ID H31_MOUSE Reviewed; 136 AA. AC P68433; P02295; P02296; P16106; Q05A97; Q3B7Z8; Q3B7Z9; Q5T009; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 187. DE RecName: Full=Histone H3.1; GN Name=H3c1 {ECO:0000312|MGI:MGI:2668828}; Synonyms=H3a, Hist1h3a; GN and GN Name=H3c8 {ECO:0000312|MGI:MGI:2145541}; GN Synonyms=H3.1-221, H3g, Hist1h3g; GN and GN Name=H3c10 {ECO:0000312|MGI:MGI:2448349}; GN Synonyms=H3.1-291, H3h, Hist1h3h; GN and GN Name=H3c11 {ECO:0000312|MGI:MGI:2448350}; GN Synonyms=H3.1-I, H3i, Hist1h3i; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6314253; DOI=10.1093/nar/11.19.6679; RA Sittman D.B., Graves R.A., Marzluff W.F.; RT "Structure of a cluster of mouse histone genes."; RL Nucleic Acids Res. 11:6679-6697(1983). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (H3C8 AND H3C10). RX PubMed=3027355; DOI=10.1007/bf02115580; RA Taylor J.D., Wellman S.E., Marzluff W.F.; RT "Sequences of four mouse histone H3 genes: implications for evolution of RT mouse histone genes."; RL J. Mol. Evol. 23:242-249(1986). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=CD-1; TISSUE=Testis; RX PubMed=2587222; DOI=10.1093/nar/17.21.8861; RA Kosciessa U., Doenecke D.; RT "Nucleotide sequences of mouse histone genes H2A and H3.1."; RL Nucleic Acids Res. 17:8861-8861(1989). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (H3C11). RC STRAIN=C57BL/CJ6; RX PubMed=8858344; DOI=10.1101/gr.6.8.688; RA Wang Z.-F., Krasikov T., Frey M.R., Wang J., Matera A.G., Marzluff W.F.; RT "Characterization of the mouse histone gene cluster on chromosome 13: 45 RT histone genes in three patches spread over 1Mb."; RL Genome Res. 6:688-701(1996). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (H3C1; H3C8; H3C10 AND H3C11). 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 [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129/Sv; RA Franke K., Drabent B., Doenecke D.; RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [9] 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 [10] RP PROTEIN SEQUENCE OF 58-64, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=OF1; TISSUE=Hippocampus; RA Lubec G., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [11] RP DEVELOPMENTAL STAGE. RX PubMed=3018484; DOI=10.1128/mcb.5.11.2879-2886.1985; RA Brown D.T., Wellman S.E., Sittman D.B.; RT "Changes in the levels of three different classes of histone mRNA during RT murine erythroleukemia cell differentiation."; RL Mol. Cell. Biol. 5:2879-2886(1985). RN [12] RP PHOSPHORYLATION AT 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 [13] RP METHYLATION AT LYS-5 AND ARG-18. RX PubMed=11747826; DOI=10.1016/s0960-9822(01)00600-5; RA Ma H., Baumann C.T., Li H., Strahl B.D., Rice R., Jelinek M.A., Aswad D.W., RA Allis C.D., Hager G.L., Stallcup M.R.; RT "Hormone-dependent, CARM1-directed, arginine-specific methylation of RT histone H3 on a steroid-regulated promoter."; RL Curr. Biol. 11:1981-1985(2001). RN [14] RP PHOSPHORYLATION AT SER-29. RX PubMed=11441012; DOI=10.1074/jbc.m103973200; RA Zhong S., Jansen C., She Q.-B., Goto H., Inagaki M., Bode A.M., Ma W.-Y., RA Dong Z.; RT "Ultraviolet B-induced phosphorylation of histone H3 at serine 28 is RT mediated by MSK1."; RL J. Biol. Chem. 276:33213-33219(2001). RN [15] RP ACETYLATION AT LYS-15; LYS-19 AND LYS-24, AND METHYLATION AT ARG-18. RX PubMed=12498683; DOI=10.1016/s0960-9822(02)01387-8; RA Daujat S., Bauer U.