreonine.
FT MOD_RES 108 108 Phosphothreonine.
FT MOD_RES 116 116 N6-acetyllysine.
FT MOD_RES 123 123 N6-acetyllysine; alternate.
FT MOD_RES 123 123 N6-methyllysine; alternate.
FT VARIANT 91 91 M -> T (in dbSNP:rs2664732).
FT /FTId=VAR_059313.
FT VARIANT 128 128 A -> V (in dbSNP:rs2664731).
FT /FTId=VAR_059314.
FT STRAND 7 9
FT HELIX 26 29
FT TURN 39 41
FT HELIX 46 57
FT HELIX 65 77
FT HELIX 87 114
FT STRAND 118 120
FT HELIX 122 131
SQ SEQUENCE 136 AA; 15388 MW; 6FD8508EA50A0EEC CRC64;
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE
LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEASEAY LVGLFEDTNL CAIHAKRVTI
MPKDIQLARR IRGERA
//
MIM
142780
*RECORD*
*FIELD* NO
142780
*FIELD* TI
*142780 HISTONE GENE CLUSTER 2, H3 HISTONE FAMILY, MEMBER C; HIST2H3C
;;HISTONE GENE CLUSTER 2, H3C;;
read moreHIST2 CLUSTER, H3C;;
H3 HISTONE, FAMILY 2; H3F2;;
H3 HISTONE FAMILY, MEMBER N; H3FN;;
H3 HISTONE FAMILY, MEMBER M; H3FM;;
H3/M;;
H3.2
*FIELD* TX
For background information on histones, histone gene clusters, and the
H3 histone family, see HIST1H3A (602810).
CLONING
By genomic sequence analysis, Marzluff et al. (2002) identified the
human HIST2H3C gene. The protein encoded by HIST2H3C, designated H3.2,
differs from H3.1, which is encoded by multiple H3 genes (see 602810),
at only 1 residue, and from histone H3.3, which is encoded by both H3F3A
(601128) and H3F3B (601058), at a few residues.
Using Northern blot analysis, Frank et al. (2003) assayed for expression
of the replacement histones H3.3A (H3F3A) and H3.3B (H3F3B) and the cell
cycle-dependent histone H3/m in human tissues and cell lines. All 6 cell
lines expressed H3.3A, H3.3B, and H3/m at high levels. Conversely, fetal
liver predominantly expressed H3/m, likely due to its rapid cell growth,
whereas adult liver, kidney, and heart predominantly expressed H3.3A and
H3.3B. The H3/m transcript was detected at 0.6 kb.
MAPPING
By study of mouse-human cell hybrids and by in situ hybridization, Green
et al. (1984) showed that H3 and H4 histone genes are on chromosome 1q,
probably 1q21. The nomenclature committee of the Human Gene Mapping
Workshops designated the histone genes on chromosome 1q21 as H3 histone,
family 2, and H4 histone, family 2 (HIST2H4A; 142750) (McAlpine, 1989).
By genomic sequence analysis, Marzluff et al. (2002) determined that the
histone gene cluster on chromosome 1q21, which they called histone gene
cluster-2 (HIST2), contains 6 histone genes, including HIST2H3C. The
cluster also contains 2 H3 pseudogenes, designated HIST2H3A and
HIST2H3B.
GENE FUNCTION
See HIST1H3A (602810) for functional information on the H3 histone
family.
- H3.2 Histone
Hake et al. (2006) noted that most studies on expression or
posttranslational modifications of H3 histones do not differentiate
between the H3.1, H3.2, and H3.3 proteins, in part due to their high
degree of amino acid identity. By quantitative PCR of 5 human cell
lines, they found that the 9 H3.1 genes, 1 H3.2 gene, and 2 H3.3 genes
examined were expressed in a cell line-specific manner. All 3 types of
H3 genes were highly expressed during S phase in human cell lines,
whereas the H3.3 genes were also highly expressed outside of S phase,
consistent with their status as replication-independent genes. Using a
combination of isotopic labeling and quantitative tandem mass
spectrometry, Hake et al. (2006) showed that the H3.1, H3.2, and H3.3
proteins differed in their posttranslational modifications. H3.1 was
enriched in marks associated with both gene activation and gene
silencing, H3.2 was enriched in repressive marks associated with gene
silencing and the formation of facultative heterochromatin, and H3.3 was
enriched in marks associated with transcriptional activation. Hake et
al. (2006) concluded that H3.1, H3.2, and H3.3 likely have unique
functions and should not be treated as equivalent proteins.
