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Histone H3.1

 H31_MOUSE               Reviewed;         136 AA.
P68433; P02295; P02296; P16106; Q05A97; Q3B7Z8; Q3B7Z9; Q5T009;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
22-NOV-2017, entry version 145.
RecName: Full=Histone H3.1;
Name=Hist1h3a; Synonyms=H3a;
and
Name=Hist1h3g; Synonyms=H3.1-221, H3g;
and
Name=Hist1h3h; Synonyms=H3.1-291, H3h;
and
Name=Hist1h3i; Synonyms=H3.1-I, H3i;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6314253; DOI=10.1093/nar/11.19.6679;
Sittman D.B., Graves R.A., Marzluff W.F.;
"Structure of a cluster of mouse histone genes.";
Nucleic Acids Res. 11:6679-6697(1983).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3G AND HIST1H3H).
PubMed=3027355; DOI=10.1007/BF02115580;
Taylor J.D., Wellman S.E., Marzluff W.F.;
"Sequences of four mouse histone H3 genes: implications for evolution
of mouse histone genes.";
J. Mol. Evol. 23:242-249(1986).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=CD-1; TISSUE=Testis;
PubMed=2587222; DOI=10.1093/nar/17.21.8861;
Kosciessa U., Doenecke D.;
"Nucleotide sequences of mouse histone genes H2A and H3.1.";
Nucleic Acids Res. 17:8861-8861(1989).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3I).
STRAIN=C57BL/CJ6;
PubMed=8858344; DOI=10.1101/gr.6.8.688;
Wang Z.-F., Krasikov T., Frey M.R., Wang J., Matera A.G.,
Marzluff W.F.;
"Characterization of the mouse histone gene cluster on chromosome 13:
45 histone genes in three patches spread over 1Mb.";
Genome Res. 6:688-701(1996).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3A; HIST1H3G; HIST1H3H AND
HIST1H3I).
PubMed=12408966; DOI=10.1006/geno.2002.6850;
Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.;
"The human and mouse replication-dependent histone genes.";
Genomics 80:487-498(2002).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/Sv;
Franke K., Drabent B., Doenecke D.;
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
PROTEIN SEQUENCE OF 58-64, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=OF1; TISSUE=Hippocampus;
Lubec G., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[11]
DEVELOPMENTAL STAGE.
PubMed=3018484; DOI=10.1128/MCB.5.11.2879;
Brown D.T., Wellman S.E., Sittman D.B.;
"Changes in the levels of three different classes of histone mRNA
during murine erythroleukemia cell differentiation.";
Mol. Cell. Biol. 5:2879-2886(1985).
[12]
PHOSPHORYLATION AT SER-11 AND SER-29.
PubMed=10464286; DOI=10.1074/jbc.274.36.25543;
Goto H., Tomono Y., Ajiro K., Kosako H., Fujita M., Sakurai M.,
Okawa K., Iwamatsu A., Okigaki T., Takahashi T., Inagaki M.;
"Identification of a novel phosphorylation site on histone H3 coupled
with mitotic chromosome condensation.";
J. Biol. Chem. 274:25543-25549(1999).
[13]
METHYLATION AT LYS-5 AND ARG-18.
PubMed=11747826; DOI=10.1016/S0960-9822(01)00600-5;
Ma H., Baumann C.T., Li H., Strahl B.D., Rice R., Jelinek M.A.,
Aswad D.W., Allis C.D., Hager G.L., Stallcup M.R.;
"Hormone-dependent, CARM1-directed, arginine-specific methylation of
histone H3 on a steroid-regulated promoter.";
Curr. Biol. 11:1981-1985(2001).
[14]
PHOSPHORYLATION AT SER-29.
PubMed=11441012; DOI=10.1074/jbc.M103973200;
Zhong S., Jansen C., She Q.-B., Goto H., Inagaki M., Bode A.M.,
Ma W.-Y., Dong Z.;
"Ultraviolet B-induced phosphorylation of histone H3 at serine 28 is
mediated by MSK1.";
J. Biol. Chem. 276:33213-33219(2001).
[15]
ACETYLATION AT LYS-15; LYS-19 AND LYS-24, AND METHYLATION AT ARG-18.
PubMed=12498683; DOI=10.1016/S0960-9822(02)01387-8;
Daujat S., Bauer U.-M., Shah V., Turner B., Berger S., Kouzarides T.;
"Crosstalk between CARM1 methylation and CBP acetylation on histone
H3.";
Curr. Biol. 12:2090-2097(2002).
[16]
METHYLATION AT ARG-18.
PubMed=11751582; DOI=10.1093/embo-reports/kvf013;
Bauer U.-M., Daujat S., Nielsen S.J., Nightingale K., Kouzarides T.;
"Methylation at arginine 17 of histone H3 is linked to gene
activation.";
EMBO Rep. 3:39-44(2002).
[17]
PHOSPHORYLATION AT SER-11 AND SER-29.
PubMed=11856369; DOI=10.1046/j.1356-9597.2001.00498.x;
Goto H., Yasui Y., Nigg E.A., Inagaki M.;
"Aurora-B phosphorylates Histone H3 at serine28 with regard to the
mitotic chromosome condensation.";
Genes Cells 7:11-17(2002).