-M., Shah V., Turner B., Berger S., Kouzarides T.; RT "Crosstalk between CARM1 methylation and CBP acetylation on histone H3."; RL Curr. Biol. 12:2090-2097(2002). RN [16] RP METHYLATION AT ARG-18. RX PubMed=11751582; DOI=10.1093/embo-reports/kvf013; RA Bauer U.-M., Daujat S., Nielsen S.J., Nightingale K., Kouzarides T.; RT "Methylation at arginine 17 of histone H3 is linked to gene activation."; RL EMBO Rep. 3:39-44(2002). RN [17] 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 [18] RP ACETYLATION AT LYS-15; LYS-19 AND LYS-24, METHYLATION AT LYS-10; LYS-28; RP LYS-37; LYS-80 AND LYS-123, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=13678296; DOI=10.1023/a:1025334006014; RA Cocklin R.R., Wang M.; RT "Identification of methylation and acetylation sites on mouse histone H3 RT using matrix-assisted laser desorption/ionization time-of-flight and RT nanoelectrospray ionization tandem mass spectrometry."; RL J. Protein Chem. 22:327-334(2003). RN [19] RP CITRULLINATION AT ARG-3; ARG-9; ARG-18 AND ARG-27. RX PubMed=15339660; DOI=10.1016/j.cell.2004.08.020; RA Cuthbert G.L., Daujat S., Snowden A.W., Erdjument-Bromage H., Hagiwara T., RA Yamada M., Schneider R., Gregory P.D., Tempst P., Bannister A.J., RA Kouzarides T.; RT "Histone deimination antagonizes arginine methylation."; RL Cell 118:545-553(2004). RN [20] RP METHYLATION AT ARG-9, AND ACETYLATION AT LYS-10. RX PubMed=15485929; DOI=10.1128/mcb.24.21.9630-9645.2004; RA Pal S., Vishwanath S.N., Erdjument-Bromage H., Tempst P., Sif S.; RT "Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and RT negatively regulates expression of ST7 and NM23 tumor suppressor genes."; RL Mol. Cell. Biol. 24:9630-9645(2004). RN [21] RP METHYLATION AT ARG-18. RX PubMed=15616592; DOI=10.1038/sj.emboj.7600500; RA Covic M., Hassa P.O., Saccani S., Buerki C., Meier N.I., Lombardi C., RA Imhof R., Bedford M.T., Natoli G., Hottiger M.O.; RT "Arginine methyltransferase CARM1 is a promoter-specific regulator of NF- RT kappaB-dependent gene expression."; RL EMBO J. 24:85-96(2005). RN [22] RP PHOSPHORYLATION AT THR-4 AND SER-11. 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 [23] 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 [24] RP PHOSPHORYLATION AT SER-11 AND SER-29. RX PubMed=15870105; DOI=10.1242/jcs.02373; RA Dyson M.H., Thomson S., Inagaki M., Goto H., Arthur S.J., Nightingale K., RA Iborra F.J., Mahadevan L.C.; RT "MAP kinase-mediated phosphorylation of distinct pools of histone H3 at S10 RT or S28 via mitogen- and stress-activated kinase 1/2."; RL J. Cell Sci. 118:2247-2259(2005). RN [25] RP PHOSPHORYLATION AT SER-11 AND SER-29. RX PubMed=15735677; DOI=10.1038/sj.onc.1208521; RA Dunn K.L., Davie J.R.; RT "Stimulation of the Ras-MAPK pathway leads to independent phosphorylation RT of histone H3 on serine 10 and 28."; RL Oncogene 24:3492-3502(2005). RN [26] RP ACETYLATION AT LYS-5; LYS-10; LYS-15; LYS-19; LYS-24 AND LYS-28, RP METHYLATION AT LYS-5; LYS-10; LYS-19; LYS-24; LYS-28; LYS-37 AND LYS-80, RP AND IDENTIFICATION BY MASS 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 [27] 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 [28] RP PHOSPHORYLATION AT THR-12 BY CHEK1. RX PubMed=18243098; DOI=10.1016/j.cell.2007.12.013; RA Shimada M., Niida H., Zineldeen D.H., Tagami H., Tanaka M., Saito H., RA Nakanishi M.; RT "Chk1 is a histone H3 threonine 11 kinase that regulates DNA damage-induced RT transcriptional repression."; RL Cell 132:221-232(2008). RN [29] RP UBIQUITINATION. RX PubMed=20122409; DOI=10.1016/j.molcel.2009.12.035; RA Grazini U., Zanardi F., Citterio E., Casola S., Goding C.R., McBlane F.; RT "The RING domain of RAG1 ubiquitylates histone H3: a novel activity in RT chromatin-mediated regulation of V(D)J joining."; RL Mol. Cell 37:282-293(2010). RN [30] 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 [31] RP SUCCINYLATION AT LYS-57 AND LYS-80. 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 [32] 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 [33] RP BUTYRYLATION AT LYS-19; LYS-24; LYS-28; LYS-37; LYS-38; LYS-80 AND LYS-123. 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 [34] RP HYDROXYBUTYRYLATION AT LYS-5; LYS-10; LYS-15; LYS-19; LYS-24 AND LYS-57. 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 [35] RP CROTONYLATION AT LYS-19, AND ACETYLATION AT LYS-19. RX PubMed=30279482; DOI=10.1038/s41598-018-32927-9; RA Kelly R.D.W., Chandru A., Watson P.J., Song Y., Blades M., Robertson N.S., RA Jamieson A.G., Schwabe J.W.R., Cowley S.M.; RT "Histone deacetylase (HDAC) 1 and 2 complexes regulate both histone RT acetylation and crotonylation in vivo."; RL Sci. Rep. 8:14690-14690(2018). RN [36] 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 [37] RP LACTYLATION AT LYS-15; LYS-19; LYS-24; LYS-28 AND LYS-57. 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). 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. Interacts with TONSL; CHAF1A; CHAF1B; MCM2 and DNAJC9 (By CC similarity). {ECO:0000250|UniProtKB:P68431}. CC -!- INTERACTION: CC P68433; P83917: Cbx1; NbExp=6; IntAct=EBI-79743, EBI-78119; CC P68433; Q8WTS6: SETD7; Xeno; NbExp=2; IntAct=EBI-79743, EBI-1268586; 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. {ECO:0000269|PubMed:3018484}. 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:11747826, CC ECO:0000269|PubMed:11751582, ECO:0000269|PubMed:12498683, CC ECO:0000269|PubMed:13678296, ECO:0000269|PubMed:15485929, CC ECO:0000269|PubMed:15616592, ECO:0000269|PubMed:17194708}. CC -!- PTM: Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 CC impairs methylation and represses transcription. CC {ECO:0000269|PubMed:11747826, ECO:0000269|PubMed:11751582, CC ECO:0000269|PubMed:12498683, ECO:0000269|PubMed:15339660, CC ECO:0000269|PubMed:15485929, ECO:0000269|PubMed:15616592}. 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 (By similarity). {ECO:0000250|UniProtKB:P68431}. 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:11747826, ECO:0000269|PubMed:11856369, CC ECO:0000269|PubMed:13678296, ECO:0000269|PubMed:15485929, CC ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:15735677, CC ECO:0000269|PubMed:15870105, ECO:0000269|PubMed:17189264, CC ECO:0000269|PubMed:17194708}. 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 Thr-12 (H3T11ph) by chromatin-associated CHEK1 CC regulates the transcription of cell cycle regulatory genes by CC modulating acetylation of Lys-10 (H3K9ac). Phosphorylation at Tyr-42 CC (H3Y41ph) by JAK2 promotes exclusion of CBX5 (HP1 alpha) from CC chromatin. {ECO:0000269|PubMed:10464286, ECO:0000269|PubMed:11441012, CC ECO:0000269|PubMed:11747826, ECO:0000269|PubMed:11856369, CC ECO:0000269|PubMed:13678296, ECO:0000269|PubMed:15485929, CC ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:15684425, CC ECO:0000269|PubMed:15735677, ECO:0000269|PubMed:15870105, CC ECO:0000269|PubMed:17194708, ECO:0000269|PubMed:18243098}. CC -!- PTM: Ubiquitinated by the CUL4-DDB-RBX1 complex in response to CC ultraviolet irradiation. This may weaken the interaction between CC histones and DNA and facilitate DNA accessibility to repair proteins CC (By similarity). Monoubiquitinated by RAG1 in lymphoid cells, CC monoubiquitination is required for V(D)J recombination. {ECO:0000250, CC ECO:0000269|PubMed:20122409}. 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 (By similarity). CC {ECO:0000250|UniProtKB:P68431}. 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:0000269|PubMed:27105113}. CC -!- PTM: Hydroxybutyrylation of histones is induced by starvation. It is CC linked to gene activation and may replace histone acetylation on the CC promoter of specific genes in response to fasting. CC {ECO:0000269|PubMed:27105115}. CC -!- PTM: Succinylation at Lys-80 (H3K79succ) by KAT2A takes place with a CC maximum frequency around the transcription start sites of genes. It CC gives a specific tag for epigenetic transcription activation. CC Desuccinylation at Lys-123 (H3K122succ) by SIRT7 in response to DNA CC damage promotes chromatin condensation and double-strand breaks (DSBs) CC repair. {ECO:0000250|UniProtKB:P68431}. CC -!- PTM: Serine ADP-ribosylation by PARP1 or PARP2 constitutes the primary CC form of ADP-ribosylation of proteins in response to DNA damage. Serine CC ADP-ribosylation at Ser-11 (H3S10ADPr) promotes recruitment of CHD1L. CC H3S10ADPr is mutually exclusive with phosphorylation at Ser-11 CC (H3S10ph) and impairs acetylation at Lys-10 (H3K9ac). CC {ECO:0000250|UniProtKB:P68431}. 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 (By similarity). 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:P68431, ECO:0000250|UniProtKB:Q6LED0}. 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:0000250|UniProtKB:P68431}. CC -!- MISCELLANEOUS: This histone is only present in mammals. CC -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X01684; CAA25839.1; -; Genomic_DNA. DR EMBL; M32460; AAA37811.1; -; Genomic_DNA. DR EMBL; M32462; AAA37813.1; -; Genomic_DNA. DR EMBL; X16496; CAA34512.1; -; Genomic_DNA. DR EMBL; U62670; AAB04763.1; -; Genomic_DNA. DR EMBL; U62672; AAB04765.1; -; Genomic_DNA. DR EMBL; AY158944; AAO06254.1; -; Genomic_DNA. DR EMBL; AY158945; AAO06255.1; -; Genomic_DNA. DR EMBL; AY158946; AAO06256.1; -; Genomic_DNA. DR EMBL; AY158952; AAO06262.1; -; Genomic_DNA. DR EMBL; Y12290; CAA72968.1; -; Genomic_DNA. DR EMBL; AK006742; BAB24722.1; -; mRNA. DR EMBL; AK018952; BAB31493.1; -; mRNA. DR EMBL; AK155722; BAE33402.1; -; mRNA. DR EMBL; AL589651; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL590388; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC107285; AAI07286.1; -; mRNA. DR EMBL; BC107287; AAI07288.1; -; mRNA. DR EMBL; BC115816; AAI15817.1; -; mRNA. DR EMBL; BC116383; AAI16384.1; -; mRNA. DR EMBL; BC125355; AAI25356.1; -; mRNA. DR EMBL; BC125357; AAI25358.1; -; mRNA. DR CCDS; CCDS26289.1; -. DR CCDS; CCDS26296.1; -. DR CCDS; CCDS26342.1; -. DR CCDS; CCDS26368.1; -. DR PIR; A39525; A39525. DR PIR; S06755; S06755. DR RefSeq; NP_038578.2; NM_013550.5. DR RefSeq; NP_659539.1; NM_145073.2. DR RefSeq; NP_835513.1; NM_178206.2. DR RefSeq; NP_835514.1; NM_178207.2. DR PDB; 1GUW; NMR; -; B=2-17. DR PDB; 1U35; X-ray; 3.00 A; A/E=1-136. DR PDB; 2V83; X-ray; 2.40 A; D/E=2-10. DR PDB; 2W5Z; X-ray; 2.20 A; C=2-9. DR PDB; 2WP1; X-ray; 2.10 A; P/Q=15-24. DR PDB; 2XL3; X-ray; 2.70 A; D/F=2-9. DR PDB; 4EZH; X-ray; 2.52 A; C/D=25-35. DR PDB; 5B1L; X-ray; 2.35 A; A/E=1-136. DR PDB; 5B1M; X-ray; 2.34 A; A/E=1-136. DR PDB; 5IX1; X-ray; 2.60 A; P/Q=2-16. DR PDB; 5IX2; X-ray; 2.90 A; P/Q=2-33. DR PDB; 7OS4; X-ray; 2.54 A; E/F/G/H=14-32. DR PDB; 7QPH; X-ray; 1.90 A; E/F/G/H=23-32. DR PDB; 7QRD; X-ray; 2.00 A; L/M=11-26. DR PDB; 7VFI; EM; 3.98 A; C=53-61. DR PDBsum; 1GUW; -. DR PDBsum; 1U35; -. DR PDBsum; 2V83; -. DR PDBsum; 2W5Z; -. DR PDBsum; 2WP1; -. DR PDBsum; 2XL3; -. DR PDBsum; 4EZH; -. DR PDBsum; 5B1L; -. DR PDBsum; 5B1M; -. DR PDBsum; 5IX1; -. DR PDBsum; 5IX2; -. DR PDBsum; 7OS4; -. DR PDBsum; 7QPH; -. DR PDBsum; 7QRD; -. DR PDBsum; 7VFI; -. DR AlphaFoldDB; P68433; -. DR SMR; P68433; -. DR BioGRID; 220918; 3. DR BioGRID; 237523; 4. DR ComplexPortal; CPX-5712; Nucleosome, variant H3.1-H2A.2-H2B.1. DR ComplexPortal; CPX-5714; Nucleosome, variant H3.g-H2A.2-H2B.1. DR ComplexPortal; CPX-5715; Nucleosome, variant H3.1-H2A.Z-H2B.1. DR ComplexPortal; CPX-5716; Nucleosome, variant H3.1-H2A.V-H2B.1. DR IntAct; P68433; 26. DR MINT; P68433; -. DR STRING; 10090.ENSMUSP00000079670; -. DR GlyGen; P68433; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P68433; -. DR MetOSite; P68433; -. DR PhosphoSitePlus; P68433; -. DR SwissPalm; P68433; -. DR EPD; P68433; -. DR jPOST; P68433; -. DR MaxQB; P68433; -. DR PaxDb; 10090-ENSMUSP00000079670; -. DR ProteomicsDB; 269794; -. DR Pumba; P68433; -. DR TopDownProteomics; P68433; -. DR ABCD; P68433; 6 sequenced antibodies. DR DNASU; 319152; -. DR DNASU; 319153; -. DR DNASU; 360198; -. DR DNASU; 97908; -. DR Ensembl; ENSMUST00000080859.8; ENSMUSP00000079670.6; ENSMUSG00000099517.3. DR Ensembl; ENSMUST00000091701.3; ENSMUSP00000089293.3; ENSMUSG00000069265.3. DR Ensembl; ENSMUST00000188775.2; ENSMUSP00000140394.2; ENSMUSG00000101355.2. DR Ensembl; ENSMUST00000189457.2; ENSMUSP00000139663.2; ENSMUSG00000101972.2. DR GeneID; 319152; -. DR GeneID; 319153; -. DR GeneID; 360198; -. DR GeneID; 97908; -. DR KEGG; mmu:319152; -. DR KEGG; mmu:319153; -. DR KEGG; mmu:360198; -. DR KEGG; mmu:97908; -. DR UCSC; uc007prc.1; mouse. DR AGR; MGI:2145541; -. DR AGR; MGI:2448349; -. DR AGR; MGI:2448350; -. DR AGR; MGI:2668828; -. DR CTD; 8350; -. DR CTD; 8354; -. DR CTD; 8355; -. DR CTD; 8357; -. DR MGI; MGI:2668828; H3c1. DR MGI; MGI:2448349; H3c10. DR MGI; MGI:2448350; H3c11. DR MGI; MGI:2145541; H3c8. DR VEuPathDB; HostDB:ENSMUSG00000069265; -. DR VEuPathDB; HostDB:ENSMUSG00000099517; -. DR VEuPathDB; HostDB:ENSMUSG00000101355; -. DR VEuPathDB; HostDB:ENSMUSG00000101972; -. DR eggNOG; KOG1745; Eukaryota. DR GeneTree; ENSGT01100000263514; -. DR HOGENOM; CLU_078295_4_0_1; -. DR InParanoid; P68433; -. DR OMA; ICIVICK; -. DR OrthoDB; 3867165at2759; -. DR PhylomeDB; P68433; -. DR TreeFam; TF314241; -. DR Reactome; R-MMU-1266695; Interleukin-7 signaling. DR Reactome; R-MMU-212300; PRC2 methylates histones and DNA. DR Reactome; R-MMU-3214841; PKMTs methylate histone lysines. DR Reactome; R-MMU-3214842; HDMs demethylate histones. DR Reactome; R-MMU-3214847; HATs acetylate histones. DR Reactome; R-MMU-3214858; RMTs methylate histone arginines. DR Reactome; R-MMU-3247509; Chromatin modifying enzymes. DR Reactome; R-MMU-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function. DR Reactome; R-MMU-9018519; Estrogen-dependent gene expression. DR Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production. DR BioGRID-ORCS; 319152; 11 hits in 41 CRISPR screens. DR BioGRID-ORCS; 319153; 10 hits in 41 CRISPR screens. DR BioGRID-ORCS; 360198; 11 hits in 45 CRISPR screens. DR BioGRID-ORCS; 97908; 14 hits in 43 CRISPR screens. DR ChiTaRS; Zfp106; mouse. DR EvolutionaryTrace; P68433; -. DR PRO; PR:P68433; -. DR Proteomes; UP000000589; Chromosome 13. DR RNAct; P68433; Protein. DR Bgee; ENSMUSG00000069265; Expressed in uterus and 55 other cell types or tissues. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0000786; C:nucleosome; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; ISO:MGI. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro. DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro. DR GO; GO:0006325; P:chromatin organization; NAS:ComplexPortal. DR Gene3D; 1.10.20.10; Histone, subunit A; 1. DR InterPro; IPR009072; Histone-fold. DR InterPro; IPR007125; Histone_H2A/H2B/H3. DR InterPro; IPR000164; Histone_H3/CENP-A. DR PANTHER; PTHR11426; HISTONE H3; 1. DR PANTHER; PTHR11426:SF242; HISTONE H3.1; 1. DR Pfam; PF00125; Histone; 1. DR PRINTS; PR00622; HISTONEH3. DR SMART; SM00428; H3; 1. DR SUPFAM; SSF47113; Histone-fold; 1. DR PROSITE; PS00322; HISTONE_H3_1; 1. DR PROSITE; PS00959; HISTONE_H3_2; 1. DR Genevisible; P68433; MM. 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; Phosphoprotein; Reference proteome; KW Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P68431" FT CHAIN 2..136 FT /note="Histone H3.1" FT /id="PRO_0000221249" 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:0000250|UniProtKB:P68431" FT MOD_RES 3 FT /note="Citrulline; alternate" FT /evidence="ECO:0000269|PubMed:15339660" FT MOD_RES 3 FT /note="Phosphoarginine; alternate" FT /evidence="ECO:0000305" FT MOD_RES 4 FT /note="Phosphothreonine; by HASPIN" FT /evidence="ECO:0000269|PubMed:15681610" FT MOD_RES 5 FT /note="Allysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 5 FT /note="N6,N6,N6-trimethyllysine; alternate" FT /evidence="ECO:0000269|PubMed:11747826, FT ECO:0000269|PubMed:17194708" FT MOD_RES 5 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000269|PubMed:11747826, 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 MOD_RES 5 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000269|PubMed:11747826, FT ECO:0000269|PubMed:17194708" FT MOD_RES 6 FT /note="5-glutamyl dopamine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" 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:0000250|UniProtKB:P68431" FT MOD_RES 9 FT /note="Citrulline; alternate" FT /evidence="ECO:0000269|PubMed:15339660" FT MOD_RES 9 FT /note="Symmetric dimethylarginine; by PRMT5; alternate" FT /evidence="ECO:0000269|PubMed:15485929" FT MOD_RES 10 FT /note="N6,N6,N6-trimethyllysine; alternate" FT /evidence="ECO:0000269|PubMed:13678296, FT ECO:0000269|PubMed:17194708" FT MOD_RES 10 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000269|PubMed:13678296, 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:15485929, FT ECO:0000269|PubMed:17194708" FT MOD_RES 10 FT /note="N6-crotonyllysine; alternate" FT /evidence="ECO:0000269|PubMed:21925322" FT MOD_RES 10 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 10 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000269|PubMed:13678296, FT ECO:0000269|PubMed:17194708" FT MOD_RES 11 FT /note="ADP-ribosylserine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" 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:15681610, FT ECO:0000269|PubMed:15735677, ECO:0000269|PubMed:15870105" FT MOD_RES 12 FT /note="Phosphothreonine; by PKC and CHEK1" FT /evidence="ECO:0000250|UniProtKB:P68431" 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:12498683, FT ECO:0000269|PubMed:13678296, ECO:0000269|PubMed:17194708" FT MOD_RES 15 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 15 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000269|PubMed:31645732" FT MOD_RES 15 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 18 FT /note="Asymmetric dimethylarginine; by CARM1; alternate" FT /evidence="ECO:0000269|PubMed:11747826, FT ECO:0000269|PubMed:11751582, ECO:0000269|PubMed:12498683, FT ECO:0000269|PubMed:15616592" FT MOD_RES 18 FT /note="Citrulline; alternate" FT /evidence="ECO:0000269|PubMed:15339660" 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:12498683, FT ECO:0000269|PubMed:13678296, ECO:0000269|PubMed:17194708, FT ECO:0000269|PubMed:30279482" 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 ECO:0000269|PubMed:30279482" FT MOD_RES 19 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" 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: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:12498683, FT ECO:0000269|PubMed:13678296, 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 MOD_RES 24 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" 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:15339660" FT MOD_RES 28 FT /note="N6,N6,N6-trimethyllysine; alternate" FT /evidence="ECO:0000269|PubMed:13678296, FT ECO:0000269|PubMed:17194708" FT MOD_RES 28 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000269|PubMed:13678296, 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-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:17194708" FT MOD_RES 28 FT /note="N6-butyryllysine; alternate" FT /evidence="ECO:0000269|PubMed:27105113" 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:0000250|UniProtKB:P68431" 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:13678296, FT ECO:0000269|PubMed:17194708" FT MOD_RES 29 FT /note="ADP-ribosylserine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 29 FT /note="Phosphoserine; alternate; by AURKB, AURKC and FT RPS6KA5" FT /evidence="ECO:0000269|PubMed:10464286, FT ECO:0000269|PubMed:11441012, ECO:0000269|PubMed:11856369, FT ECO:0000269|PubMed:15684425, ECO:0000269|PubMed:15735677, FT ECO:0000269|PubMed:15870105" FT MOD_RES 37 FT /note="N6,N6,N6-trimethyllysine; alternate" FT /evidence="ECO:0000305|PubMed:13678296, FT ECO:0000305|PubMed:17194708" FT MOD_RES 37 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000269|PubMed:13678296, 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 MOD_RES 37 FT /note="N6-butyryllysine; alternate" FT /evidence="ECO:0000269|PubMed:27105113" FT MOD_RES 37 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000269|PubMed:13678296, FT ECO:0000269|PubMed:17194708" FT MOD_RES 38 FT /note="N6-butyryllysine; alternate" FT /evidence="ECO:0000269|PubMed:27105113" FT MOD_RES 38 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 42 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 57 FT /note="N6,N6,N6-trimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" 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:0000250|UniProtKB:P68431" 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:0000250|UniProtKB:P68431" FT MOD_RES 57 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000269|PubMed:31645732" FT MOD_RES 57 FT /note="N6-methyllysine; by EHMT2; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" 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:0000250|UniProtKB:P68431" 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:0000250|UniProtKB:P68431" FT MOD_RES 80 FT /note="N6,N6,N6-trimethyllysine; alternate" FT /evidence="ECO:0000269|PubMed:13678296, FT ECO:0000269|PubMed:17194708" FT MOD_RES 80 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000269|PubMed:13678296, 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-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 80 FT /note="N6-butyryllysine; alternate" FT /evidence="ECO:0000269|PubMed:27105113" FT MOD_RES 80 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 80 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 80 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000269|PubMed:13678296, FT ECO:0000269|PubMed:17194708" FT MOD_RES 80 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000269|PubMed:22389435" FT MOD_RES 81 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 87 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P84243" FT MOD_RES 108 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 116 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 116 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 123 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000269|PubMed:24681537" FT MOD_RES 123 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 123 FT /note="N6-butyryllysine; alternate" FT /evidence="ECO:0000269|PubMed:27105113" FT MOD_RES 123 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 123 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000269|PubMed:13678296" FT MOD_RES 123 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 129 FT /note="Phosphoarginine" FT /evidence="ECO:0000305" FT MOD_RES 130 FT /note="Phosphoarginine" FT /evidence="ECO:0000305" FT MOD_RES 132 FT /note="Phosphoarginine" FT /evidence="ECO:0000255" FT LIPID 19 FT /note="N6-decanoyllysine" FT /evidence="ECO:0000250|UniProtKB:P68431" FT STRAND 4..7 FT /evidence="ECO:0007829|PDB:5IX1" FT HELIX 46..57 FT /evidence="ECO:0007829|PDB:5B1M" FT HELIX 65..77 FT /evidence="ECO:0007829|PDB:5B1M" FT STRAND 80..82 FT /evidence="ECO:0007829|PDB:5B1M" FT HELIX 87..114 FT /evidence="ECO:0007829|PDB:5B1M" FT STRAND 118..120 FT /evidence="ECO:0007829|PDB:5B1M" FT HELIX 122..131 FT /evidence="ECO:0007829|PDB:5B1M" SQ SEQUENCE 136 AA; 15404 MW; 9B89008EA50A0EF6 CRC64; MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEACEAY LVGLFEDTNL CAIHAKRVTI MPKDIQLARR IRGERA //