*FIELD* RF
1. Frank, D.; Doenecke, D.; Albig, W.: Differential expression of
human replacement and cell cycle dependent H3 histone genes. Gene 312:
135-143, 2003.
2. Green, L.; Van Antwerpen, R.; Stein, J.; Stein, G.; Tripputi, P.;
Emanuel, B.; Selden, J.; Croce, C.: A major human histone gene cluster
on the long arm of chromosome 1. Science 226: 838-840, 1984.
3. Hake, S. B.; Garcia, B. A.; Duncan, E. M.; Kauer, M.; Dellaire,
G.; Shabanowitz, J.; Bazett-Jones, D. P.; Allis, C. D.; Hunt, D. F.
: Expression patterns and post-translational modifications associated
with mammalian histone H3 variants. J. Biol. Chem. 281: 559-568,
2006.
4. Marzluff, W. F.; Gongidi, P.; Woods, K. R.; Jin, J.; Maltais, L.
J.: The human and mouse replication-dependent histone genes. Genomics 80:
487-498, 2002.
5. McAlpine, P. J.: Personal Communication. Winnipeg, Manitoba,
Canada 1989.
*FIELD* CN
Patricia A. Hartz - updated: 02/06/2013
Matthew B. Gross - updated: 2/4/2013
Rebekah S. Rasooly - updated: 7/8/1998
*FIELD* CD
Victor A. McKusick: 6/4/1986
*FIELD* ED
mgross: 02/06/2013
mgross: 2/4/2013
mgross: 7/22/2010
alopez: 3/25/2008
alopez: 7/18/2006
alopez: 10/20/2004
tkritzer: 10/5/2004
alopez: 10/4/2004
tkritzer: 9/28/2004
alopez: 7/8/1998
psherman: 4/28/1998
mark: 9/22/1996
mimadm: 4/29/1994
warfield: 4/8/1994
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/27/1989
root: 9/15/1989
*RECORD*
*FIELD* NO
142780
*FIELD* TI
*142780 HISTONE GENE CLUSTER 2, H3 HISTONE FAMILY, MEMBER C; HIST2H3C
;;HISTONE GENE CLUSTER 2, H3C;;
read moreHIST2 CLUSTER, H3C;;
H3 HISTONE, FAMILY 2; H3F2;;
H3 HISTONE FAMILY, MEMBER N; H3FN;;
H3 HISTONE FAMILY, MEMBER M; H3FM;;
H3/M;;
H3.2
*FIELD* TX
For background information on histones, histone gene clusters, and the
H3 histone family, see HIST1H3A (602810).
CLONING
By genomic sequence analysis, Marzluff et al. (2002) identified the
human HIST2H3C gene. The protein encoded by HIST2H3C, designated H3.2,
differs from H3.1, which is encoded by multiple H3 genes (see 602810),
at only 1 residue, and from histone H3.3, which is encoded by both H3F3A
(601128) and H3F3B (601058), at a few residues.
Using Northern blot analysis, Frank et al. (2003) assayed for expression
of the replacement histones H3.3A (H3F3A) and H3.3B (H3F3B) and the cell
cycle-dependent histone H3/m in human tissues and cell lines. All 6 cell
lines expressed H3.3A, H3.3B, and H3/m at high levels. Conversely, fetal
liver predominantly expressed H3/m, likely due to its rapid cell growth,
whereas adult liver, kidney, and heart predominantly expressed H3.3A and
H3.3B. The H3/m transcript was detected at 0.6 kb.
