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Biol. Chem.27425543-25549PHOSPHORYLATION AT SER-11 AND SER-29Ultraviolet B-induced phosphorylation of histone H3 at serine 28 is mediated by MSK1.Zhong S.Jansen C.She Q.-B.Goto H.Inagaki M.Bode A.M.Ma W.-Y.Dong Z.doi:10.1074/jbc.m1039732002001J. Biol. Chem.27633213-33219PHOSPHORYLATION AT SER-29Crosstalk between CARM1 methylation and CBP acetylation on histone H3.Daujat S.Bauer U.-M.Shah V.Turner B.Berger S.Kouzarides T.doi:10.1016/s0960-9822(02)01387-82002Curr. Biol.122090-2097ACETYLATION AT LYS-15; LYS-19 AND LYS-24METHYLATION AT ARG-18Methylation at arginine 17 of histone H3 is linked to gene activation.Bauer U.-M.Daujat S.Nielsen S.J.Nightingale K.Kouzarides T.doi:10.1093/embo-reports/kvf0132002EMBO Rep.339-44METHYLATION AT ARG-18Aurora-B phosphorylates Histone H3 at serine28 with regard to the mitotic chromosome condensation.Goto H.Yasui Y.Nigg E.A.Inagaki M.doi:10.1046/j.1356-9597.2001.00498.x2002Genes Cells711-17PHOSPHORYLATION AT SER-11 AND SER-29Identification of methylation and acetylation sites on mouse histone H3 using matrix-assisted laser desorption/ionization time-of-flight and nanoelectrospray ionization tandem mass spectrometry.Cocklin R.R.Wang M.doi:10.1023/a:10253340060142003J. Protein Chem.22327-334ACETYLATION AT LYS-15; LYS-19 AND LYS-24METHYLATION AT LYS-10; LYS-28; LYS-37; LYS-80 AND LYS-123IDENTIFICATION BY MASS SPECTROMETRYHistone deimination antagonizes arginine methylation.Cuthbert G.L.Daujat S.Snowden A.W.Erdjument-Bromage H.Hagiwara T.Yamada M.Schneider R.Gregory P.D.Tempst P.Bannister A.J.Kouzarides T.doi:10.1016/j.cell.2004.08.0202004Cell118545-553CITRULLINATION AT ARG-3; ARG-9; ARG-18 AND ARG-27Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes.Pal S.Vishwanath S.N.Erdjument-Bromage H.Tempst P.Sif S.doi:10.1128/mcb.24.21.9630-9645.20042004Mol. Cell. Biol.249630-9645METHYLATION AT ARG-9ACETYLATION AT LYS-10Arginine methyltransferase CARM1 is a promoter-specific regulator of NF-kappaB-dependent gene expression.Covic M.Hassa P.O.Saccani S.Buerki C.Meier N.I.Lombardi C.Imhof R.Bedford M.T.Natoli G.Hottiger M.O.doi:10.1038/sj.emboj.76005002005EMBO J.2485-96METHYLATION AT ARG-18The kinase haspin is required for mitotic histone H3 Thr 3 phosphorylation and normal metaphase chromosome alignment.Dai J.Sultan S.Taylor S.S.Higgins J.M.G.doi:10.1101/gad.12671052005Genes Dev.19472-488PHOSPHORYLATION AT THR-4 AND SER-11Phosphorylation of Ser28 in histone H3 mediated by mixed lineage kinase-like mitogen-activated protein triple kinase alpha.Choi H.S.Choi B.Y.Cho Y.-Y.Zhu F.Bode A.M.Dong Z.doi:10.1074/jbc.m4105212002005J. Biol. Chem.28013545-13553PHOSPHORYLATION AT SER-29MAP kinase-mediated phosphorylation of distinct pools of histone H3 at S10 or S28 via mitogen- and stress-activated kinase 1/2.Dyson M.H.Thomson S.Inagaki M.Goto H.Arthur S.J.Nightingale K.Iborra F.J.Mahadevan L.C.doi:10.1242/jcs.023732005J. Cell Sci.1182247-2259PHOSPHORYLATION AT SER-11 AND SER-29Stimulation of the Ras-MAPK pathway leads to independent phosphorylation of histone H3 on serine 10 and 28.Dunn K.L.Davie J.R.doi:10.1038/sj.onc.12085212005Oncogene243492-3502PHOSPHORYLATION AT SER-11 AND SER-29Identification of histone H3 lysine 36 acetylation as a highly conserved histone modification.Morris S.A.Rao B.Garcia B.A.Hake S.B.Diaz R.L.Shabanowitz J.Hunt D.F.Allis C.D.Lieb J.D.Strahl B.D.doi:10.1074/jbc.m6079092002007J. Biol. Chem.2827632-7640ACETYLATION AT LYS-37Organismal differences in post-translational modifications in histones H3 and H4.Garcia B.A.Hake S.B.Diaz R.L.Kauer M.Morris