H33_MOUSE
ID H33_MOUSE Reviewed; 136 AA.
AC P84244; P06351; P33155; Q3TW79; Q3U6D6; Q569U8; Q5HZY8; Q6TXQ5; Q8VDJ2;
AC Q9D0H3; Q9V3W4;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Histone H3.3;
GN Name=H3-3a {ECO:0000250|UniProtKB:P84243};
GN Synonyms=H3.3a, H3f3a {ECO:0000312|MGI:MGI:1097686};
GN and
GN Name=H3-3b {ECO:0000250|UniProtKB:P84243};
GN Synonyms=H3.3b, H3f3b {ECO:0000312|MGI:MGI:1101768};
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 [MRNA] (H3-3A).
RX PubMed=2470025; DOI=10.1093/nar/17.7.2449;
RA Hraba-Renevey S., Kress M.;
RT "Expression of a mouse replacement histone H3.3 gene with a highly
RT conserved 3' noncoding region during SV40- and polyoma-induced Go to S-
RT phase transition.";
RL Nucleic Acids Res. 17:2449-2461(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (H3-3A AND H3-3B), AND DEVELOPMENTAL STAGE.
RC TISSUE=Spermatid;
RX PubMed=9373943; DOI=10.1046/j.1432-0436.1997.6210013.x;
RA Bramlage B., Kosciessa U., Doenecke D.;
RT "Differential expression of the murine histone genes H3.3A and H3.3B.";
RL Differentiation 62:13-20(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (H3-3A).
RC STRAIN=SWR/J; TISSUE=Ovary;
RX PubMed=9174168; DOI=10.1089/dna.1997.16.639;
RA Lopez-Alanon D.M., Lopez-Fernandez L.A., Castaneda V., Krimer D.B.,
RA Del Mazo J.;
RT "H3.3A variant histone mRNA containing an alpha-globin insertion: modulated
RT expression during mouse gametogenesis correlates with meiotic onset.";
RL DNA Cell Biol. 16:639-644(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (H3-3A AND H3-3B).
RC STRAIN=BALB/cJ, C57BL/6J, DBA/2J, and NOD;
RC TISSUE=Bone marrow, Egg, Head, Kidney, Muellerian duct, Stomach, and
RC Thymus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (H3-3A AND H3-3B).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, Colon, Mammary tumor, and Retina;
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-122.
RX PubMed=15638457; DOI=10.1007/s00239-004-2637-4;
RA Mancini P., Pulcrano G., Piscopo M., Aniello F., Branno M., Fucci L.;
RT "A new family of 'H3L-like' histone genes.";
RL J. Mol. Evol. 59:458-463(2004).
RN [7]
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 [8]
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 [9]
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 [10]
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 [11]
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 [12]
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 [13]
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 [14]
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 [15]
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 [16]
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 [17]
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 [18]
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 [19]
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 [20]
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 [21]
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 [22]
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 [23]
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 [24]
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 [25]
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 [26]
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 [27]
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 [28]
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 [29]
RP SEROTONYLATION AT GLN-6, AND MUTAGENESIS OF 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 [30]
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: Variant histone H3 which replaces conventional H3 in a wide
CC range of nucleosomes in active genes. Constitutes the predominant form
CC of histone H3 in non-dividing cells and is incorporated into chromatin
CC independently of DNA synthesis. Deposited at sites of nucleosomal
CC displacement throughout transcribed genes, suggesting that it
CC represents an epigenetic imprint of transcriptionally active chromatin.
CC Nucleosomes wrap and compact DNA into chromatin, limiting DNA
CC accessibility to the cellular machineries which require DNA as a
CC template. Histones thereby play a central role in transcription
CC regulation, DNA repair, DNA replication and chromosomal stability. DNA
CC accessibility is regulated via a complex set of post-translational
CC modifications of histones, also called histone code, and nucleosome
CC remodeling. {ECO:0000250|UniProtKB:P84243}.