[18]
ACETYLATION AT LYS-15; LYS-19 AND LYS-24, METHYLATION AT LYS-10;
LYS-28; LYS-37; LYS-80 AND LYS-123, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=13678296; DOI=10.1023/A:1025334006014;
Cocklin R.R., Wang M.;
"Identification of methylation and acetylation sites on mouse histone
H3 using matrix-assisted laser desorption/ionization time-of-flight
and nanoelectrospray ionization tandem mass spectrometry.";
J. Protein Chem. 22:327-334(2003).
[19]
CITRULLINATION AT ARG-3; ARG-9; ARG-18 AND ARG-27.
PubMed=15339660; DOI=10.1016/j.cell.2004.08.020;
Cuthbert G.L., Daujat S., Snowden A.W., Erdjument-Bromage H.,
Hagiwara T., Yamada M., Schneider R., Gregory P.D., Tempst P.,
Bannister A.J., Kouzarides T.;
"Histone deimination antagonizes arginine methylation.";
Cell 118:545-553(2004).
[20]
METHYLATION AT ARG-9, AND ACETYLATION AT LYS-10.
PubMed=15485929; DOI=10.1128/MCB.24.21.9630-9645.2004;
Pal S., Vishwanath S.N., Erdjument-Bromage H., Tempst P., Sif S.;
"Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and
negatively regulates expression of ST7 and NM23 tumor suppressor
genes.";
Mol. Cell. Biol. 24:9630-9645(2004).
[21]
METHYLATION AT ARG-18.
PubMed=15616592; DOI=10.1038/sj.emboj.7600500;
Covic M., Hassa P.O., Saccani S., Buerki C., Meier N.I., Lombardi C.,
Imhof R., Bedford M.T., Natoli G., Hottiger M.O.;
"Arginine methyltransferase CARM1 is a promoter-specific regulator of
NF-kappaB-dependent gene expression.";
EMBO J. 24:85-96(2005).
[22]
PHOSPHORYLATION AT THR-4 AND SER-11.
PubMed=15681610; DOI=10.1101/gad.1267105;
Dai J., Sultan S., Taylor S.S., Higgins J.M.G.;
"The kinase haspin is required for mitotic histone H3 Thr 3
phosphorylation and normal metaphase chromosome alignment.";
Genes Dev. 19:472-488(2005).
[23]
PHOSPHORYLATION AT SER-29.
PubMed=15684425; DOI=10.1074/jbc.M410521200;
Choi H.S., Choi B.Y., Cho Y.-Y., Zhu F., Bode A.M., Dong Z.;
"Phosphorylation of Ser28 in histone H3 mediated by mixed lineage
kinase-like mitogen-activated protein triple kinase alpha.";
J. Biol. Chem. 280:13545-13553(2005).
[24]
PHOSPHORYLATION AT SER-11 AND SER-29.
PubMed=15870105; DOI=10.1242/jcs.02373;
Dyson M.H., Thomson S., Inagaki M., Goto H., Arthur S.J.,
Nightingale K., Iborra F.J., Mahadevan L.C.;
"MAP kinase-mediated phosphorylation of distinct pools of histone H3
at S10 or S28 via mitogen- and stress-activated kinase 1/2.";
J. Cell Sci. 118:2247-2259(2005).
[25]
PHOSPHORYLATION AT SER-11 AND SER-29.
PubMed=15735677; DOI=10.1038/sj.onc.1208521;
Dunn K.L., Davie J.R.;
"Stimulation of the Ras-MAPK pathway leads to independent
phosphorylation of histone H3 on serine 10 and 28.";
Oncogene 24:3492-3502(2005).
[26]
ACETYLATION AT LYS-5; LYS-10; LYS-15; LYS-19; LYS-24 AND LYS-28,
METHYLATION AT LYS-5; LYS-10; LYS-19; LYS-24; LYS-28; LYS-37 AND
LYS-80, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17194708; DOI=10.1074/jbc.M607900200;
Garcia B.A., Hake S.B., Diaz R.L., Kauer M., Morris S.A., Recht J.,
Shabanowitz J., Mishra N., Strahl B.D., Allis C.D., Hunt D.F.;
"Organismal differences in post-translational modifications in
histones H3 and H4.";
J. Biol. Chem. 282:7641-7655(2007).
[27]
ACETYLATION AT LYS-37.
PubMed=17189264; DOI=10.1074/jbc.M607909200;
Morris S.A., Rao B., Garcia B.A., Hake S.B., Diaz R.L.,
Shabanowitz J., Hunt D.F., Allis C.D., Lieb J.D., Strahl B.D.;
"Identification of histone H3 lysine 36 acetylation as a highly
conserved histone modification.";
J. Biol. Chem. 282:7632-7640(2007).
[28]
PHOSPHORYLATION AT THR-12 BY CHEK1.
PubMed=18243098; DOI=10.1016/j.cell.2007.12.013;
Shimada M., Niida H., Zineldeen D.H., Tagami H., Tanaka M., Saito H.,
Nakanishi M.;
"Chk1 is a histone H3 threonine 11 kinase that regulates DNA damage-
induced transcriptional repression.";
Cell 132:221-232(2008).
[29]
UBIQUITINATION.
PubMed=20122409; DOI=10.1016/j.molcel.2009.12.035;
Grazini U., Zanardi F., Citterio E., Casola S., Goding C.R.,
McBlane F.;
"The RING domain of RAG1 ubiquitylates histone H3: a novel activity in
chromatin-mediated regulation of V(D)J joining.";
Mol. Cell 37:282-293(2010).
[30]
CROTONYLATION AT LYS-5; LYS-10; LYS-19; LYS-24; LYS-28 AND LYS-57.
