ID   H3_CAEEL                Reviewed;         136 AA.
AC   P08898; Q9TW44;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   27-MAR-2024, entry version 190.
DE   RecName: Full=Histone H3;
GN   Name=his-2; ORFNames=T10C6.13;
GN   and
GN   Name=his-6; ORFNames=F45F2.13;
GN   and
GN   Name=his-9; ORFNames=ZK131.3;
GN   and
GN   Name=his-13; ORFNames=ZK131.7;
GN   and
GN   Name=his-17; ORFNames=K06C4.5;
GN   and
GN   Name=his-25; ORFNames=ZK131.2;
GN   and
GN   Name=his-27; ORFNames=K06C4.13;
GN   and
GN   Name=his-32; ORFNames=F17E9.10;
GN   and
GN   Name=his-42; ORFNames=F08G2.3;
GN   and
GN   Name=his-45; ORFNames=B0035.10;
GN   and
GN   Name=his-49; ORFNames=F07B7.5;
GN   and
GN   Name=his-55; ORFNames=F54E12.1;
GN   and
GN   Name=his-59; ORFNames=F55G1.2;
GN   and
GN   Name=his-63; ORFNames=F22B3.2;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIS-10).
RC   STRAIN=Bristol N2;
RX   PubMed=2544730; DOI=10.1016/0022-2836(89)90566-4;
RA   Roberts S.B., Emmons S.W., Childs G.;
RT   "Nucleotide sequences of Caenorhabditis elegans core histone genes. Genes
RT   for different histone classes share common flanking sequence elements.";
RL   J. Mol. Biol. 206:567-577(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (HIS-4).
RC   STRAIN=Bristol N2;
RA   Kohara Y., Shin-i T., Suzuki Y., Sugano S., Potdevin M., Thierry-Mieg Y.,
RA   Thierry-Mieg D., Thierry-Mieg J.;
RT   "The Caenorhabditis elegans transcriptome project, a complementary view of
RT   the genome.";
RL   Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PROTEIN SEQUENCE OF 2-136, ACETYLATION AT LYS-5; LYS-15 AND LYS-24, AND
RP   METHYLATION AT LYS-10; LYS-28; LYS-37 AND LYS-80.
RC   STRAIN=DR27;
RX   PubMed=3803587; DOI=10.1016/0014-5793(87)81274-7;
RA   Vanfleteren J.R., van Bun S.M., van Beeumen J.J.;
RT   "The primary structure of histone H3 from the nematode Caenorhabditis
RT   elegans.";
RL   FEBS Lett. 211:59-63(1987).
RN   [5]
RP   PHOSPHORYLATION AT SER-11.
RX   PubMed=10975519; DOI=10.1016/s0092-8674(00)00034-9;
RA   Hsu J.-Y., Sun Z.-W., Li X., Reuben M., Tatchell K., Bishop D.K.,
RA   Grushcow J.M., Brame C.J., Caldwell J.A., Hunt D.F., Lin R., Smith M.M.,
RA   Allis C.D.;
RT   "Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase
RT   and Glc7/PP1 phosphatase in budding yeast and nematodes.";
RL   Cell 102:279-291(2000).
RN   [6]
RP   PHOSPHORYLATION AT SER-11 AND SER-29.
RX   PubMed=12015116; DOI=10.1016/s0960-9822(02)00820-5;
RA   Kaitna S., Pasierbek P., Jantsch M., Loidl J., Glotzer M.;
RT   "The aurora B kinase AIR-2 regulates kinetochores during mitosis and is
RT   required for separation of homologous Chromosomes during meiosis.";
RL   Curr. Biol. 12:798-812(2002).
RN   [7]
RP   METHYLATION AT LYS-5 AND LYS-10, PHOSPHORYLATION AT SER-11, AND ACETYLATION
RP   AT LYS-10 AND LYS-15.