S.A.Recht J.Shabanowitz J.Mishra N.Strahl B.D.Allis C.D.Hunt D.F.doi:10.1074/jbc.m6079002002007J. Biol. Chem.2827641-7655ACETYLATION AT LYS-5; LYS-10; LYS-15; LYS-19; LYS-24 AND LYS-28METHYLATION AT LYS-5; LYS-10; LYS-19; LYS-24; LYS-28; LYS-37 AND LYS-80IDENTIFICATION BY MASS SPECTROMETRYThe RING domain of RAG1 ubiquitylates histone H3: a novel activity in chromatin-mediated regulation of V(D)J joining.Grazini U.Zanardi F.Citterio E.Casola S.Goding C.R.McBlane F.doi:10.1016/j.molcel.2009.12.0352010Mol. Cell37282-293UBIQUITINATIONIdentification of 67 histone marks and histone lysine crotonylation as a new type of histone modification.Tan M.Luo H.Lee S.Jin F.Yang J.S.Montellier E.Buchou T.Cheng Z.Rousseaux S.Rajagopal N.Lu Z.Ye Z.Zhu Q.Wysocka J.Ye Y.Khochbin S.Ren B.Zhao Y.doi:10.1016/j.cell.2011.08.0082011Cell1461016-1028CROTONYLATION AT LYS-5; LYS-10; LYS-19; LYS-24; LYS-28 AND LYS-57Lysine succinylation and lysine malonylation in histones.Xie Z.Dai J.Dai L.Tan M.Cheng Z.Wu Y.Boeke J.D.Zhao Y.doi:10.1074/mcp.m111.0158752012Mol. Cell. Proteomics11100-107SUCCINYLATION AT LYS-57 AND LYS-80Lysine 2-hydroxyisobutyrylation is a widely distributed active histone mark.Dai L.Peng C.Montellier E.Lu Z.Chen Y.Ishii H.Debernardi A.Buchou T.Rousseaux S.Jin F.Sabari B.R.Deng Z.Allis C.D.Ren B.Khochbin S.Zhao Y.doi:10.1038/nchembio.14972014Nat. Chem. Biol.10365-370HYDROXYBUTYRYLATION AT LYS-5; LYS-10; LYS-15; LYS-19; LYS-24; LYS-28; LYS-37; LYS-57; LYS-65; LYS-80 AND LYS-123Dynamic competing histone H4 K5K8 acetylation and butyrylation are hallmarks of highly active gene promoters.Goudarzi A.Zhang D.Huang H.Barral S.Kwon O.K.Qi S.Tang Z.Buchou T.Vitte A.L.He T.Cheng Z.Montellier E.Gaucher J.Curtet S.Debernardi A.Charbonnier G.Puthier D.Petosa C.Panne D.Rousseaux S.Roeder R.G.Zhao Y.Khochbin S.doi:10.1016/j.molcel.2016.03.0142016Mol. Cell62169-180BUTYRYLATION AT LYS-19; LYS-24; LYS-28; LYS-37; LYS-38; LYS-80 AND LYS-123Metabolic regulation of gene expression by histone lysine beta-hydroxybutyrylation.Xie Z.Zhang D.Chung D.Tang Z.Huang H.Dai L.Qi S.Li J.Colak G.Chen Y.Xia C.Peng C.Ruan H.Kirkey M.Wang D.Jensen L.M.Kwon O.K.Lee S.Pletcher S.D.Tan M.Lombard D.B.White K.P.Zhao H.Li J.'Roeder R.G.Yang X.Zhao Y.doi:10.1016/j.molcel.2016.03.0362016Mol. Cell62194-206HYDROXYBUTYRYLATION AT LYS-5; LYS-10; LYS-15; LYS-19; LYS-24 AND LYS-57Histone deacetylase (HDAC) 1 and 2 complexes regulate both histone acetylation and crotonylation in vivo.Kelly R.D.W.Chandru A.Watson P.J.Song Y.Blades M.Robertson N.S.Jamieson A.G.Schwabe J.W.R.Cowley S.M.doi:10.1038/s41598-018-32927-92018Sci. Rep.814690CROTONYLATION AT LYS-19ACETYLATION AT LYS-19Histone serotonylation is a permissive modification that enhances TFIID binding to H3K4me3.Farrelly L.A.Thompson R.E.Zhao S.Lepack A.E.Lyu Y.Bhanu N.V.Zhang B.Loh Y.E.Ramakrishnan A.Vadodaria K.C.Heard K.J.Erikson G.Nakadai T.Bastle R.M.Lukasak B.J.Zebroski H. IIIAlenina N.Bader M.Berton O.Roeder R.G.Molina H.Gage F.H.Shen L.Garcia B.A.Li H.Muir T.W.Maze I.doi:10.1038/s41586-019-1024-72019Nature567535-539SEROTONYLATION AT GLN-6Metabolic regulation of gene expression by histone lactylation.Zhang D.Tang Z.Huang H.Zhou G.Cui C.Weng Y.Liu W.Kim S.Lee S.Perez-Neut M.Ding J.Czyz D.Hu R.Ye Z.He M.Zheng Y.G.Shuman H.A.Dai L.Ren B.Roeder R.G.Becker L.Zhao Y.doi:10.1038/s41586-019-1678-12019Nature574575-580LACTYLATION AT LYS-15; LYS-19; LYS-24; LYS-28 AND LYS-57Different initiation.Different initiation.S451112.05D/E=2-91.80D/E=2-142.00D/F=2-82.10E/F=30-442.34E/F=30-441.65E/F=30-441.60E/F=30-441.75E/F=30-442.20E/F=30-4411716421Nucleosome, variant