PubMed=21925322; DOI=10.1016/j.cell.2011.08.008;
Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T.,
Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q.,
Wysocka J., Ye Y., Khochbin S., Ren B., Zhao Y.;
"Identification of 67 histone marks and histone lysine crotonylation
as a new type of histone modification.";
Cell 146:1016-1028(2011).
[31]
SUCCINYLATION AT LYS-57 AND LYS-80.
PubMed=22389435; DOI=10.1074/mcp.M111.015875;
Xie Z., Dai J., Dai L., Tan M., Cheng Z., Wu Y., Boeke J.D., Zhao Y.;
"Lysine succinylation and lysine malonylation in histones.";
Mol. Cell. Proteomics 11:100-107(2012).
[32]
BUTYRYLATION AT LYS-19; LYS-24; LYS-28; LYS-37; LYS-38; LYS-80 AND
LYS-123.
PubMed=27105113; DOI=10.1016/j.molcel.2016.03.014;
Goudarzi A., Zhang D., Huang H., Barral S., Kwon O.K., Qi S., Tang Z.,
Buchou T., Vitte A.L., He T., Cheng Z., Montellier E., Gaucher J.,
Curtet S., Debernardi A., Charbonnier G., Puthier D., Petosa C.,
Panne D., Rousseaux S., Roeder R.G., Zhao Y., Khochbin S.;
"Dynamic competing histone H4 K5K8 acetylation and butyrylation are
hallmarks of highly active gene promoters.";
Mol. Cell 62:169-180(2016).
[33]
HYDROXYBUTYRYLATION AT LYS-5; LYS-10; LYS-15; LYS-19; LYS-24 AND
LYS-57.
PubMed=27105115; DOI=10.1016/j.molcel.2016.03.036;
Xie Z., Zhang D., Chung D., Tang Z., Huang H., Dai L., Qi S., Li J.,
Colak G., Chen Y., Xia C., Peng C., Ruan H., Kirkey M., Wang D.,
Jensen L.M., Kwon O.K., Lee S., Pletcher S.D., Tan M., Lombard D.B.,
White K.P., Zhao H., Li J., Roeder R.G., Yang X., Zhao Y.;
"Metabolic regulation of gene expression by histone lysine beta-
hydroxybutyrylation.";
Mol. Cell 62:194-206(2016).
[34]
HYDROXYBUTYRYLATION AT LYS-5; LYS-10; LYS-15; LYS-19; LYS-24; LYS-28;
LYS-37; LYS-57; LYS-65; LYS-80 AND LYS-123.
PubMed=24681537; DOI=10.1038/nchembio.1497;
Dai L., Peng C., Montellier E., Lu Z., Chen Y., Ishii H.,
Debernardi A., Buchou T., Rousseaux S., Jin F., Sabari B.R., Deng Z.,
Allis C.D., Ren B., Khochbin S., Zhao Y.;
"Lysine 2-hydroxyisobutyrylation is a widely distributed active
histone mark.";
Nat. Chem. Biol. 10:365-370(2014).
-!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and
compact DNA into chromatin, limiting DNA accessibility to the
cellular machineries which require DNA as a template. Histones
thereby play a central role in transcription regulation, DNA
repair, DNA replication and chromosomal stability. DNA
accessibility is regulated via a complex set of post-translational
modifications of histones, also called histone code, and
nucleosome remodeling.
-!- SUBUNIT: The nucleosome is a histone octamer containing two
molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4
heterotetramer and two H2A-H2B heterodimers. The octamer wraps
approximately 147 bp of DNA.
-!- INTERACTION:
P83917:Cbx1; NbExp=6; IntAct=EBI-79743, EBI-78119;
Q8WTS6:SETD7 (xeno); NbExp=2; IntAct=EBI-79743, EBI-1268586;
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
-!- DEVELOPMENTAL STAGE: Expressed during S phase, then expression
strongly decreases as cell division slows down during the process
of differentiation. {ECO:0000269|PubMed:3018484}.
-!- PTM: Acetylation is generally linked to gene activation.
Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9
(H3R8me2s). Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac)
favors methylation at Arg-18 (H3R17me). Acetylation at Lys-123
(H3K122ac) by EP300/p300 plays a central role in chromatin
structure: localizes at the surface of the histone octamer and
stimulates transcription, possibly by promoting nucleosome
instability. {ECO:0000269|PubMed:11747826,
ECO:0000269|PubMed:11751582, ECO:0000269|PubMed:12498683,
ECO:0000269|PubMed:13678296, ECO:0000269|PubMed:15485929,
ECO:0000269|PubMed:15616592, ECO:0000269|PubMed:17194708}.
-!- PTM: Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by
PADI4 impairs methylation and represses transcription.
{ECO:0000269|PubMed:11747826, ECO:0000269|PubMed:11751582,
ECO:0000269|PubMed:12498683, ECO:0000269|PubMed:15339660,
ECO:0000269|PubMed:15485929, ECO:0000269|PubMed:15616592}.
-!- PTM: Asymmetric dimethylation at Arg-18 (H3R17me2a) by CARM1 is
linked to gene activation. Symmetric dimethylation at Arg-9
(H3R8me2s) by PRMT5 is linked to gene repression. Asymmetric
dimethylation at Arg-3 (H3R2me2a) by PRMT6 is linked to gene
repression and is mutually exclusive with H3 Lys-5 methylation
(H3K4me2 and H3K4me3). H3R2me2a is present at the 3' of genes
regardless of their transcription state and is enriched on
inactive promoters, while it is absent on active promoters (By
similarity). {ECO:0000250|UniProtKB:P68431}.