RX   PubMed=11807039; DOI=10.1242/dev.129.2.479;
RA   Kelly W.G., Schaner C.E., Dernburg A.F., Lee M.-H., Kim S.K.,
RA   Villeneuve A.M., Reinke V.;
RT   "X-chromosome silencing in the germline of C. elegans.";
RL   Development 129:479-492(2002).
RN   [8]
RP   METHYLATION AT LYS-5 AND LYS-10.
RX   PubMed=11969256; DOI=10.1006/dbio.2002.0634;
RA   Reuben M., Lin R.;
RT   "Germline X chromosomes exhibit contrasting patterns of histone H3
RT   methylation in Caenorhabditis elegans.";
RL   Dev. Biol. 245:71-82(2002).
RN   [9]
RP   PHOSPHORYLATION AT SER-11, AND METHYLATION AT LYS-5; LYS-10 AND LYS-37.
RX   PubMed=14614817; DOI=10.1016/j.cub.2003.10.035;
RA   Han Z., Saam J.R., Adams H.P., Mango S.E., Schumacher J.M.;
RT   "The C. elegans Tousled-like kinase (TLK-1) has an essential role in
RT   transcription.";
RL   Curr. Biol. 13:1921-1929(2003).
RN   [10]
RP   PHOSPHORYLATION AT SER-11.
RX   PubMed=12837290; DOI=10.1016/s0014-4827(03)00157-5;
RA   Sassa T., Ueda-Ohba H., Kitamura K., Harada S., Hosono R.;
RT   "Role of Caenorhabditis elegans protein phosphatase type 1, CeGLC-7 beta,
RT   in metaphase to anaphase transition during embryonic development.";
RL   Exp. Cell Res. 287:350-360(2003).
RN   [11]
RP   PHOSPHORYLATION AT SER-11 AND SER-29.
RX   PubMed=14622138; DOI=10.1046/j.1365-2443.2003.00682.x;
RA   Sasagawa Y., Urano T., Kohara Y., Takahashi H., Higashitani A.;
RT   "Caenorhabditis elegans RBX1 is essential for meiosis, mitotic chromosomal
RT   condensation and segregation, and cytokinesis.";
RL   Genes Cells 8:857-872(2003).
RN   [12]
RP   METHYLATION AT LYS-28.
RX   PubMed=15380065; DOI=10.1016/j.cub.2004.08.062;
RA   Bender L.B., Cao R., Zhang Y., Strome S.;
RT   "The MES-2/MES-3/MES-6 complex and regulation of histone H3 methylation in
RT   C. elegans.";
RL   Curr. Biol. 14:1639-1643(2004).
RN   [13]
RP   ACETYLATION AT LYS-10 AND LYS-15, METHYLATION AT LYS-5 AND LYS-10, AND
RP   PHOSPHORYLATION AT SER-11.
RX   PubMed=14702046; DOI=10.1038/ng1283;
RA   Bean C.J., Schaner C.E., Kelly W.G.;
RT   "Meiotic pairing and imprinted X chromatin assembly in Caenorhabditis
RT   elegans.";
RL   Nat. Genet. 36:100-105(2004).
RN   [14]
RP   METHYLATION AT LYS-10 AND LYS-37.
RX   PubMed=16603238; DOI=10.1016/j.cell.2006.03.028;
RA   Whetstine J.R., Nottke A., Lan F., Huarte M., Smolikov S., Chen Z.,
RA   Spooner E., Li E., Zhang G., Colaiacovo M., Shi Y.;
RT   "Reversal of histone lysine trimethylation by the JMJD2 family of histone
RT   demethylases.";
RL   Cell 125:467-481(2006).
RN   [15] {ECO:0007744|PDB:7LHY}
RP   X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 8-21 IN COMPLEX WITH THE BROMO
RP   DOMAIN OF SWSN-4, AND INTERACTION WITH SWSN-4.