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 HIRA, a chaperone required for its incorporation
CC into nucleosomes. Interacts with ZMYND11; when trimethylated at 'Lys-
CC 36' (H3.3K36me3). Found in a co-chaperone complex with DNJC9, MCM2 and
CC histone H3.3-H4 dimers (By similarity). Within the complex, interacts
CC with DNJC9 (via C-terminus); the interaction is direct (By similarity).
CC Interacts with ASF1A, MCM2, NASP and SPT2 (By similarity).
CC {ECO:0000250|UniProtKB:P84243}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout the cell cycle independently
CC of DNA synthesis. {ECO:0000269|PubMed:9373943}.
CC -!- DOMAIN: Specific interaction of trimethylated form at 'Lys-36'
CC (H3.3K36me3) with ZMYND11 is mediated by the encapsulation of Ser-32
CC residue with a composite pocket formed by the tandem bromo-PWWP domains
CC (By similarity). Interacts with ZMYND11; when trimethylated at 'Lys-36'
CC (H3.3K36me3). {ECO:0000250|UniProtKB:P84243}.
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:11751582,
CC ECO:0000269|PubMed:12498683, ECO:0000269|PubMed:13678296,
CC ECO:0000269|PubMed:15485929, ECO:0000269|PubMed:15616592,
CC 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:11751582, ECO:0000269|PubMed:12498683,
CC ECO:0000269|PubMed:15339660, ECO:0000269|PubMed:15485929,
CC 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. {ECO:0000250|UniProtKB:P84243}.
CC -!- PTM: Specifically enriched in modifications associated with active
CC chromatin such as methylation at Lys-5 (H3K4me), Lys-37 and Lys-80.
CC Methylation at Lys-5 (H3K4me) facilitates subsequent acetylation of H3
CC and H4. Methylation at Lys-80 (H3K79me) is associated with DNA double-
CC strand break (DSB) responses and is a specific target for TP53BP1.
CC Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me), which are linked
CC to gene repression, are underrepresented. Methylation at Lys-10
CC (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:11856369, ECO:0000269|PubMed:13678296,
CC ECO:0000269|PubMed:15485929, ECO:0000269|PubMed:15681610,
CC ECO:0000269|PubMed:15735677, ECO:0000269|PubMed:15870105,
CC ECO:0000269|PubMed:17189264, 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 Tyr-42 (H3Y41ph) by JAK2 promotes exclusion of CBX5
CC (HP1 alpha) from chromatin. Phosphorylation on Ser-32 (H3S31ph) is
CC specific to regions bordering centromeres in metaphase chromosomes.
CC metaphase chromosomes. {ECO:0000269|PubMed:10464286,
CC ECO:0000269|PubMed:11441012, 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}.
CC -!- PTM: Ubiquitinated. Monoubiquitinated by RAG1 in lymphoid cells,
CC monoubiquitination is required for V(D)J recombination.
CC {ECO:0000305|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. {ECO:0000250|UniProtKB:P84243}.
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:P84243}.
CC -!- PTM: Serine ADP-ribosylation constitutes the primary form of ADP-
CC ribosylation of proteins in response to DNA damage. Serine ADP-
CC ribosylation at Ser-11 (H3S10ADPr) is mutually exclusive with
CC phosphorylation at Ser-11 (H3S10ph) and impairs acetylation at Lys-10
CC (H3K9ac). {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:P84243, ECO:0000250|UniProtKB:P84245}.
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:P84243}.
CC -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH92300.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB27616.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAE35387.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
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DR EMBL; X13605; CAA31940.1; -; mRNA.
DR EMBL; Z85979; CAB06625.1; -; mRNA.
DR EMBL; X91866; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK002928; BAB22464.1; -; mRNA.
DR EMBL; AK011431; BAB27616.1; ALT_FRAME; mRNA.
DR EMBL; AK037900; BAC29895.1; -; mRNA.
DR EMBL; AK088075; BAC40130.1; -; mRNA.
DR EMBL; AK135839; BAE22687.1; -; mRNA.