-!- PTM: Methylation at Lys-5 (H3K4me), Lys-37 (H3K36me) and Lys-80
(H3K79me) are linked to gene activation. Methylation at Lys-5
(H3K4me) facilitates subsequent acetylation of H3 and H4.
Methylation at Lys-80 (H3K79me) is associated with DNA double-
strand break (DSB) responses and is a specific target for TP53BP1.
Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are linked to
gene repression. Methylation at Lys-10 (H3K9me) is a specific
target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents
subsequent phosphorylation at Ser-11 (H3S10ph) and acetylation of
H3 and H4. Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me)
require preliminary monoubiquitination of H2B at 'Lys-120'.
Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched
in inactive X chromosome chromatin. Monomethylation at Lys-57
(H3K56me1) by EHMT2/G9A in G1 phase promotes interaction with PCNA
and is required for DNA replication. {ECO:0000269|PubMed:10464286,
ECO:0000269|PubMed:11747826, ECO:0000269|PubMed:11856369,
ECO:0000269|PubMed:13678296, ECO:0000269|PubMed:15485929,
ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:15735677,
ECO:0000269|PubMed:15870105, ECO:0000269|PubMed:17189264,
ECO:0000269|PubMed:17194708}.
-!- PTM: Phosphorylated at Thr-4 (H3T3ph) by HASPIN during prophase
and dephosphorylated during anaphase. Phosphorylation at Ser-11
(H3S10ph) by AURKB is crucial for chromosome condensation and
cell-cycle progression during mitosis and meiosis. In addition
phosphorylation at Ser-11 (H3S10ph) by RPS6KA4 and RPS6KA5 is
important during interphase because it enables the transcription
of genes following external stimulation, like mitogens, stress,
growth factors or UV irradiation and result in the activation of
genes, such as c-fos and c-jun. Phosphorylation at Ser-11
(H3S10ph), which is linked to gene activation, prevents
methylation at Lys-10 (H3K9me) but facilitates acetylation of H3
and H4. Phosphorylation at Ser-11 (H3S10ph) by AURKB mediates the
dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from
heterochromatin. Phosphorylation at Ser-11 (H3S10ph) is also an
essential regulatory mechanism for neoplastic cell transformation.
Phosphorylated at Ser-29 (H3S28ph) by MAP3K20 isoform 1, RPS6KA5
or AURKB during mitosis or upon ultraviolet B irradiation.
Phosphorylation at Thr-7 (H3T6ph) by PRKCB is a specific tag for
epigenetic transcriptional activation that prevents demethylation
of Lys-5 (H3K4me) by LSD1/KDM1A. At centromeres, specifically
phosphorylated at Thr-12 (H3T11ph) from prophase to early
anaphase, by DAPK3 and PKN1. Phosphorylation at Thr-12 (H3T11ph)
by PKN1 is a specific tag for epigenetic transcriptional
activation that promotes demethylation of Lys-10 (H3K9me) by
KDM4C/JMJD2C. Phosphorylation at Thr-12 (H3T11ph) by chromatin-
associated CHEK1 regulates the transcription of cell cycle
regulatory genes by modulating acetylation of Lys-10 (H3K9ac).
Phosphorylation at Tyr-42 (H3Y41ph) by JAK2 promotes exclusion of
CBX5 (HP1 alpha) from chromatin. {ECO:0000269|PubMed:10464286,
ECO:0000269|PubMed:11441012, ECO:0000269|PubMed:11747826,
ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:13678296,
ECO:0000269|PubMed:15485929, ECO:0000269|PubMed:15681610,
ECO:0000269|PubMed:15684425, ECO:0000269|PubMed:15735677,
ECO:0000269|PubMed:15870105, ECO:0000269|PubMed:17194708,
ECO:0000269|PubMed:18243098}.
-!- PTM: Ubiquitinated by the CUL4-DDB-RBX1 complex in response to
ultraviolet irradiation. This may weaken the interaction between
histones and DNA and facilitate DNA accessibility to repair
proteins (By similarity). Monoubiquitinated by RAG1 in lymphoid
cells, monoubiquitination is required for V(D)J recombination.
{ECO:0000250, ECO:0000269|PubMed:20122409}.
-!- PTM: Lysine deamination at Lys-5 (H3K4all) to form allysine is
mediated by LOXL2. Allysine formation by LOXL2 only takes place on
H3K4me3 and results in gene repression (By similarity).
{ECO:0000250|UniProtKB:P68431}.
-!- PTM: Crotonylation (Kcr) is specifically present in male germ
cells and marks testis-specific genes in post-meiotic cells,
including X-linked genes that escape sex chromosome inactivation
in haploid cells. Crotonylation marks active promoters and
enhancers and confers resistance to transcriptional repressors. It
is also associated with post-meiotically activated genes on
autosomes. {ECO:0000269|PubMed:21925322}.
-!- PTM: Butyrylation of histones marks active promoters and competes
with histone acetylation. It is present during late
spermatogenesis. {ECO:0000269|PubMed:27105113}.
-!- PTM: Hydroxybutyrylation of histones is induced by starvation. It
is linked to gene activation and may replace histone acetylation
on the promoter of specific genes in response to fasting.
{ECO:0000269|PubMed:27105115}.
-!- MISCELLANEOUS: This histone is only present in mammals.
-!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X01684; CAA25839.1; -; Genomic_DNA.
EMBL; M32460; AAA37811.1; -; Genomic_DNA.
EMBL; M32462; AAA37813.1; -; Genomic_DNA.
EMBL; X16496; CAA34512.1; -; Genomic_DNA.
EMBL; U62670; AAB04763.1; -; Genomic_DNA.
EMBL; U62672; AAB04765.1; -; Genomic_DNA.
EMBL; AY158944; AAO06254.1; -; Genomic_DNA.
EMBL; AY158945; AAO06255.1; -; Genomic_DNA.
EMBL; AY158946; AAO06256.1; -; Genomic_DNA.
EMBL; AY158952; AAO06262.1; -; Genomic_DNA.
EMBL; Y12290; CAA72968.1; -; Genomic_DNA.
EMBL; AK006742; BAB24722.1; -; mRNA.
EMBL; AK018952; BAB31493.1; -; mRNA.
EMBL; AK155722; BAE33402.1; -; mRNA.
EMBL; AL590388; CAI25837.1; -; Genomic_DNA.
EMBL; AL589651; CAI24113.1; -; Genomic_DNA.
EMBL; AL589651; CAI24105.1; -; Genomic_DNA.
EMBL; BC107285; AAI07286.1; -; mRNA.
EMBL; BC107287; AAI07288.1; -; mRNA.
EMBL; BC115816; AAI15817.1; -; mRNA.
EMBL; BC116383; AAI16384.1; -; mRNA.
EMBL; BC125355; AAI25356.1; -; mRNA.
EMBL; BC125357; AAI25358.1; -; mRNA.
CCDS; CCDS26289.1; -.
CCDS; CCDS26296.1; -.
CCDS; CCDS26342.1; -.
CCDS; CCDS26368.1; -.
PIR; A39525; A39525.
PIR; S06755; S06755.
RefSeq; NP_038578.2; NM_013550.5.
RefSeq; NP_659539.1; NM_145073.2.
RefSeq; NP_835513.1; NM_178206.2.
RefSeq; NP_835514.1; NM_178207.2.
UniGene; Mm.221301; -.
UniGene; Mm.261657; -.
UniGene; Mm.377874; -.
UniGene; Mm.390558; -.
UniGene; Mm.397328; -.
PDB; 1GUW; NMR; -; B=2-17.
PDB; 1U35; X-ray; 3.00 A; A/E=1-136.
PDB; 2V83; X-ray; 2.40 A; D/E=2-10.
PDB; 2W5Z; X-ray; 2.20 A; C=2-9.
PDB; 2WP1; X-ray; 2.10 A; P/Q=15-24.
PDB; 2XL3; X-ray; 2.70 A; D/F=2-9.
PDB; 4EZH; X-ray; 2.52 A; C/D=25-35.
PDB; 5B1L; X-ray; 2.35 A; A/E=1-136.
PDB; 5B1M; X-ray; 2.34 A; A/E=1-136.
PDB; 5IX1; X-ray; 2.60 A; P/Q=2-16.
PDB; 5IX2; X-ray; 2.90 A; P/Q=2-33.
PDBsum; 1GUW; -.
PDBsum; 1U35; -.
PDBsum; 2V83; -.
PDBsum; 2W5Z; -.
PDBsum; 2WP1; -.
PDBsum; 2XL3; -.
PDBsum; 4EZH; -.
PDBsum; 5B1L; -.
PDBsum; 5B1M; -.
PDBsum; 5IX1; -.
PDBsum; 5IX2; -.
ProteinModelPortal; P68433; -.
SMR; P68433; -.
BioGrid; 237523; 1.
IntAct; P68433; 26.
MINT; MINT-191105; -.
STRING; 10090.ENSMUSP00000097295; -.
iPTMnet; P68433; -.
PhosphoSitePlus; P68433; -.
EPD; P68433; -.
MaxQB; P68433; -.
PaxDb; P68433; -.
PRIDE; P68433; -.
TopDownProteomics; P68433; -.
Ensembl; ENSMUST00000080859; ENSMUSP00000079670; ENSMUSG00000099517.
Ensembl; ENSMUST00000091701; ENSMUSP00000089293; ENSMUSG00000069265.
Ensembl; ENSMUST00000188775; ENSMUSP00000140394; ENSMUSG00000101355.
Ensembl; ENSMUST00000189457; ENSMUSP00000139663; ENSMUSG00000101972.
GeneID; 319152; -.
GeneID; 319153; -.
GeneID; 360198; -.
GeneID; 97908; -.
KEGG; mmu:319152; -.
KEGG; mmu:319153; -.
KEGG; mmu:360198; -.
KEGG; mmu:97908; -.
UCSC; uc007prc.1; mouse.
CTD; 8350; -.
CTD; 8354; -.
CTD; 8355; -.
CTD; 8357; -.
MGI; MGI:2668828; Hist1h3a.
MGI; MGI:2145541; Hist1h3g.
MGI; MGI:2448349; Hist1h3h.
MGI; MGI:2448350; Hist1h3i.
eggNOG; KOG1745; Eukaryota.
eggNOG; COG2036; LUCA.
GeneTree; ENSGT00760000118967; -.
HOVERGEN; HBG001172; -.
InParanoid; P68433; -.
KO; K11253; -.
OMA; RPYRGGV; -.
OrthoDB; EOG091G0XGD; -.
PhylomeDB; P68433; -.
TreeFam; TF314241; -.
Reactome; R-MMU-1221633; Meiotic Synapsis.
Reactome; R-MMU-1266695; Interleukin-7 signaling.
Reactome; R-MMU-212300; PRC2 methylates histones and DNA.
Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
Reactome; R-MMU-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
Reactome; R-MMU-3214842; HDMs demethylate histones.
Reactome; R-MMU-3214847; HATs acetylate histones.
Reactome; R-MMU-3214858; RMTs methylate histone arginines.
Reactome; R-MMU-3247509; Chromatin modifying enzymes.
Reactome; R-MMU-427359; SIRT1 negatively regulates rRNA expression.
Reactome; R-MMU-427413; NoRC negatively regulates rRNA expression.
Reactome; R-MMU-5250924; B-WICH complex positively regulates rRNA expression.
Reactome; R-MMU-5578749; Transcriptional regulation by small RNAs.
Reactome; R-MMU-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
Reactome; R-MMU-573389; NoRC negatively regulates rRNA expression.
Reactome; R-MMU-73728; RNA Polymerase I Promoter Opening.
Reactome; R-MMU-73777; RNA Polymerase I Chain Elongation.
Reactome; R-MMU-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
Reactome; R-MMU-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
Reactome; R-MMU-912497; Meiotic Recombination.
Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
EvolutionaryTrace; P68433; -.
PRO; PR:P68433; -.
Proteomes; UP000000589; Chromosome 13.
Bgee; ENSMUSG00000069265; -.
CleanEx; MM_HIST1H3A; -.
CleanEx; MM_HIST1H3G; -.
CleanEx; MM_HIST1H3H; -.
CleanEx; MM_HIST1H3I; -.
Genevisible; P68433; MM.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0000228; C:nuclear chromosome; ISO:MGI.
GO; GO:0000784; C:nuclear chromosome, telomeric region; ISO:MGI.
GO; GO:0000788; C:nuclear nucleosome; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0000786; C:nucleosome; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0043234; C:protein complex; ISO:MGI.
GO; GO:0045296; F:cadherin binding; ISO:MGI.
GO; GO:0042393; F:histone binding; ISO:MGI.
GO; GO:0031492; F:nucleosomal DNA binding; IBA:GO_Central.
GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
GO; GO:0000183; P:chromatin silencing at rDNA; TAS:Reactome.
GO; GO:0032776; P:DNA methylation on cytosine; TAS:Reactome.
GO; GO:0006335; P:DNA replication-dependent nucleosome assembly; ISO:MGI.
GO; GO:0006334; P:nucleosome assembly; ISO:MGI.
GO; GO:0045815; P:positive regulation of gene expression, epigenetic; TAS:Reactome.
GO; GO:0051290; P:protein heterotetramerization; ISO:MGI.
GO; GO:0060968; P:regulation of gene silencing; ISO:MGI.
InterPro; IPR009072; Histone-fold.
InterPro; IPR007125; Histone_H2A/H2B/H3.
InterPro; IPR000164; Histone_H3/CENP-A.
PANTHER; PTHR11426; PTHR11426; 1.
Pfam; PF00125; Histone; 1.
PRINTS; PR00622; HISTONEH3.
SMART; SM00428; H3; 1.
SUPFAM; SSF47113; SSF47113; 1.
PROSITE; PS00322; HISTONE_H3_1; 1.
PROSITE; PS00959; HISTONE_H3_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ADP-ribosylation; Chromosome;
Citrullination; Complete proteome; Direct protein sequencing;
DNA-binding; Hydroxylation; Methylation; Nucleosome core; Nucleus;
Phosphoprotein; Reference proteome; Ubl conjugation.
CHAIN 1 136 Histone H3.1.
/FTId=PRO_0000221249.
MOD_RES 3 3 Asymmetric dimethylarginine; by PRMT6;
alternate.
{ECO:0000250|UniProtKB:P68431}.
MOD_RES 3 3 Citrulline; alternate.
{ECO:0000269|PubMed:15339660}.
MOD_RES 3 3 Phosphoarginine; alternate.
{ECO:0000305}.
MOD_RES 4 4 Phosphothreonine; by HASPIN.
{ECO:0000269|PubMed:15681610}.
MOD_RES 5 5 Allysine; alternate.
{ECO:0000250|UniProtKB:P68431}.
MOD_RES 5 5 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000269|PubMed:11747826,
ECO:0000269|PubMed:17194708}.
MOD_RES 5 5 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:11747826,
ECO:0000269|PubMed:17194708}.
MOD_RES 5 5 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 5 5 N6-(beta-hydroxybutyryl)lysine;
alternate. {ECO:0000269|PubMed:27105115}.
MOD_RES 5 5 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:17194708}.
MOD_RES 5 5 N6-crotonyllysine; alternate.
{ECO:0000269|PubMed:21925322}.
MOD_RES 5 5 N6-methyllysine; alternate.
{ECO:0000269|PubMed:11747826,
ECO:0000269|PubMed:17194708}.
MOD_RES 7 7 Phosphothreonine; by PKC.
{ECO:0000250|UniProtKB:P68431}.
MOD_RES 9 9 Citrulline; alternate.
{ECO:0000269|PubMed:15339660}.
MOD_RES 9 9 Symmetric dimethylarginine; by PRMT5;
alternate. {ECO:0000269|PubMed:15485929}.
MOD_RES 10 10 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000269|PubMed:13678296,
ECO:0000269|PubMed:17194708}.
MOD_RES 10 10 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:13678296,
ECO:0000269|PubMed:17194708}.
MOD_RES 10 10 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 10 10 N6-(beta-hydroxybutyryl)lysine;
alternate. {ECO:0000269|PubMed:27105115}.
MOD_RES 10 10 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:15485929,
ECO:0000269|PubMed:17194708}.
MOD_RES 10 10 N6-crotonyllysine; alternate.
{ECO:0000269|PubMed:21925322}.
MOD_RES 10 10 N6-methyllysine; alternate.
{ECO:0000269|PubMed:13678296,
ECO:0000269|PubMed:17194708}.
MOD_RES 11 11 ADP-ribosylserine; alternate.
{ECO:0000250|UniProtKB:P68431}.
MOD_RES 11 11 Phosphoserine; alternate; by AURKB,
AURKC, RPS6KA3, RPS6KA4 and RPS6KA5.
{ECO:0000269|PubMed:10464286,
ECO:0000269|PubMed:11856369,
ECO:0000269|PubMed:15681610,
ECO:0000269|PubMed:15735677,
ECO:0000269|PubMed:15870105}.
MOD_RES 12 12 Phosphothreonine; by PKC and CHEK1.
{ECO:0000250|UniProtKB:P68431}.
MOD_RES 15 15 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 15 15 N6-(beta-hydroxybutyryl)lysine;
alternate. {ECO:0000269|PubMed:27105115}.
MOD_RES 15 15 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:12498683,
ECO:0000269|PubMed:13678296,
ECO:0000269|PubMed:17194708}.
MOD_RES 18 18 Asymmetric dimethylarginine; by CARM1;
alternate. {ECO:0000269|PubMed:11747826,
ECO:0000269|PubMed:11751582,
ECO:0000269|PubMed:12498683,
ECO:0000269|PubMed:15616592}.
MOD_RES 18 18 Citrulline; alternate.
{ECO:0000269|PubMed:15339660}.
MOD_RES 19 19 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 19 19 N6-(beta-hydroxybutyryl)lysine;
alternate. {ECO:0000269|PubMed:27105115}.
MOD_RES 19 19 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:12498683,
ECO:0000269|PubMed:13678296,
ECO:0000269|PubMed:17194708}.
MOD_RES 19 19 N6-butyryllysine; alternate.
{ECO:0000269|PubMed:27105113}.
MOD_RES 19 19 N6-crotonyllysine; alternate.
{ECO:0000269|PubMed:21925322}.
MOD_RES 19 19 N6-methyllysine; alternate.
{ECO:0000269|PubMed:17194708}.
MOD_RES 24 24 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 24 24 N6-(beta-hydroxybutyryl)lysine;
alternate. {ECO:0000269|PubMed:27105115}.
MOD_RES 24 24 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:12498683,
ECO:0000269|PubMed:13678296,
ECO:0000269|PubMed:17194708}.
MOD_RES 24 24 N6-butyryllysine; alternate.
{ECO:0000269|PubMed:27105113}.
MOD_RES 24 24 N6-crotonyllysine; alternate.
{ECO:0000269|PubMed:21925322}.
MOD_RES 24 24 N6-methyllysine; alternate.
{ECO:0000269|PubMed:17194708}.
MOD_RES 27 27 Citrulline.
{ECO:0000269|PubMed:15339660}.
MOD_RES 28 28 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000269|PubMed:13678296,
ECO:0000269|PubMed:17194708}.
MOD_RES 28 28 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:13678296,
ECO:0000269|PubMed:17194708}.
MOD_RES 28 28 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 28 28 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:17194708}.
MOD_RES 28 28 N6-butyryllysine; alternate.
{ECO:0000269|PubMed:27105113}.
MOD_RES 28 28 N6-crotonyllysine; alternate.
{ECO:0000269|PubMed:21925322}.
MOD_RES 28 28 N6-methyllysine; alternate.
{ECO:0000269|PubMed:13678296,
ECO:0000269|PubMed:17194708}.
MOD_RES 29 29 ADP-ribosylserine; alternate.
{ECO:0000250|UniProtKB:P68431}.
MOD_RES 29 29 Phosphoserine; alternate; by AURKB, AURKC
and RPS6KA5.
{ECO:0000269|PubMed:10464286,
ECO:0000269|PubMed:11441012,
ECO:0000269|PubMed:11856369,
ECO:0000269|PubMed:15684425,
ECO:0000269|PubMed:15735677,
ECO:0000269|PubMed:15870105}.
MOD_RES 37 37 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000305|PubMed:13678296,
ECO:0000305|PubMed:17194708}.
MOD_RES 37 37 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:13678296,
ECO:0000269|PubMed:17194708}.
MOD_RES 37 37 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 37 37 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:17189264}.
MOD_RES 37 37 N6-butyryllysine; alternate.
{ECO:0000269|PubMed:27105113}.
MOD_RES 37 37 N6-methyllysine; alternate.
{ECO:0000269|PubMed:13678296,
ECO:0000269|PubMed:17194708}.
MOD_RES 38 38 N6-butyryllysine; alternate.
{ECO:0000269|PubMed:27105113}.
MOD_RES 42 42 Phosphotyrosine.
{ECO:0000250|UniProtKB:P68431}.
MOD_RES 57 57 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000250|UniProtKB:P68431}.
MOD_RES 57 57 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 57 57 N6-(beta-hydroxybutyryl)lysine;
alternate. {ECO:0000269|PubMed:27105115}.
MOD_RES 57 57 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P68431}.
MOD_RES 57 57 N6-crotonyllysine; alternate.
{ECO:0000269|PubMed:21925322}.
MOD_RES 57 57 N6-methyllysine; by EHMT2; alternate.
{ECO:0000250|UniProtKB:P68431}.
MOD_RES 57 57 N6-succinyllysine; alternate.
{ECO:0000269|PubMed:22389435}.
MOD_RES 58 58 Phosphoserine.
{ECO:0000250|UniProtKB:P68431}.
MOD_RES 65 65 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 65 65 N6-methyllysine.
{ECO:0000250|UniProtKB:P68431}.
MOD_RES 80 80 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000269|PubMed:13678296,
ECO:0000269|PubMed:17194708}.
MOD_RES 80 80 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:13678296,
ECO:0000269|PubMed:17194708}.
MOD_RES 80 80 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 80 80 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P68431}.
MOD_RES 80 80 N6-butyryllysine; alternate.
{ECO:0000269|PubMed:27105113}.
MOD_RES 80 80 N6-methyllysine; alternate.
{ECO:0000269|PubMed:13678296,
ECO:0000269|PubMed:17194708}.
MOD_RES 80 80 N6-succinyllysine; alternate.
{ECO:0000269|PubMed:22389435}.
MOD_RES 81 81 Phosphothreonine.
{ECO:0000250|UniProtKB:P68431}.
MOD_RES 87 87 Phosphoserine.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 108 108 Phosphothreonine.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 116 116 N6-acetyllysine.
{ECO:0000250|UniProtKB:P68431}.
MOD_RES 123 123 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 123 123 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P68431}.
MOD_RES 123 123 N6-butyryllysine; alternate.
{ECO:0000269|PubMed:27105113}.
MOD_RES 123 123 N6-methyllysine; alternate.
{ECO:0000269|PubMed:13678296}.
MOD_RES 129 129 Phosphoarginine. {ECO:0000305}.
MOD_RES 130 130 Phosphoarginine. {ECO:0000305}.
MOD_RES 132 132 Phosphoarginine. {ECO:0000255}.
STRAND 4 7 {ECO:0000244|PDB:5IX1}.
HELIX 46 57 {ECO:0000244|PDB:5B1M}.
HELIX 65 77 {ECO:0000244|PDB:5B1M}.
STRAND 80 82 {ECO:0000244|PDB:5B1M}.
HELIX 87 114 {ECO:0000244|PDB:5B1M}.
STRAND 118 120 {ECO:0000244|PDB:5B1M}.
HELIX 122 131 {ECO:0000244|PDB:5B1M}.
SEQUENCE 136 AA; 15404 MW; 9B89008EA50A0EF6 CRC64;
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE
LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEACEAY LVGLFEDTNL CAIHAKRVTI
MPKDIQLARR IRGERA


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27-131 POLE3 is a histone-fold protein that interacts with other histone-fold proteins to bind DNA in a sequence-independent manner. These histone-fold protein dimers combine within larger enzymatic complexe 0.05 mg
27-775 POLE3 is a histone-fold protein that interacts with other histone-fold proteins to bind DNA in a sequence-independent manner. These histone-fold protein dimers combine within larger enzymatic complexe 0.1 mg
25-113 CHRAC1 is a histone-fold protein that interacts with other histone-fold proteins to bind DNA in a sequence-independent manner. These histone-fold protein dimers combine within larger enzymatic complex 0.05 mg
bs-0931P Peptides: Histone H1b(Histone H1.4) Protein Length:12-25 amino acids. 200ug lyophilized
SET3001 Histone-related : SET7_9 Histone methyltransferase Human, E.coli 0.5mg
SET3001 Histone-related : SET7_9 Histone methyltransferase Human, E.coli 100ug
E0356h ELISA H2B_s,H2BFS,Histone H2B type F-S,Histone H2B.s,Homo sapiens,Human 96T
E0356h ELISA kit H2B_s,H2BFS,Histone H2B type F-S,Histone H2B.s,Homo sapiens,Human 96T
U0356h CLIA H2B_s,H2BFS,Histone H2B type F-S,Histone H2B.s,Homo sapiens,Human 96T
303-35199 Anti_phospho Histone H3 (P_Ser10), monoclonal antibody Binds to Histone H3 phosphorylated at serine 10. 100 ul
30-333 DOT1L is a histone methyltransferase. It methylates 'Lys-79' of histone H3. Nucleosomes are preferred as substrate compared to free histones. 0.05 mg
ANTY021260 Polyclonal Antibodies: Histone H2A.X (Ab-139) ; Specificity: Histone H2A.X (Ab-139) ; Application: IHC 100ug
31-007 Histone H3, along with histone H4, plays a central role in nucleosome formation. 0.1 mg
ANTY021137 Polyclonal Antibodies: Histone H3.1 (Ab-10) ; Specificity: Histone H3.1 (Ab-10) ; Application: IHC 100ug
3623BP-50 Histone H3 Blocking Peptide target: Histone H3 50 μg
3624BP-50 Histone H4 Blocking Peptide target: Histone H4 50 μg
3621BP-50 Histone H2A Blocking Peptide target: Histone H2A 50 μg
3622BP-50 Histone H2B Blocking Peptide target: Histone H2B 50 μg


 

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