H3.2-H2A.2-H2B.1271 site, 1 O-linked glycan (1 site)mouseH3c13H3c14H3c15H3c2H3c3H3c4H3c6H3c7EukaryotaInterleukin-7 signalingPRC2 methylates histones and DNAPKMTs methylate histone lysinesHDMs demethylate histonesHATs acetylate histonesRMTs methylate histone argininesChromatin modifying enzymesRUNX1 regulates genes involved in megakaryocyte differentiation and platelet functionEstrogen-dependent gene expressionFactors involved in megakaryocyte development and platelet production12 hits in 40 CRISPR screens13 hits in 45 CRISPR screens11 hits in 53 CRISPR screens11 hits in 42 CRISPR screens8 hits in 41 CRISPR screens12 hits in 46 CRISPR screens14 hits in 43 CRISPR screens15 hits in 46 CRISPR screensmousemouseProteinExpressed in uterus and 52 other cell types or tissuesbaseline and differentialHistone, subunit AHistone-foldHistone_H2A/H2B/H3Histone_H3/CENP-AHISTONE H3HISTONE H3.1THistoneHISTONEH3H3Histone-foldHISTONE_H3_1HISTONE_H3_2MMHistone H3.2H3-clustered histone 13H3-clustered histone 14H3-clustered histone 15H3-clustered histone 2H3-clustered histone 3H3-clustered histone 4H3-clustered histone 6H3-clustered histone 7H3c2H3-53H3.2H3bHist1h3bH3c3H3-143Hist1h3cH3c4H3-BHist1h3dH3c6H3-FHist1h3eH3c7H3.2-221H3fHist1h3fH3c13H3.2-616Hist2h3bH3c14H3.2-615Hist2h3c1Hist2h3ca1H3c15H3.2-614Hist2h3c2Hist2h3ca2Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. During nucleosome assembly the chaperone ASF1A interacts with the histone H3-H4 heterodimer (By similarity). Interacts with DNAJC9, CHAF1A and CHAF1B (By similarity).Expressed during S phase, then expression strongly decreases as cell division slows down during the process of differentiation.Acetylation is generally linked to gene activation. Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s). Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me). Acetylation at Lys-123 (H3K122ac) by EP300/p300 plays a central role in chromatin structure: localizes at the surface of the histone octamer and stimulates transcription, possibly by promoting nucleosome instability.Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription.Asymmetric dimethylation at Arg-18 (H3R17me2a) by CARM1 is linked to gene activation. Symmetric dimethylation at Arg-9 (H3R8me2s) by PRMT5 is linked to gene repression. Asymmetric dimethylation at Arg-3 (H3R2me2a) by PRMT6 is linked to gene repression and is mutually exclusive with H3 Lys-5 methylation (H3K4me2 and H3K4me3). H3R2me2a is present at the 3' of genes regardless of their transcription state and is enriched on inactive promoters, while it is absent on active promoters (By similarity).Methylation at Lys-5 (H3K4me), Lys-37 (H3K36me) and Lys-80 (H3K79me) are linked to gene activation. Methylation at Lys-5 (H3K4me) facilitates subsequent acetylation of H3 and H4. Methylation at Lys-80 (H3K79me) is associated with DNA double-strand break (DSB) responses and is a specific target for TP53BP1. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are linked to gene repression. Methylation at Lys-10 (H3K9me) is a specific target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents subsequent phosphorylation at Ser-11 (H3S10ph) and acetylation of H3 and H4. Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120'. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched in inactive X chromosome chromatin. Monomethylation at Lys-57 (H3K56me1) by EHMT2/G9A in G1 phase promotes interaction with PCNA and is required for DNA replication.Phosphorylated at Thr-4 (H3T3ph) by HASPIN during prophase and dephosphorylated during anaphase. Phosphorylation at Ser-11 (H3S10ph) by AURKB is crucial for chromosome condensation and cell-cycle progression during mitosis and meiosis. In addition phosphorylation at Ser-11 (H3S10ph) by RPS6KA4 and RPS6KA5 is important during interphase because it enables the transcription of genes following external stimulation, like mitogens, stress, growth factors or UV irradiation and result in the activation of genes, such as c-fos and c-jun. Phosphorylation at Ser-11 (H3S10ph), which is linked to gene activation, prevents methylation at Lys-10 (H3K9me) but facilitates acetylation of H3 and H4. Phosphorylation at Ser-11 (H3S10ph) by AURKB mediates the dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from heterochromatin. Phosphorylation at Ser-11 (H3S10ph) is also an essential regulatory mechanism for neoplastic cell transformation. Phosphorylated at Ser-29 (H3S28ph) by MAP3K20 isoform 1, RPS6KA5 or AURKB during mitosis or upon ultraviolet B irradiation. Phosphorylation at Thr-7 (H3T6ph) by PRKCB is a specific tag for epigenetic transcriptional activation that prevents demethylation of Lys-5 (H3K4me) by LSD1/KDM1A. At centromeres, specifically phosphorylated at Thr-12 (H3T11ph) from prophase to early anaphase, by DAPK3 and PKN1. Phosphorylation at Thr-12 (H3T11ph) by PKN1 or isoform M2 of PKM (PKM2) is a specific tag for epigenetic transcriptional activation that promotes demethylation of Lys-10 (H3K9me) by KDM4C/JMJD2C. Phosphorylation at Tyr-42 (H3Y41ph) by JAK2 promotes exclusion of CBX5 (HP1 alpha) from chromatin.Ubiquitinated by the CUL4-DDB-RBX1 complex in response to ultraviolet irradiation. This may weaken the interaction between histones and DNA and facilitate DNA accessibility to repair proteins (By similarity). Monoubiquitinated by RAG1 in lymphoid cells, monoubiquitination is required for V(D)J recombination.Lysine deamination at Lys-5 (H3K4all) to form allysine is mediated by LOXL2. Allysine formation by LOXL2 only takes place on H3K4me3 and results in gene repression (By similarity).Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes.Butyrylation of histones marks active promoters and competes with histone acetylation. It is present during late spermatogenesis.Hydroxybutyrylation of histones is induced by starvation. It is linked to gene activation and may replace histone acetylation on the promoter of specific genes in response to fasting.Succinylation at Lys-80 (H3K79succ) by KAT2A takes place with a maximum frequency around the transcription start sites of genes. It gives a specific tag for epigenetic transcription activation. Desuccinylation at Lys-123 (H3K122succ) by SIRT7 in response to DNA damage promotes chromatin condensation and double-strand breaks (DSBs) repair.Serine ADP-ribosylation by PARP1 or PARP2 constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage. Serine ADP-ribosylation at Ser-11 (H3S10ADPr) promotes recruitment of CHD1L. H3S10ADPr is mutually exclusive with phosphorylation at Ser-11 (H3S10ph) and impairs acetylation at Lys-10 (H3K9ac).Serotonylated by TGM2 at Gln-6 (H3Q5ser) during serotonergic neuron differentiation (PubMed:30867594). H3Q5ser is associated with trimethylation of Lys-5 (H3K4me3) and enhances general transcription factor IID (TFIID) complex-binding to H3K4me3, thereby facilitating transcription (PubMed:30867594).Dopaminylated by TGM2 at Gln-6 (H3Q5dop) in ventral tegmental area (VTA) neurons (By similarity). H3Q5dop mediates neurotransmission-independent role of nuclear dopamine by regulating relapse-related transcriptional plasticity in the reward system (By similarity).Lactylated in macrophages by