DR EMBL; AK150467; BAE29584.1; -; mRNA.
DR EMBL; AK150468; BAE29585.1; -; mRNA.
DR EMBL; AK150591; BAE29685.1; -; mRNA.
DR EMBL; AK150928; BAE29966.1; -; mRNA.
DR EMBL; AK151274; BAE30261.1; -; mRNA.
DR EMBL; AK151336; BAE30314.1; -; mRNA.
DR EMBL; AK151451; BAE30411.1; -; mRNA.
DR EMBL; AK151634; BAE30566.1; -; mRNA.
DR EMBL; AK151658; BAE30586.1; -; mRNA.
DR EMBL; AK151661; BAE30589.1; -; mRNA.
DR EMBL; AK151869; BAE30757.1; -; mRNA.
DR EMBL; AK152293; BAE31102.1; -; mRNA.
DR EMBL; AK152453; BAE31231.1; -; mRNA.
DR EMBL; AK152455; BAE31233.1; -; mRNA.
DR EMBL; AK152623; BAE31366.1; -; mRNA.
DR EMBL; AK152911; BAE31590.1; -; mRNA.
DR EMBL; AK153034; BAE31666.1; -; mRNA.
DR EMBL; AK153189; BAE31789.1; -; mRNA.
DR EMBL; AK153239; BAE31831.1; -; mRNA.
DR EMBL; AK153294; BAE31877.1; -; mRNA.
DR EMBL; AK153371; BAE31939.1; -; mRNA.
DR EMBL; AK153530; BAE32069.1; -; mRNA.
DR EMBL; AK159615; BAE35232.1; -; mRNA.
DR EMBL; AK159807; BAE35387.1; ALT_FRAME; mRNA.
DR EMBL; AK159850; BAE35427.1; -; mRNA.
DR EMBL; AK160677; BAE35953.1; -; mRNA.
DR EMBL; AK161675; BAE36524.1; -; mRNA.
DR EMBL; AK162040; BAE36694.1; -; mRNA.
DR EMBL; AK163244; BAE37253.1; -; mRNA.
DR EMBL; AK167828; BAE39850.1; -; mRNA.
DR EMBL; AK167879; BAE39892.1; -; mRNA.
DR EMBL; AK168197; BAE40157.1; -; mRNA.
DR EMBL; AK168698; BAE40542.1; -; mRNA.
DR EMBL; AK169042; BAE40831.1; -; mRNA.
DR EMBL; AK169226; BAE40995.1; -; mRNA.
DR EMBL; BC002268; AAH02268.1; -; mRNA.
DR EMBL; BC012687; AAH12687.1; -; mRNA.
DR EMBL; BC021768; AAH21768.1; -; mRNA.
DR EMBL; BC037730; AAH37730.1; -; mRNA.
DR EMBL; BC083353; AAH83353.1; -; mRNA.
DR EMBL; BC088835; AAH88835.1; -; mRNA.
DR EMBL; BC092043; AAH92043.1; -; mRNA.
DR EMBL; BC092300; AAH92300.1; ALT_FRAME; mRNA.
DR EMBL; BC106177; AAI06178.1; -; mRNA.
DR EMBL; AY383567; AAQ96274.1; -; Genomic_DNA.
DR CCDS; CCDS15573.1; -.
DR CCDS; CCDS36377.1; -.
DR PIR; S04186; S04186.
DR RefSeq; NP_032236.1; NM_008210.5.
DR RefSeq; NP_032237.1; NM_008211.3.
DR RefSeq; XP_006532311.1; XM_006532248.2.
DR PDB; 2RVN; NMR; -; B=2-18.
DR PDB; 5XM0; X-ray; 2.87 A; A/E=1-136.
DR PDB; 5XM1; X-ray; 3.45 A; A/E=1-136.
DR PDBsum; 2RVN; -.
DR PDBsum; 5XM0; -.
DR PDBsum; 5XM1; -.
DR AlphaFoldDB; P84244; -.
DR SMR; P84244; -.
DR BioGRID; 200196; 28.
DR BioGRID; 200199; 4.
DR DIP; DIP-35190N; -.
DR IntAct; P84244; 37.
DR MINT; P84244; -.
DR STRING; 10090.ENSMUSP00000102062; -.
DR iPTMnet; P84244; -.
DR PhosphoSitePlus; P84244; -.
DR SwissPalm; P84244; -.
DR EPD; P84244; -.
DR jPOST; P84244; -.
DR MaxQB; P84244; -.
DR PaxDb; P84244; -.
DR PeptideAtlas; P84244; -.
DR PRIDE; P84244; -.
DR Antibodypedia; 54014; 609 antibodies from 19 providers.
DR Antibodypedia; 79211; 181 antibodies from 2 providers.
DR DNASU; 15078; -.
DR DNASU; 15081; -.
DR Ensembl; ENSMUST00000016703; ENSMUSP00000016703; ENSMUSG00000016559.
DR Ensembl; ENSMUST00000106454; ENSMUSP00000102062; ENSMUSG00000016559.
DR Ensembl; ENSMUST00000161308; ENSMUSP00000124509; ENSMUSG00000060743.
DR Ensembl; ENSMUST00000162814; ENSMUSP00000125104; ENSMUSG00000060743.
DR GeneID; 15078; -.
DR GeneID; 15081; -.
DR KEGG; mmu:15078; -.
DR KEGG; mmu:15081; -.
DR UCSC; uc007dwr.1; mouse.
DR CTD; 15078; -.
DR CTD; 15081; -.
DR MGI; MGI:1097686; H3f3a.
DR MGI; MGI:1101768; H3f3b.
DR VEuPathDB; HostDB:ENSMUSG00000016559; -.
DR VEuPathDB; HostDB:ENSMUSG00000060743; -.
DR eggNOG; KOG1745; Eukaryota.
DR GeneTree; ENSGT01050000244918; -.
DR HOGENOM; CLU_078295_4_0_1; -.
DR InParanoid; P84244; -.
DR OMA; SDCERRK; -.
DR OrthoDB; 1564596at2759; -.
DR PhylomeDB; P84244; -.
DR TreeFam; TF314241; -.
DR Reactome; R-MMU-212300; PRC2 methylates histones and DNA.
DR Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-MMU-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-MMU-427359; SIRT1 negatively regulates rRNA expression.
DR Reactome; R-MMU-427413; NoRC negatively regulates rRNA expression.
DR Reactome; R-MMU-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-MMU-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-MMU-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR Reactome; R-MMU-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-MMU-73728; RNA Polymerase I Promoter Opening.
DR Reactome; R-MMU-73772; RNA Polymerase I Promoter Escape.
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; 15078; 5 hits in 43 CRISPR screens.
DR BioGRID-ORCS; 15081; 7 hits in 73 CRISPR screens.
DR ChiTaRS; H3f3a; mouse.
DR ChiTaRS; H3f3b; mouse.
DR PRO; PR:P84244; -.
DR Proteomes; UP000000589; Chromosome 1.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P84244; protein.
DR Bgee; ENSMUSG00000016559; Expressed in vestibular epithelium and 265 other tissues.
DR ExpressionAtlas; P84244; baseline and differential.
DR Genevisible; P84244; MM.
DR GO; GO:0001740; C:Barr body; IDA:MGI.
DR GO; GO:0000785; C:chromatin; IDA:MGI.
DR GO; GO:0005694; C:chromosome; IDA:MGI.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:MGI.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:MGI.
DR GO; GO:0000939; C:inner kinetochore; IDA:MGI.
DR GO; GO:0000228; C:nuclear chromosome; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0000786; C:nucleosome; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0031492; F:nucleosomal DNA binding; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0008283; P:cell population proliferation; IGI:MGI.
DR GO; GO:0006336; P:DNA replication-independent chromatin assembly; ISO:MGI.
DR GO; GO:0007566; P:embryo implantation; IMP:MGI.
DR GO; GO:0008584; P:male gonad development; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0042692; P:muscle cell differentiation; IGI:MGI.
DR GO; GO:1902340; P:negative regulation of chromosome condensation; IGI:MGI.
DR GO; GO:0006334; P:nucleosome assembly; ISO:MGI.
DR GO; GO:0006997; P:nucleus organization; IMP:MGI.
DR GO; GO:0001556; P:oocyte maturation; IDA:MGI.
DR GO; GO:0048477; P:oogenesis; IGI:MGI.
DR GO; GO:0001649; P:osteoblast differentiation; IGI:MGI.
DR GO; GO:0031508; P:pericentric heterochromatin assembly; IGI:MGI.
DR GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI.
DR GO; GO:0090230; P:regulation of centromere complex assembly; IMP:MGI.
DR GO; GO:0007338; P:single fertilization; IMP:MGI.
DR GO; GO:0007286; P:spermatid development; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IGI:MGI.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR000164; Histone_H3/CENP-A.
DR PANTHER; PTHR11426; PTHR11426; 1.
DR Pfam; PF00125; Histone; 1.
DR PRINTS; PR00622; HISTONEH3.
DR SMART; SM00428; H3; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00322; HISTONE_H3_1; 1.
DR PROSITE; PS00959; HISTONE_H3_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ADP-ribosylation; Chromosome; Citrullination;
KW DNA-binding; Hydroxylation; Methylation; Nucleosome core; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..136
FT /note="Histone H3.3"
FT /id="PRO_0000221251"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 32
FT /note="Interaction with ZMYND11"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 3
FT /note="Asymmetric dimethylarginine; by PRMT6; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 3
FT /note="Citrulline; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
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:P84243"
FT MOD_RES 5
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17194708"
FT MOD_RES 5
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="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:17194708"
FT MOD_RES 6
FT /note="5-glutamyl dopamine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
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:P84243"
FT MOD_RES 9
FT /note="Citrulline; alternate"
FT /evidence="ECO:0000305|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:P84243"
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"
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:P84243"
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:P84243"
FT MOD_RES 18
FT /note="Asymmetric dimethylarginine; by CARM1; alternate"
FT /evidence="ECO:0000269|PubMed:11751582,
FT ECO:0000269|PubMed:12498683, 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:P84243"
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:P84243"
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:0000250|UniProtKB:P84243"
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:P84243"
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 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 37
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
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:P84243"
FT MOD_RES 57
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
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:P84243"
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:P84243"
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:P84243"
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:P84243"
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:P84243"
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:P84243"
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:P84243"
FT MOD_RES 80
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
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:P84243"
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:P84243"
FT MOD_RES 116
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
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:P84243"
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:P84243"
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:P84243"
FT MUTAGEN 6
FT /note="Q->A: Abolished serotonylation by TGM2. Reduced
FT neurite length."
FT /evidence="ECO:0000269|PubMed:30867594"
FT CONFLICT 75
FT /note="I -> T (in Ref. 5; AAH21768)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="A -> E (in Ref. 4; BAE31789/BAE30411)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="R -> C (in Ref. 3; X91866)"
FT /evidence="ECO:0000305"
FT HELIX 46..55
FT /evidence="ECO:0007829|PDB:5XM0"
FT HELIX 65..77
FT /evidence="ECO:0007829|PDB:5XM0"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:5XM0"
FT HELIX 87..114
FT /evidence="ECO:0007829|PDB:5XM0"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:5XM0"
FT HELIX 122..131
FT /evidence="ECO:0007829|PDB:5XM0"
SQ SEQUENCE 136 AA; 15328 MW; 5158ED279E6F9E1C CRC64;
MARTKQTARK STGGKAPRKQ LATKAARKSA PSTGGVKKPH RYRPGTVALR EIRRYQKSTE
LLIRKLPFQR LVREIAQDFK TDLRFQSAAI GALQEASEAY LVGLFEDTNL CAIHAKRVTI
MPKDIQLARR IRGERA