RX   PubMed=34473995; DOI=10.1016/j.jbc.2021.101145;
RA   Enriquez P., Krajewski K., Strahl B.D., Rothbart S.B., Dowen R.H.,
RA   Rose R.B.;
RT   "Binding specificity and function of the SWI/SNF subunit SMARCA4
RT   bromodomain interaction with acetylated histone H3K14.";
RL   J. Biol. Chem. 297:101145-101145(2021).
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 (via N-terminal tail mono-acetylated on Lys-15) with
CC       swsn-4 (via Bromo domain); the interaction is direct (PubMed:34473995).
CC       {ECO:0000269|PubMed:34473995}.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC   -!- PTM: Phosphorylated at Ser-11 and Ser-29 during M phase.
CC       Phosphorylation of Ser-11 requires air-2 but not air-1.
CC       Dephosphorylated by gsp-1 and/or gsp-2 during chromosome segregation.
CC       {ECO:0000269|PubMed:10975519, ECO:0000269|PubMed:11807039,
CC       ECO:0000269|PubMed:12015116, ECO:0000269|PubMed:12837290,
CC       ECO:0000269|PubMed:14614817, ECO:0000269|PubMed:14622138,
CC       ECO:0000269|PubMed:14702046}.
CC   -!- PTM: Acetylation is generally linked to gene activation. {ECO:0000250}.
CC   -!- PTM: Methylation at Lys-5 is linked to gene activation and is absent
CC       from male inactive X chromosome chromatin. Methylation at Lys-10 is
CC       linked to gene repression and is enriched in male inactive X chromosome
CC       chromatin. Methylation at Lys-37 occurs on the entire length of
CC       autosomes during meiotic prophase. Trimethylation at Lys-10 and Lys-37
CC       is specifically antagonized by jmjd-2. Dimethylation and trimethylation
CC       at Lys-28 occurs in all nuclei. The mes-2-mes-3-mes-6 complex may be
CC       responsible for Lys-28 methylation in most of the germline and in the
CC       early embryo. {ECO:0000269|PubMed:11807039,
CC       ECO:0000269|PubMed:11969256, ECO:0000269|PubMed:14614817,
CC       ECO:0000269|PubMed:14702046, ECO:0000269|PubMed:15380065,
CC       ECO:0000269|PubMed:16603238, ECO:0000269|PubMed:3803587}.
CC   -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
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DR   EMBL; X15634; CAA33644.1; -; Genomic_DNA.
DR   EMBL; FO081018; CCD68531.1; -; Genomic_DNA.
DR   EMBL; FO081059; CCD68868.1; -; Genomic_DNA.
DR   EMBL; FO081135; CCD69390.1; -; Genomic_DNA.
DR   EMBL; FO081223; CCD70027.1; -; Genomic_DNA.
DR   EMBL; FO081551; CCD72363.1; -; Genomic_DNA.
DR   EMBL; FO081551; CCD72373.1; -; Genomic_DNA.
DR   EMBL; Z68336; CAA92733.1; -; Genomic_DNA.
DR   EMBL; Z73102; CAA97411.1; -; Genomic_DNA.
DR   EMBL; Z81495; CAB04057.1; -; Genomic_DNA.
DR   EMBL; Z82271; CAB05209.1; -; Genomic_DNA.
DR   EMBL; Z83245; CAB05831.1; -; Genomic_DNA.
DR   EMBL; Z83245; CAB05833.1; -; Genomic_DNA.
DR   EMBL; Z83245; CAB05834.1; -; Genomic_DNA.
DR   EMBL; Z93388; CAB07653.1; -; Genomic_DNA.
DR   EMBL; AF304122; AAG50235.1; -; mRNA.
DR   PIR; S04241; HSKW3.
DR   RefSeq; NP_001263958.1; NM_001277029.1.
DR   RefSeq; NP_496890.1; NM_064489.1.
DR   RefSeq; NP_496894.1; NM_064493.5.
DR   RefSeq; NP_496895.1; NM_064494.1.