EP300/P300 by using lactoyl-CoA directly derived from endogenous or exogenous lactate, leading to stimulates gene transcription.Belongs to the histone H3 family.Histone H3.2153881136Disordered43Asymmetric dimethylarginine; by PRMT6; alternate3Citrulline; alternatePhosphothreonine; by HASPIN4Allysine; alternate5N6,N6,N6-trimethyllysine; alternateN6,N6-dimethyllysine; alternateN6-(2-hydroxyisobutyryl)lysine; alternateN6-(beta-hydroxybutyryl)lysine; alternateN6-acetyllysine; alternateN6-crotonyllysine; alternateN6-methyllysine; alternate5-glutamyl dopamine; alternate65-glutamyl serotonin; alternatePhosphothreonine; by PKC7Citrulline; alternate9Symmetric dimethylarginine; by PRMT5; alternateN6,N6,N6-trimethyllysine; alternate10N6,N6-dimethyllysine; alternateN6-(2-hydroxyisobutyryl)lysine; alternateN6-(beta-hydroxybutyryl)lysine; alternateN6-acetyllysine; alternateN6-crotonyllysine; alternateN6-lactoyllysine; alternateN6-methyllysine; alternateADP-ribosylserine; alternate11Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5Phosphothreonine; by PKC12N6-(2-hydroxyisobutyryl)lysine; alternate15N6-(beta-hydroxybutyryl)lysine; alternateN6-acetyllysine; alternateN6-glutaryllysine; alternateN6-lactoyllysine; alternateN6-succinyllysine; alternateAsymmetric dimethylarginine; by CARM1; alternate18Citrulline; alternateN6-(2-hydroxyisobutyryl)lysine; alternate19N6-(beta-hydroxybutyryl)lysine; alternateN6-acetyllysine; alternateN6-butyryllysine; alternateN6-crotonyllysine; alternateN6-glutaryllysine; alternateN6-lactoyllysine; alternateN6-methyllysine; alternateN6-(2-hydroxyisobutyryl)lysine; alternate24N6-(beta-hydroxybutyryl)lysine; alternateN6-acetyllysine; alternateN6-butyryllysine; alternateN6-crotonyllysine; alternateN6-glutaryllysine; alternateN6-lactoyllysine; alternateN6-methyllysine; alternateCitrulline27N6,N6,N6-trimethyllysine; alternate28N6,N6-dimethyllysine; alternateN6-(2-hydroxyisobutyryl)lysine; alternateN6-acetyllysine; alternateN6-butyryllysine; alternateN6-crotonyllysine; alternateN6-glutaryllysine; alternateN6-lactoyllysine; alternateN6-methyllysine; alternateADP-ribosylserine; alternate29Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5N6,N6,N6-trimethyllysine; alternate37N6,N6-dimethyllysine; alternateN6-(2-hydroxyisobutyryl)lysine; alternateN6-acetyllysine; alternateN6-butyryllysine; alternateN6-methyllysine; alternateN6-butyryllysine; alternate38N6-methyllysine; alternatePhosphotyrosine42N6,N6,N6-trimethyllysine; alternate57N6-(2-hydroxyisobutyryl)lysine; alternateN6-(beta-hydroxybutyryl)lysine; alternateN6-acetyllysine; alternateN6-crotonyllysine; alternateN6-glutaryllysine; alternateN6-lactoyllysine; alternateN6-methyllysine; by EHMT2; alternateN6-succinyllysine; alternatePhosphoserine58N6-(2-hydroxyisobutyryl)lysine; alternate65N6-methyllysine; alternateN6,N6,N6-trimethyllysine; alternate80N6,N6-dimethyllysine; alternateN6-(2-hydroxyisobutyryl)lysine; alternateN6-acetyllysine; alternateN6-butyryllysine; alternateN6-glutaryllysine; alternateN6-lactoyllysine; alternateN6-methyllysine; alternateN6-succinyllysine; alternatePhosphothreonine81Phosphoserine87Phosphothreonine108N6-acetyllysine; alternate116N6-glutaryllysine; alternateN6-(2-hydroxyisobutyryl)lysine; alternate123N6-acetyllysine; alternateN6-butyryllysine; alternateN6-glutaryllysine; alternateN6-methyllysine; alternateN6-succinyllysine; alternateN6-decanoyllysineS-palmitoyl cysteine111true3HASPIN2007-01-23215388420dfce8d910d2eb7aa5c8d92bdae351MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERAtruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetrue