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}; Synonyms=H3.1-221, H3g, Hist1h3g;
GN and
GN Name=H3c10 {ECO:0000312|MGI:MGI:2448349}; Synonyms=H3.1-291, H3h, Hist1h3h;
GN and
GN Name=H3c11 {ECO:0000312|MGI:MGI:2448350}; 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 ---------------------------------------------------------------------------
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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 Genevisible; P68433; MM.
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.
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
//