DR   RefSeq; NP_496899.1; NM_064498.1.
DR   RefSeq; NP_501204.1; NM_068803.3.
DR   RefSeq; NP_501407.1; NM_069006.3.
DR   RefSeq; NP_502134.1; NM_069733.3.
DR   RefSeq; NP_502138.1; NM_069737.1.
DR   RefSeq; NP_502153.1; NM_069752.3.
DR   RefSeq; NP_505199.1; NM_072798.1.
DR   RefSeq; NP_505276.1; NM_072875.1.
DR   RefSeq; NP_505292.1; NM_072891.1.
DR   RefSeq; NP_505297.1; NM_072896.3.
DR   RefSeq; NP_507033.1; NM_074632.3.
DR   PDB; 3N9L; X-ray; 2.80 A; B=2-16.
DR   PDB; 3N9N; X-ray; 2.30 A; B/C=2-33.
DR   PDB; 3N9O; X-ray; 2.31 A; B=2-16, C=2-18.
DR   PDB; 3N9P; X-ray; 2.39 A; B/C=2-33.
DR   PDB; 3N9Q; X-ray; 2.30 A; B=2-16, C=20-36.
DR   PDB; 7LHY; X-ray; 1.30 A; B=8-21.
DR   PDBsum; 3N9L; -.
DR   PDBsum; 3N9N; -.
DR   PDBsum; 3N9O; -.
DR   PDBsum; 3N9P; -.
DR   PDBsum; 3N9Q; -.
DR   PDBsum; 7LHY; -.
DR   AlphaFoldDB; P08898; -.
DR   BMRB; P08898; -.
DR   SMR; P08898; -.
DR   BioGRID; 42741; 1.
DR   BioGRID; 45065; 4.
DR   BioGRID; 46690; 1.
DR   BioGRID; 49588; 1.
DR   BioGRID; 50996; 1.
DR   BioGRID; 56173; 1.
DR   IntAct; P08898; 1.
DR   STRING; 6239.B0035.10.1; -.
DR   iPTMnet; P08898; -.
DR   PaxDb; 6239-B0035-10; -.
DR   PeptideAtlas; P08898; -.
DR   EnsemblMetazoa; B0035.10.1; B0035.10.1; WBGene00001919.
DR   EnsemblMetazoa; F07B7.5.1; F07B7.5.1; WBGene00001923.
DR   EnsemblMetazoa; F08G2.3.1; F08G2.3.1; WBGene00001916.
DR   EnsemblMetazoa; F17E9.10.1; F17E9.10.1; WBGene00001906.
DR   EnsemblMetazoa; F22B3.2.1; F22B3.2.1; WBGene00001937.
DR   EnsemblMetazoa; F45F2.13.1; F45F2.13.1; WBGene00001880.
DR   EnsemblMetazoa; F54E12.1.1; F54E12.1.1; WBGene00001929.
DR   EnsemblMetazoa; F55G1.2.1; F55G1.2.1; WBGene00001933.
DR   EnsemblMetazoa; K06C4.13.1; K06C4.13.1; WBGene00001901.
DR   EnsemblMetazoa; K06C4.5.1; K06C4.5.1; WBGene00001891.
DR   EnsemblMetazoa; T10C6.13.1; T10C6.13.1; WBGene00001876.
DR   EnsemblMetazoa; ZK131.2.1; ZK131.2.1; WBGene00001899.
DR   EnsemblMetazoa; ZK131.3.1; ZK131.3.1; WBGene00001883.
DR   EnsemblMetazoa; ZK131.7.1; ZK131.7.1; WBGene00001887.
DR   GeneID; 13221387; -.
DR   GeneID; 175030; -.
DR   GeneID; 175031; -.
DR   GeneID; 177628; -.
DR   GeneID; 180074; -.
DR   GeneID; 181821; -.
DR   GeneID; 184113; -.
DR   GeneID; 184804; -.