MAPPING
By study of mouse-human cell hybrids and by in situ hybridization, Green
et al. (1984) showed that H3 and H4 histone genes are on chromosome 1q,
probably 1q21. The nomenclature committee of the Human Gene Mapping
Workshops designated the histone genes on chromosome 1q21 as H3 histone,
family 2, and H4 histone, family 2 (HIST2H4A; 142750) (McAlpine, 1989).
By genomic sequence analysis, Marzluff et al. (2002) determined that the
histone gene cluster on chromosome 1q21, which they called histone gene
cluster-2 (HIST2), contains 6 histone genes, including HIST2H3C. The
cluster also contains 2 H3 pseudogenes, designated HIST2H3A and
HIST2H3B.
GENE FUNCTION
See HIST1H3A (602810) for functional information on the H3 histone
family.
- H3.2 Histone
Hake et al. (2006) noted that most studies on expression or
posttranslational modifications of H3 histones do not differentiate
between the H3.1, H3.2, and H3.3 proteins, in part due to their high
degree of amino acid identity. By quantitative PCR of 5 human cell
lines, they found that the 9 H3.1 genes, 1 H3.2 gene, and 2 H3.3 genes
examined were expressed in a cell line-specific manner. All 3 types of
H3 genes were highly expressed during S phase in human cell lines,
whereas the H3.3 genes were also highly expressed outside of S phase,
consistent with their status as replication-independent genes. Using a
combination of isotopic labeling and quantitative tandem mass
spectrometry, Hake et al. (2006) showed that the H3.1, H3.2, and H3.3
proteins differed in their posttranslational modifications. H3.1 was
enriched in marks associated with both gene activation and gene
silencing, H3.2 was enriched in repressive marks associated with gene
silencing and the formation of facultative heterochromatin, and H3.3 was
enriched in marks associated with transcriptional activation. Hake et
al. (2006) concluded that H3.1, H3.2, and H3.3 likely have unique
functions and should not be treated as equivalent proteins.
*FIELD* RF
1. Frank, D.; Doenecke, D.; Albig, W.: Differential expression of
human replacement and cell cycle dependent H3 histone genes. Gene 312:
135-143, 2003.
2. Green, L.; Van Antwerpen, R.; Stein, J.; Stein, G.; Tripputi, P.;
Emanuel, B.; Selden, J.; Croce, C.: A major human histone gene cluster
on the long arm of chromosome 1. Science 226: 838-840, 1984.
3. Hake, S. B.; Garcia, B. A.; Duncan, E. M.; Kauer, M.; Dellaire,
G.; Shabanowitz, J.; Bazett-Jones, D. P.; Allis, C. D.; Hunt, D. F.
: Expression patterns and post-translational modifications associated
with mammalian histone H3 variants. J. Biol. Chem. 281: 559-568,
2006.
4. Marzluff, W. F.; Gongidi, P.; Woods, K. R.; Jin, J.; Maltais, L.
J.: The human and mouse replication-dependent histone genes. Genomics 80:
487-498, 2002.
5. McAlpine, P. J.: Personal Communication. Winnipeg, Manitoba,
Canada 1989.
*FIELD* CN
Patricia A. Hartz - updated: 02/06/2013
Matthew B. Gross - updated: 2/4/2013
Rebekah S. Rasooly - updated: 7/8/1998
*FIELD* CD
Victor A. McKusick: 6/4/1986
*FIELD* ED
mgross: 02/06/2013
mgross: 2/4/2013
mgross: 7/22/2010
alopez: 3/25/2008
alopez: 7/18/2006
alopez: 10/20/2004
tkritzer: 10/5/2004
alopez: 10/4/2004
tkritzer: 9/28/2004
alopez: 7/8/1998
psherman: 4/28/1998
mark: 9/22/1996
mimadm: 4/29/1994
warfield: 4/8/1994
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/27/1989
root: 9/15/1989