DR   GeneID; 186250; -.
DR   GeneID; 186325; -.
DR   GeneID; 191668; -.
DR   GeneID; 191672; -.
DR   GeneID; 191673; -.
DR   GeneID; 246024; -.
DR   KEGG; cel:CELE_B0035.10; -.
DR   KEGG; cel:CELE_F07B7.5; -.
DR   KEGG; cel:CELE_F17E9.10; -.
DR   KEGG; cel:CELE_F22B3.2; -.
DR   KEGG; cel:CELE_F45F2.13; -.
DR   KEGG; cel:CELE_F54E12.1; -.
DR   KEGG; cel:CELE_F55G1.2; -.
DR   KEGG; cel:CELE_K03A1.1; -.
DR   KEGG; cel:CELE_K06C4.13; -.
DR   KEGG; cel:CELE_K06C4.5; -.
DR   KEGG; cel:CELE_T10C6.13; -.
DR   KEGG; cel:CELE_ZK131.2; -.
DR   KEGG; cel:CELE_ZK131.3; -.
DR   KEGG; cel:CELE_ZK131.7; -.
DR   UCSC; ZK131.7; c. elegans.
DR   AGR; WB:WBGene00001876; -.
DR   AGR; WB:WBGene00001880; -.
DR   AGR; WB:WBGene00001883; -.
DR   AGR; WB:WBGene00001887; -.
DR   AGR; WB:WBGene00001891; -.
DR   AGR; WB:WBGene00001899; -.
DR   AGR; WB:WBGene00001901; -.
DR   AGR; WB:WBGene00001906; -.
DR   AGR; WB:WBGene00001916; -.
DR   AGR; WB:WBGene00001919; -.
DR   AGR; WB:WBGene00001923; -.
DR   AGR; WB:WBGene00001929; -.
DR   AGR; WB:WBGene00001933; -.
DR   AGR; WB:WBGene00001937; -.
DR   WormBase; B0035.10; CE03253; WBGene00001919; his-45.
DR   WormBase; F07B7.5; CE03253; WBGene00001923; his-49.
DR   WormBase; F08G2.3; CE03253; WBGene00001916; his-42.
DR   WormBase; F17E9.10; CE03253; WBGene00001906; his-32.
DR   WormBase; F22B3.2; CE03253; WBGene00001937; his-63.
DR   WormBase; F45F2.13; CE03253; WBGene00001880; his-6.
DR   WormBase; F54E12.1; CE03253; WBGene00001929; his-55.
DR   WormBase; F55G1.2; CE03253; WBGene00001933; his-59.
DR   WormBase; K06C4.13; CE03253; WBGene00001901; his-27.
DR   WormBase; K06C4.5; CE03253; WBGene00001891; his-17.
DR   WormBase; T10C6.13; CE03253; WBGene00001876; his-2.
DR   WormBase; ZK131.2; CE03253; WBGene00001899; his-25.
DR   WormBase; ZK131.3; CE03253; WBGene00001883; his-9.
DR   WormBase; ZK131.7; CE03253; WBGene00001887; his-13.
DR   eggNOG; KOG1745; Eukaryota.
DR   GeneTree; ENSGT01100000263514; -.
DR   HOGENOM; CLU_078295_4_0_1; -.
DR   InParanoid; P08898; -.
DR   OrthoDB; 2873654at2759; -.
DR   PhylomeDB; P08898; -.
DR   EvolutionaryTrace; P08898; -.
DR   PRO; PR:P08898; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00001876; Expressed in pharyngeal muscle cell (C elegans) and 4 other cell types or tissues.
DR   GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0035064; F:methylated histone binding; IPI:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
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; Chromosome; Direct protein sequencing;
KW   DNA-binding; Methylation; Nucleosome core; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:3803587"
FT   CHAIN           2..136
FT                   /note="Histone H3"
FT                   /id="PRO_0000221297"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         5
FT                   /note="N6,N6,N6-trimethyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:11807039,
FT                   ECO:0000269|PubMed:11969256, ECO:0000269|PubMed:14614817,
FT                   ECO:0000269|PubMed:14702046"
FT   MOD_RES         5
FT                   /note="N6,N6-dimethyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:11807039,
FT                   ECO:0000269|PubMed:11969256, ECO:0000269|PubMed:14614817,
FT                   ECO:0000269|PubMed:14702046"
FT   MOD_RES         5
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:3803587"
FT   MOD_RES         5
FT                   /note="N6-methyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:11807039,
FT                   ECO:0000269|PubMed:11969256, ECO:0000269|PubMed:14614817,
FT                   ECO:0000269|PubMed:14702046"
FT   MOD_RES         10
FT                   /note="N6,N6,N6-trimethyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:11807039,
FT                   ECO:0000269|PubMed:11969256, ECO:0000269|PubMed:14614817,
FT                   ECO:0000269|PubMed:14702046, ECO:0000269|PubMed:16603238,
FT                   ECO:0000269|PubMed:3803587"
FT   MOD_RES         10
FT                   /note="N6,N6-dimethyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:11807039,
FT                   ECO:0000269|PubMed:11969256, ECO:0000269|PubMed:14614817,
FT                   ECO:0000269|PubMed:14702046, ECO:0000269|PubMed:16603238,
FT                   ECO:0000269|PubMed:3803587"
FT   MOD_RES         10
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:11807039,
FT                   ECO:0000269|PubMed:14702046"
FT   MOD_RES         11
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:10975519,
FT                   ECO:0000269|PubMed:11807039, ECO:0000269|PubMed:12015116,
FT                   ECO:0000269|PubMed:12837290, ECO:0000269|PubMed:14614817,
FT                   ECO:0000269|PubMed:14622138, ECO:0000269|PubMed:14702046"
FT   MOD_RES         15
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:11807039,
FT                   ECO:0000269|PubMed:14702046, ECO:0000269|PubMed:3803587"
FT   MOD_RES         24
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:3803587"
FT   MOD_RES         28
FT                   /note="N6,N6,N6-trimethyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:15380065,
FT                   ECO:0000269|PubMed:3803587"
FT   MOD_RES         28
FT                   /note="N6,N6-dimethyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:15380065,
FT                   ECO:0000269|PubMed:3803587"
FT   MOD_RES         28
FT                   /note="N6-methyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:15380065,
FT                   ECO:0000269|PubMed:3803587"
FT   MOD_RES         29
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:12015116,
FT                   ECO:0000269|PubMed:14622138"
FT   MOD_RES         37
FT                   /note="N6,N6,N6-trimethyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:14614817,
FT                   ECO:0000269|PubMed:16603238, ECO:0000269|PubMed:3803587"
FT   MOD_RES         37
FT                   /note="N6,N6-dimethyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:14614817,
FT                   ECO:0000269|PubMed:16603238, ECO:0000269|PubMed:3803587"
FT   MOD_RES         37
FT                   /note="N6-methyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:14614817,
FT                   ECO:0000269|PubMed:16603238, ECO:0000269|PubMed:3803587"
FT   MOD_RES         80
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000269|PubMed:3803587"
FT   VARIANT         97
FT                   /note="C -> A"
FT   VARIANT         101
FT                   /note="L -> I"
FT   STRAND          4..6
FT                   /evidence="ECO:0007829|PDB:3N9N"
SQ   SEQUENCE   136 AA;  15376 MW;  40D7DE0EF5BA6F1F CRC64;
     MARTKQTARK STGGKAPRKQ LATKAARKSA PASGGVKKPH RYRPGTVALR EIRRYQKSTE
     LLIRRAPFQR LVREIAQDFK TDLRFQSSAV MALQEACEAY LVGLFEDTNL CAIHAKRVTI
     MPKDIQLARR IRGERA
//