ID H32_XENLA Reviewed; 136 AA. AC P84233; A4FVE2; P02295; P02297; P16105; P17269; P17320; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 04-NOV-2026, entry version 156. DE RecName: Full=Histone H3.2; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=4059058; DOI=10.1093/nar/13.20.7341; RA Old R.W., Sheikh S.A., Chambers A., Newton C.A., Mohammed A., RA Aldridge T.C.; RT "Individual Xenopus histone genes are replication-independent in oocytes RT and replication-dependent in Xenopus or mouse somatic cells."; RL Nucleic Acids Res. 13:7341-7358(1985). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (GENE CLUSTERS X1H1 AND X1H3). RX PubMed=3863963; DOI=10.1016/0022-2836(85)90065-8; RA Perry M., Thomsen G.H., Roeder R.G.; RT "Genomic organization and nucleotide sequence of two distinct histone gene RT clusters from Xenopus laevis. Identification of novel conserved upstream RT sequence elements."; RL J. Mol. Biol. 185:479-499(1985). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Embryo; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [4] RP METHYLATION AT LYS-5; LYS-10 AND ARG-18, PHOSPHORYLATION AT SER-11, AND RP ACETYLATION AT LYS-15. RX PubMed=12138181; DOI=10.1128/mcb.22.16.5688-5697.2002; RA Li J., Lin Q., Yoon H.-G., Huang Z.-Q., Strahl B.D., Allis C.D., Wong J.; RT "Involvement of histone methylation and phosphorylation in regulation of RT transcription by thyroid hormone receptor."; RL Mol. Cell. Biol. 22:5688-5697(2002). RN [5] RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH H2A; H2B AND H4. RX PubMed=12079350; DOI=10.1016/s0022-2836(02)00386-8; RA Davey C.A., Sargent D.F., Luger K., Maeder A.W., Richmond T.J.; RT "Solvent mediated interactions in the structure of the nucleosome core RT particle at 1.9 A resolution."; RL J. Mol. Biol. 319:1097-1113(2002). RN [6] {ECO:0007744|PDB:5NL0} RP X-RAY CRYSTALLOGRAPHY OF NUCLEOSOME AND HISTONE H1, FUNCTION, AND SUBUNIT. RX PubMed=28475873; DOI=10.1016/j.molcel.2017.04.012; RA Bednar J., Garcia-Saez I., Boopathi R., Cutter A.R., Papai G., Reymer A., RA Syed S.H., Lone I.N., Tonchev O., Crucifix C., Menoni H., Papin C., RA Skoufias D.A., Kurumizaka H., Lavery R., Hamiche A., Hayes J.J., RA Schultz P., Angelov D., Petosa C., Dimitrov S.; RT "Structure and Dynamics of a 197bp Nucleosome in Complex with Linker RT Histone H1."; RL Mol. Cell 66:384-397(2017). RN [7] {ECO:0007744|PDB:6ZHX, ECO:0007744|PDB:6ZHY} RP STRUCTURE BY ELECTRON MICROSCOPY OF NUCLEOSOME CORE COMPLEX IN COMPLEX WITH RP CHD1L. RX PubMed=33357431; DOI=10.1016/j.celrep.2020.108529; RA Lehmann L.C., Bacic L., Hewitt G., Brackmann K., Sabantsev A., Gaullier G., RA Pytharopoulou S., Degliesposti G., Okkenhaug H., Tan S., Costa A., RA Skehel J.M., Boulton S.J., Deindl S.; RT "Mechanistic insights into regulation of the ALC1 remodeler by the RT nucleosome acidic patch."; RL Cell Rep. 33:108529-108529(2020). RN [8] {ECO:0007744|PDB:7OTQ} RP STRUCTURE BY ELECTRON MICROSCOPY OF NUCLEOSOME CORE COMPLEX IN COMPLEX WITH RP CHD1L. RX PubMed=34486521; DOI=10.7554/elife.71420; RA Bacic L., Gaullier G., Sabantsev A., Lehmann L.C., Brackmann K., RA Dimakou D., Halic M., Hewitt G., Boulton S.J., Deindl S.; RT "Structure and dynamics of the chromatin remodeler ALC1 bound to a RT PARylated nucleosome."; RL Elife 10:0-0(2021). RN [9] {ECO:0007744|PDB:7ENN} RP STRUCTURE BY ELECTRON MICROSCOPY OF NUCLEOSOME CORE COMPLEX IN COMPLEX WITH RP CHD1L. RX PubMed=34210977; DOI=10.1038/s41467-021-24320-4; RA Wang L., Chen K., Chen Z.; RT "Structural basis of ALC1/CHD1L autoinhibition and the mechanism of RT activation by the nucleosome."; RL Nat. Commun. 12:4057-4057(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. {ECO:0000269|PubMed:28475873}. 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. {ECO:0000269|PubMed:12079350, ECO:0000269|PubMed:28475873}. CC -!- INTERACTION: CC P84233; P62799; NbExp=2; IntAct=EBI-350041, EBI-302085; CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. CC -!- DEVELOPMENTAL STAGE: Expressed during S phase, then expression strongly CC decreases as cell division slows down during the process of CC differentiation. CC -!- PTM: Acetylation is generally linked to gene activation. 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 (By similarity). {ECO:0000250|UniProtKB:Q71DI3}. CC -!- PTM: Asymmetric dimethylation at Arg-18 (H3R17me2a) is linked to gene CC activation. Asymmetric dimethylation at Arg-3 (H3R2me2a) by prmt6 is CC linked to gene repression and is mutually exclusive with H3 Lys-5 CC methylation (H3K4me2 and H3K4me3). H3R2me2a is present at the 3' of CC genes regardless of their transcription state and is enriched on CC inactive promoters, while it is absent on active promoters (By CC similarity). {ECO:0000250|UniProtKB:Q71DI3}. CC -!- PTM: Methylation at Lys-5 (H3K4me), Lys-37 (H3K36me) and Lys-80 CC (H3K79me) are linked to gene activation. Methylation at Lys-5 (H3K4me) CC facilitates subsequent acetylation of H3 and H4. Methylation at Lys-80 CC (H3K79me) is associated with DNA double-strand break (DSB) responses CC and is a specific target for tp53bp1. Methylation at Lys-10 (H3K9me) CC and Lys-28 (H3K27me) are linked to gene repression. Methylation at Lys- CC 10 (H3K9me) is a specific target for HP1 proteins (cbx1, cbx3 and cbx5) CC and prevents subsequent phosphorylation at Ser-11 (H3S10ph) and CC acetylation of H3 and H4. Methylation at Lys-5 (H3K4me) and Lys-80 CC (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120' CC (By similarity). {ECO:0000250|UniProtKB:Q71DI3}. CC -!- PTM: Phosphorylated at Thr-4 (H3T3ph) by VRK1 (By similarity). CC 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 (By similarity). CC {ECO:0000250|UniProtKB:Q71DI3}. CC -!- PTM: Monoubiquitinated at Lys-15 (H3K14ub), Lys-19 (H3K18ub) and Lys-24 CC (H3K23ub) by UHRF1 and HLTF at hemimethylated DNA sites following DNA CC replication, promoting recruitment of DNMT1 DNA methyltransferase and CC replication-coupled DNA methylation maintenance (By similarity). CC Monoubiquitinated at Lys-15 (H3K14ub) by G2E3: H3K14ub represents a CC specific tag for heterochromatin formation by facilitating the CC deposition of H3K9me3 (By similarity). Monoubiquitinated by RAG1 in CC lymphoid cells, monoubiquitination is required for V(D)J recombination CC (By similarity). {ECO:0000250|UniProtKB:P68431}. CC -!- PTM: Lysine deamination at Lys-5 (H3K4all) to form allysine only takes CC place on H3K4me3 and results in gene repression. CC {ECO:0000250|UniProtKB:Q71DI3}. CC -!- PTM: Butyrylation of histones marks active promoters and competes with CC histone acetylation. It is present during late spermatogenesis. CC {ECO:0000250|UniProtKB:P68433}. 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:Q71DI3}. CC -!- PTM: Serine ADP-ribosylation by PARP1 or PARP2 constitutes the primary CC form of ADP-ribosylation of proteins in response to DNA damage. Serine CC ADP-ribosylation at Ser-11 (H3S10ADPr) promotes recruitment of CHD1L. CC H3S10ADPr is mutually exclusive with phosphorylation at Ser-11 CC (H3S10ph) and impairs acetylation at Lys-10 (H3K9ac). CC {ECO:0000250|UniProtKB:P68431}. CC -!- PTM: Serotonylated by TGM2 at Gln-6 (H3Q5ser) during serotonergic CC neuron differentiation (By similarity). 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 (By similarity). {ECO:0000250|UniProtKB:Q71DI3}. 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:P84245, ECO:0000250|UniProtKB:Q71DI3}. 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:Q71DI3}. CC -!- PTM: Propionylated at 'Lys-19' (H3K18Pr) by CREBBP. CC {ECO:0000250|UniProtKB:Q71DI3}. CC -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X03104; CAA26890.1; -; Genomic_DNA. DR EMBL; X03017; CAA26813.1; -; Genomic_DNA. DR EMBL; X03018; CAA26818.1; -; Genomic_DNA. DR EMBL; M21286; AAA49765.1; -; Genomic_DNA. DR EMBL; M21287; AAA49770.1; -; Genomic_DNA. DR EMBL; BC133776; AAI33777.1; -; mRNA. DR PIR; A93596; HSXL31. DR PIR; I51448; I51448. DR RefSeq; XP_018079657.1; XM_018224168.2. DR RefSeq; XP_018096296.1; XM_018240807.2. DR RefSeq; XP_018098036.1; XM_018242547.2. DR RefSeq; XP_018118226.1; XM_018262737.2. DR RefSeq; XP_018118227.1; XM_018262738.2. DR RefSeq; XP_041418540.1; XM_041562606.1. DR RefSeq; XP_041420127.1; XM_041564193.1. DR RefSeq; XP_041432548.1; XM_041576614.1. DR RefSeq; XP_041432550.1; XM_041576616.1. DR RefSeq; XP_041434997.1; XM_041579063.1. DR RefSeq; XP_041434998.1; XM_041579064.1. DR RefSeq; XP_041434999.1; XM_041579065.1. DR RefSeq; XP_041444756.1; XM_041588822.1. DR PDB; 1F66; X-ray; 2.60 A; A/E=1-136. DR PDB; 1KX3; X-ray; 2.00 A; A/E=2-136. DR PDB; 1KX4; X-ray; 2.60 A; A/E=2-136. DR PDB; 1KX5; X-ray; 1.94 A; A/E=2-136. DR PDB; 1P34; X-ray; 2.70 A; A/E=2-136. DR PDB; 1P3A; X-ray; 3.00 A; A/E=2-136. DR PDB; 1P3B; X-ray; 3.00 A; A/E=2-136. DR PDB; 1P3F; X-ray; 2.90 A; A/E=2-136. DR PDB; 1P3G; X-ray; 2.70 A; A/E=2-136. DR PDB; 1P3I; X-ray; 2.30 A; A/E=2-136. DR PDB; 1P3K; X-ray; 2.90 A; A/E=2-136. DR PDB; 1P3L; X-ray; 2.40 A; A/E=2-136. DR PDB; 1P3M; X-ray; 2.90 A; A/E=2-136. DR PDB; 1P3O; X-ray; 2.75 A; A/E=2-136. DR PDB; 1P3P; X-ray; 2.70 A; A/E=2-136. DR PDB; 1S32; X-ray; 2.05 A; A/E=2-136. DR PDB; 1ZBB; X-ray; 9.00 A; A/E/a/e=2-136. DR PDB; 1ZLA; X-ray; 2.90 A; A/E=2-136. DR PDB; 2F8N; X-ray; 2.90 A; A/E=1-136. DR PDB; 2FJ7; X-ray; 3.20 A; A/E=2-136. DR PDB; 2HUE; X-ray; 1.70 A; B=62-136. DR PDB; 2IO5; X-ray; 2.70 A; B=2-136. DR PDB; 2L11; NMR; -; B=2-16. DR PDB; 2L12; NMR; -; B=2-16. DR PDB; 2NZD; X-ray; 2.65 A; A/E=2-136. DR PDB; 3B6F; X-ray; 3.45 A; A/E=2-136. DR PDB; 3B6G; X-ray; 3.45 A; A/E=2-136. DR PDB; 3C1B; X-ray; 2.20 A; A/E=2-136. DR PDB; 3C1C; X-ray; 3.15 A; A/E=2-136. DR PDB; 3GV6; X-ray; 1.76 A; B=2-16. DR PDB; 3KUY; X-ray; 2.90 A; A/E=2-136. DR PDB; 3KWQ; X-ray; 3.50 A; A/E=39-136. DR PDB; 3KXB; X-ray; 3.20 A; A/E=2-136. DR PDB; 3LEL; X-ray; 2.95 A; A/E/K/O=1-136. DR PDB; 3LJA; X-ray; 2.75 A; A/E=2-136. DR PDB; 3LZ0; X-ray; 2.50 A; A/E=2-136. DR PDB; 3LZ1; X-ray; 2.50 A; A/E=2-136. DR PDB; 3MGP; X-ray; 2.44 A; A/E=2-136. DR PDB; 3MGQ; X-ray; 2.65 A; A/E=2-136. DR PDB; 3MGR; X-ray; 2.30 A; A/E=2-136. DR PDB; 3MGS; X-ray; 3.15 A; A/E=2-136. DR PDB; 3MNN; X-ray; 2.50 A; A/E=2-136. DR PDB; 3MVD; X-ray; 2.90 A; A/E=2-136. DR PDB; 3O62; X-ray; 3.22 A; A/E=2-136. DR PDB; 3REH; X-ray; 2.50 A; A/E=2-136. DR PDB; 3REI; X-ray; 2.65 A; A/E=2-136. DR PDB; 3REJ; X-ray; 2.55 A; A/E=2-136. DR PDB; 3REK; X-ray; 2.60 A; A/E=2-136. DR PDB; 3REL; X-ray; 2.70 A; A/E=2-136. DR PDB; 3TU4; X-ray; 3.00 A; A/E=2-136. DR PDB; 3UT9; X-ray; 2.20 A; A/E=2-136. DR PDB; 3UTA; X-ray; 2.07 A; A/E=2-136. DR PDB; 3UTB; X-ray; 2.20 A; A/E=2-136. DR PDB; 4EO5; X-ray; 2.35 A; B=62-136. DR PDB; 4J8U; X-ray; 2.38 A; A/E=2-136. DR PDB; 4J8V; X-ray; 2.58 A; A/E=2-136. DR PDB; 4J8W; X-ray; 2.41 A; A/E=2-136. DR PDB; 4J8X; X-ray; 2.87 A; A/E=2-136. DR PDB; 4KGC; X-ray; 2.69 A; A/E=1-136. DR PDB; 4LD9; X-ray; 3.31 A; A/E=1-136. DR PDB; 4QEO; X-ray; 2.00 A; P=2-16. DR PDB; 4R8P; X-ray; 3.28 A; A/E=2-136. DR PDB; 4WU8; X-ray; 2.45 A; A/E=2-136. DR PDB; 4WU9; X-ray; 2.60 A; A/E=2-136. DR PDB; 4XUJ; X-ray; 3.18 A; A/E=2-136. DR PDB; 4XZQ; X-ray; 2.40 A; A/E=39-136. DR PDB; 4YS3; X-ray; 3.00 A; A/E=39-136. DR PDB; 4Z66; X-ray; 2.50 A; A/E=39-136. DR PDB; 4ZUX; X-ray; 3.82 A; A/E/K/O=1-136. DR PDB; 5BS7; X-ray; 3.30 A; A/B=26-136. DR PDB; 5BSA; X-ray; 4.61 A; A/B=27-136. DR PDB; 5CP6; X-ray; 2.60 A; A/E=2-136. DR PDB; 5DNM; X-ray; 2.81 A; A/E=2-136. DR PDB; 5DNN; X-ray; 2.80 A; A/E=2-136. DR PDB; 5E5A; X-ray; 2.81 A; A/E=1-136. DR PDB; 5F99; X-ray; 2.63 A; A/E=2-136. DR PDB; 5HQ2; X-ray; 4.50 A; A=2-136. DR PDB; 5KGF; EM; 4.54 A; A/E=1-136. DR PDB; 5MLU; X-ray; 2.80 A; A/E=40-136. DR PDB; 5NL0; X-ray; 5.40 A; A/E/K=2-136. DR PDB; 5O9G; EM; 4.80 A; A/E=1-136. DR PDB; 5OMX; X-ray; 2.32 A; A/E=2-136. DR PDB; 5ONG; X-ray; 2.80 A; A/E=2-136. DR PDB; 5ONW; X-ray; 2.80 A; A/E=2-136. DR PDB; 5OXV; X-ray; 6.72 A; A/E/K/O=2-136. DR PDB; 5OY7; X-ray; 5.77 A; A/E/I/M/Q/U/Y/c=2-136. DR PDB; 5X0X; EM; 3.97 A; A/E=1-136. DR PDB; 5X0Y; EM; 3.97 A; A/E=2-136. DR PDB; 5XBK; X-ray; 3.22 A; E=2-19. DR PDB; 5XF6; X-ray; 2.63 A; A/E=2-136. DR PDB; 5Z3L; EM; 4.31 A; A/E=2-136. DR PDB; 5Z3O; EM; 3.62 A; A/E=2-136. DR PDB; 5Z3U; EM; 4.31 A; A/E=2-136. DR PDB; 5Z3V; EM; 4.22 A; A/E=2-136. DR PDB; 6ESF; EM; 3.70 A; A/E=2-136. DR PDB; 6ESG; EM; 5.40 A; A/E=2-136. DR PDB; 6ESH; EM; 5.10 A; A/E=2-136. DR PDB; 6ESI; EM; 6.30 A; A/E=2-136. DR PDB; 6FQ5; EM; 3.80 A; A/E=38-135. DR PDB; 6FQ6; EM; 4.00 A; A/E=38-135. DR PDB; 6I84; EM; 4.40 A; M/S=1-136. DR PDB; 6IRO; EM; 3.40 A; A/E=2-136. DR PDB; 6IY2; EM; 3.47 A; A/E=37-136. DR PDB; 6IY3; EM; 3.67 A; A/E=37-136. DR PDB; 6JM9; EM; 7.30 A; A/E=39-136. DR PDB; 6JMA; EM; 6.80 A; A/E=39-136. DR PDB; 6KIU; EM; 3.20 A; A/E=2-136. DR PDB; 6KIV; EM; 4.00 A; A/E=2-136. DR PDB; 6KIW; EM; 4.00 A; A/E=2-136. DR PDB; 6KIX; EM; 4.10 A; A/E=2-136. DR PDB; 6KIZ; EM; 4.50 A; A/E=2-136. DR PDB; 6KW3; EM; 7.13 A; N/Q=1-136. DR PDB; 6KW4; EM; 7.55 A; N/Q=1-136. DR PDB; 6KW5; EM; 10.13 A; R/V=1-136. DR PDB; 6NE3; EM; 3.90 A; A/E=1-136. DR PDB; 6NJ9; EM; 2.96 A; A/E=2-136. DR PDB; 6NN6; EM; 3.90 A; A/E=2-136. DR PDB; 6NOG; EM; 3.90 A; A/E=2-136. DR PDB; 6NQA; EM; 3.54 A; A/E=2-136. DR PDB; 6O22; Other; -; E=1-136. DR PDB; 6O96; EM; 3.50 A; A/E=2-136. DR PDB; 6OM3; X-ray; 3.30 A; A/E/M/Q=2-136. DR PDB; 6PA7; EM; 2.94 A; A/E=2-136. DR PDB; 6PWV; EM; 6.20 A; G/K=1-136. DR PDB; 6PWW; EM; 4.40 A; G/K=1-136. DR PDB; 6PWX; EM; 4.20 A; G/K=1-136. DR PDB; 6R1T; EM; 3.70 A; A/E=38-136. DR PDB; 6R1U; EM; 4.36 A; A/E/M=2-136. DR PDB; 6R25; EM; 4.61 A; A/E/M=2-136. DR PDB; 6RYR; EM; 3.10 A; A/E=1-136. DR PDB; 6RYU; EM; 4.00 A; A/E=1-136. DR PDB; 6S01; EM; 3.20 A; A/E=2-136. DR PDB; 6T9L; EM; 3.60 A; A/E=2-136. DR PDB; 6TDA; EM; 15.00 A; A/E=2-136. DR PDB; 6UH5; EM; 3.50 A; R=2-9. DR PDB; 6UXW; EM; 8.96 A; R/V=2-136. DR PDB; 6VEN; EM; 3.37 A; A/E=2-136. DR PDB; 6VYP; X-ray; 4.99 A; A/E/a/e=2-136. DR PDB; 6W5I; EM; 6.90 A; G/K=1-136. DR PDB; 6W5M; EM; 4.60 A; G/K=1-136. DR PDB; 6W5N; EM; 6.00 A; G/K=1-136. DR PDB; 6WKR; EM; 3.50 A; I/O=1-136. DR PDB; 6WZ5; EM; 2.20 A; A/E=2-136. DR PDB; 6WZ9; EM; 2.80 A; A/E=2-136. DR PDB; 6X0N; EM; 10.00 A; A/E/a/e=2-136. DR PDB; 6Z6P; EM; 4.43 A; E=40-136. DR PDB; 6ZHX; EM; 2.50 A; A/E=1-136. DR PDB; 6ZHY; EM; 3.00 A; A/E=1-136. DR PDB; 7AT8; EM; 4.40 A; D/H=2-136. DR PDB; 7E8I; EM; 3.10 A; A/E=2-136. DR PDB; 7EA5; EM; 3.30 A; A/E=35-135. DR PDB; 7EG6; EM; 3.10 A; A/E=2-136. DR PDB; 7EGP; EM; 6.90 A; O/S=2-136. DR PDB; 7ENN; EM; 2.80 A; A/E=2-136. DR PDB; 7K6P; EM; 3.20 A; A/E=38-135. DR PDB; 7K6Q; EM; 3.10 A; A/E=38-135. DR PDB; 7KBD; EM; 3.38 A; A/E=1-136. DR PDB; 7KBE; EM; 3.50 A; A/E=1-136. DR PDB; 7KBF; EM; 4.42 A; A/E=1-136. DR PDB; 7KTQ; EM; 3.30 A; A/E=38-136. DR PDB; 7MBM; EM; -; G/K=1-136. DR PDB; 7MBN; EM; -; G/K=1-136. DR PDB; 7NKX; EM; 2.90 A; a/e=1-136. DR PDB; 7NKY; EM; 3.20 A; a/e=1-136. DR PDB; 7OH9; EM; 3.00 A; A/E=2-136. DR PDB; 7OHA; EM; 2.90 A; A/E=2-136. DR PDB; 7OHB; EM; 3.40 A; A/E=2-136. DR PDB; 7OHC; EM; 2.50 A; A/E=2-136. DR PDB; 7OTQ; EM; 4.80 A; A/E=1-136. DR PDB; 7SSA; EM; 3.20 A; A/E=2-136. DR PDB; 7SWY; EM; 2.60 A; A/E=2-136. DR PDB; 7TN2; EM; 2.30 A; A/E=2-136. DR PDB; 7UD5; EM; 4.25 A; A/E=1-136. DR PDB; 7UNC; EM; 3.00 A; a/e=1-136. DR PDB; 7UND; EM; 3.00 A; a/e=1-136. DR PDB; 7VDT; EM; 2.80 A; E/K=1-136. DR PDB; 7VDV; EM; 3.40 A; E/K=1-136. DR PDB; 7VVU; EM; 3.40 A; A/O=1-136. DR PDB; 7VVZ; EM; 8.80 A; A/O=1-136. DR PDB; 7X3T; EM; 5.40 A; A/E/K/O=1-136. DR PDB; 7X3V; EM; 3.09 A; A/E=1-136. DR PDB; 7X3W; EM; 3.10 A; A/E=1-136. DR PDB; 7X3X; EM; 3.20 A; A/E=1-136. DR PDB; 7XFC; EM; 2.90 A; A/E=1-136. DR PDB; 7XFH; EM; 2.90 A; A/E=1-136. DR PDB; 7XFI; EM; 2.90 A; A/E=1-136. DR PDB; 7XFJ; EM; 3.00 A; A/E=1-136. DR PDB; 7XFL; EM; 2.80 A; A/E=1-136. DR PDB; 7XFM; EM; 3.10 A; A/E=1-136. DR PDB; 7XFN; EM; 2.80 A; A/E=1-136. DR PDB; 7XNP; EM; 2.90 A; A/E=1-136. DR PDB; 7XPX; EM; 3.20 A; A/E=2-136. DR PDB; 7YI1; EM; 2.80 A; A/E=2-136. DR PDB; 7YI4; EM; 3.96 A; G/K=2-136. DR PDB; 7YI5; EM; 3.96 A; G/K=2-136. DR PDB; 7YRG; EM; 4.20 A; A/E=34-136. DR PDB; 7ZS9; EM; 3.10 A; a/e=2-136. DR PDB; 7ZSA; EM; 4.00 A; a/e=2-136. DR PDB; 7ZSB; EM; 6.60 A; a/e=2-136. DR PDB; 8A3Y; EM; 3.30 A; a/e=1-136. DR PDB; 8B0A; EM; 3.00 A; A/E=1-136. DR PDB; 8BVW; EM; 4.00 A; a/e=1-136. DR PDB; 8BYQ; EM; 4.10 A; a/e=1-136. DR PDB; 8BZ1; EM; 3.80 A; a/e=1-136. DR PDB; 8CBN; EM; 3.34 A; A/E=2-136. DR PDB; 8CBQ; EM; 4.00 A; A/E=2-136. DR PDB; 8CEO; EM; 3.60 A; r/v=2-136. DR PDB; 8CWW; EM; 2.74 A; A/E=2-136. DR PDB; 8CZE; EM; 2.58 A; A/E=2-136. DR PDB; 8ETT; EM; 6.68 A; A/E=1-136. DR PDB; 8ETV; EM; 3.16 A; A/E=1-136. DR PDB; 8EUE; EM; 3.48 A; A/E=1-136. DR PDB; 8EUJ; EM; 3.36 A; M/f=41-136. DR PDB; 8F86; EM; 3.10 A; A/E=2-136. DR PDB; 8G57; EM; 3.07 A; A/E=4-135. DR PDB; 8G6G; EM; 2.93 A; A/E=1-136. DR PDB; 8G6H; EM; 3.06 A; A/E=1-136. DR PDB; 8G6Q; EM; 3.41 A; A/E=1-136. DR PDB; 8G6S; EM; 3.47 A; A/E=1-136. DR PDB; 8G86; EM; 2.30 A; A/E=2-136. DR PDB; 8G88; EM; 4.80 A; A/E=2-136. DR PDB; 8G8B; EM; 4.30 A; A/E=2-136. DR PDB; 8G8G; EM; 3.20 A; A/E=2-136. DR PDB; 8GPN; EM; 3.20 A; A/E=1-136. DR PDB; 8HXX; EM; 3.00 A; E=2-136. DR PDB; 8HXY; EM; 3.10 A; A/E=2-136. DR PDB; 8HXZ; EM; 3.40 A; A/E=2-136. DR PDB; 8HY0; EM; 3.10 A; A/E=2-136. DR PDB; 8IHM; EM; 3.58 A; A/E=2-136. DR PDB; 8IHN; EM; 3.37 A; A=2-25. DR PDB; 8IHT; EM; 3.72 A; A/E=2-136. DR PDB; 8JHO; EM; 7.60 A; A/E/a/e=2-136. DR PDB; 8KD2; EM; 3.02 A; O/S=2-136. DR PDB; 8KD4; EM; 2.93 A; O/S=2-136. DR PDB; 8KD5; EM; 2.90 A; O/S=2-136. DR PDB; 8KD6; EM; 3.07 A; O/S=2-136. DR PDB; 8KD7; EM; 3.09 A; O/S=2-136. DR PDB; 8OF4; EM; 2.94 A; A/E=1-136. DR PDB; 8PC5; EM; 3.02 A; A/E=2-136. DR PDB; 8PC6; EM; 3.04 A; A/E=2-136. DR PDB; 8PEO; EM; 2.69 A; A/E=2-136. DR PDB; 8PEP; EM; 3.33 A; E=2-136. DR PDB; 8RUP; EM; 2.42 A; A=1-136. DR PDB; 8RUQ; EM; 2.29 A; A=2-136. DR PDB; 8SIY; EM; 2.90 A; C/G=2-136. DR PDB; 8SKZ; EM; 3.50 A; B/E=1-136. DR PDB; 8SVF; EM; 3.20 A; A/E=1-136. DR PDB; 8T3T; EM; 3.21 A; A/E=2-136. DR PDB; 8T3W; EM; 3.25 A; A/E=2-136. DR PDB; 8T3Y; EM; 3.47 A; A/E=2-136. DR PDB; 8T9F; EM; 2.60 A; A/E=2-136. DR PDB; 8T9G; EM; 6.20 A; A/W=1-136. DR PDB; 8T9H; EM; 3.37 A; A/E=2-136. DR PDB; 8TAS; EM; 4.10 A; I/W=1-136. DR PDB; 8TB9; EM; 4.00 A; I/W=1-136. DR PDB; 8THU; EM; 3.10 A; A/E=2-136. DR PDB; 8UW1; EM; 2.88 A; A/E=1-136. DR PDB; 8UXQ; EM; 6.30 A; E/K=2-136. DR PDB; 8V25; EM; 3.32 A; A/E=1-136. DR PDB; 8V26; EM; 3.33 A; A/E=1-136. DR PDB; 8V27; EM; 3.34 A; A/E=1-136. DR PDB; 8V28; EM; 3.36 A; A/E=1-136. DR PDB; 8V4Y; EM; 2.80 A; A/E=2-136. DR PDB; 8V6V; EM; 2.80 A; A/E=2-136. DR PDB; 8V7L; EM; 2.90 A; A/E=2-136. DR PDB; 8VX5; EM; 3.30 A; A/E=1-136. DR PDB; 8VX6; EM; 3.20 A; A/E=1-136. DR PDB; 9B2S; EM; 3.01 A; A/E=1-136. DR PDB; 9B2T; EM; 2.99 A; A/E=1-136. DR PDB; 9B2U; EM; 3.64 A; E=1-136. DR PDB; 9CA7; EM; 3.35 A; U/W=2-136. DR PDB; 9CA8; EM; 3.92 A; U/W=2-136. DR PDB; 9CAA; EM; 4.04 A; U/W=2-136. DR PDB; 9CAB; EM; 3.94 A; U/W=2-136. DR PDB; 9CG9; EM; 2.94 A; A/E=2-136. DR PDB; 9DBY; EM; 2.80 A; A/E=1-136. DR PDB; 9DDE; EM; 3.20 A; A/E=1-136. DR PDB; 9DG3; EM; 3.46 A; A/E=1-136. DR PDB; 9DGG; EM; 2.98 A; A/E=1-136. DR PDB; 9E1L; EM; 3.15 A; A/E=1-136. DR PDB; 9E1M; EM; 3.25 A; A/E=1-136. DR PDB; 9E1N; EM; 3.40 A; A/E=1-136. DR PDB; 9E1O; EM; 3.30 A; A/E=1-136. DR PDB; 9E1P; EM; 3.25 A; A/E=1-136. DR PDB; 9E1Q; EM; 3.10 A; A/E=1-136. DR PDB; 9E1R; EM; 3.10 A; A/E=1-136. DR PDB; 9E1U; EM; 3.10 A; A/E=1-136. DR PDB; 9E1V; EM; 3.10 A; A/E=1-136. DR PDB; 9E1W; EM; 3.20 A; A/E=1-136. DR PDB; 9E1X; EM; 3.40 A; A/E=1-136. DR PDB; 9E1Y; EM; 2.60 A; A/E=1-136. DR PDB; 9EIL; EM; 3.20 A; A/E=2-136. DR PDB; 9F0O; EM; 2.30 A; A/E=39-136. DR PDB; 9GD0; EM; 2.80 A; A/E/K/O=1-136. DR PDB; 9GD1; EM; 4.00 A; A/E/K/O=1-136. DR PDB; 9GD2; EM; 4.20 A; A/E/K/O=1-136. DR PDB; 9GD3; EM; 3.00 A; A/E=1-136. DR PDB; 9GEN; EM; 3.76 A; A/E=38-136. DR PDB; 9GEO; EM; 2.79 A; A/E=38-136. DR PDB; 9GEP; EM; 2.89 A; A/E=38-136. DR PDB; 9GEQ; EM; 3.12 A; A/E=38-136. DR PDB; 9GER; EM; 3.58 A; A/E=38-136. DR PDB; 9IHD; EM; 2.97 A; A/E=38-136. DR PDB; 9IHE; EM; 2.95 A; A/E=38-136. DR PDB; 9IHF; EM; 3.16 A; A/E=38-136. DR PDB; 9MPP; EM; 3.10 A; A/E=2-136. DR PDB; 9N6K; EM; 2.90 A; A/E=40-136. DR PDB; 9NH8; EM; 3.20 A; A/E/V=1-136. DR PDB; 9NY4; EM; 2.98 A; A/E=1-136. DR PDB; 9PM0; EM; 2.90 A; C/G=2-136. DR PDB; 9QAJ; EM; 2.95 A; A/E=2-136. DR PDB; 9R5K; EM; 4.20 A; A/E=1-136. DR PDB; 9R5S; EM; 3.80 A; A/E=1-136. DR PDB; 9R5W; EM; 3.80 A; A/E=1-136. DR PDB; 9SI3; EM; 2.83 A; A/E=2-136. DR PDB; 9SI9; EM; 2.86 A; A=2-136. DR PDB; 9SJ5; EM; 2.85 A; A/E=2-136. DR PDB; 9SLJ; EM; 3.80 A; A/E=2-136. DR PDB; 9T4V; EM; 6.60 A; A/E=1-136. DR PDB; 9W74; EM; 4.94 A; A/E/K/O=1-136. DR PDB; 9WBZ; EM; 2.90 A; E/K=2-136. DR PDB; 9WC0; EM; 2.40 A; E/K=2-136. DR PDB; 9XYC; EM; 3.50 A; a/e=1-136. DR PDB; 9Y4P; EM; 3.84 A; E/Q/W=2-136. DR AlphaFoldDB; P84233; -. DR EMDB; EMD-0458; -. DR EMDB; EMD-0468; -. DR EMDB; EMD-0480; -. DR EMDB; EMD-0777; -. DR EMDB; EMD-0778; -. DR EMDB; EMD-0779; -. DR EMDB; EMD-10058; -. DR EMDB; EMD-10059; -. DR EMDB; EMD-10415; -. DR EMDB; EMD-10465; -. DR EMDB; EMD-11102; -. DR EMDB; EMD-11910; -. DR EMDB; EMD-12449; -. DR EMDB; EMD-12450; -. DR EMDB; EMD-12897; -. DR EMDB; EMD-12898; -. DR EMDB; EMD-12899; -. DR EMDB; EMD-12900; -. DR EMDB; EMD-13065; -. DR EMDB; EMD-14927; -. DR EMDB; EMD-14928; -. DR EMDB; EMD-14929; -. DR EMDB; EMD-15127; -. DR EMDB; EMD-16274; -. DR EMDB; EMD-16331; -. DR EMDB; EMD-16335; -. DR EMDB; EMD-16611; -. DR EMDB; EMD-16842; -. DR EMDB; EMD-16845; -. DR EMDB; EMD-17944; -. DR EMDB; EMD-19513; -. DR EMDB; EMD-19514; -. DR EMDB; EMD-20281; -. DR EMDB; EMD-20512; -. DR EMDB; EMD-20513; -. DR EMDB; EMD-20514; -. DR EMDB; EMD-20934; -. DR EMDB; EMD-21157; -. DR EMDB; EMD-21542; -. DR EMDB; EMD-21543; -. DR EMDB; EMD-21544; -. DR EMDB; EMD-21707; -. DR EMDB; EMD-21970; -. DR EMDB; EMD-21971; -. DR EMDB; EMD-21980; -. DR EMDB; EMD-22691; -. DR EMDB; EMD-22692; -. DR EMDB; EMD-22790; -. DR EMDB; EMD-22791; -. DR EMDB; EMD-22792; -. DR EMDB; EMD-25406; -. DR EMDB; EMD-26620; -. DR EMDB; EMD-26621; -. DR EMDB; EMD-27030; -. DR EMDB; EMD-27096; -. DR EMDB; EMD-28915; -. DR EMDB; EMD-29778; -. DR EMDB; EMD-29781; -. DR EMDB; EMD-29837; -. DR EMDB; EMD-29843; -. DR EMDB; EMD-29845; -. DR EMDB; EMD-29850; -. DR EMDB; EMD-31106; -. DR EMDB; EMD-31137; -. DR EMDB; EMD-31217; -. DR EMDB; EMD-33171; -. DR EMDB; EMD-33172; -. DR EMDB; EMD-33173; -. DR EMDB; EMD-33174; -. DR EMDB; EMD-33175; -. DR EMDB; EMD-33176; -. DR EMDB; EMD-33177; -. DR EMDB; EMD-33322; -. DR EMDB; EMD-33385; -. DR EMDB; EMD-34053; -. DR EMDB; EMD-34055; -. DR EMDB; EMD-34195; -. DR EMDB; EMD-3765; -. DR EMDB; EMD-3947; -. DR EMDB; EMD-3948; -. DR EMDB; EMD-3949; -. DR EMDB; EMD-3950; -. DR EMDB; EMD-40522; -. DR EMDB; EMD-40569; -. DR EMDB; EMD-40789; -. DR EMDB; EMD-41011; -. DR EMDB; EMD-41015; -. DR EMDB; EMD-41016; -. DR EMDB; EMD-41109; -. DR EMDB; EMD-41110; -. DR EMDB; EMD-41111; -. DR EMDB; EMD-41113; -. DR EMDB; EMD-41141; -. DR EMDB; EMD-41146; -. DR EMDB; EMD-41272; -. DR EMDB; EMD-41839; -. DR EMDB; EMD-41851; -. DR EMDB; EMD-41852; -. DR EMDB; EMD-41853; -. DR EMDB; EMD-42636; -. DR EMDB; EMD-42774; -. DR EMDB; EMD-42898; -. DR EMDB; EMD-42899; -. DR EMDB; EMD-42900; -. DR EMDB; EMD-42901; -. DR EMDB; EMD-4297; -. DR EMDB; EMD-42977; -. DR EMDB; EMD-4298; -. DR EMDB; EMD-43000; -. DR EMDB; EMD-43001; -. DR EMDB; EMD-43002; -. DR EMDB; EMD-43003; -. DR EMDB; EMD-43004; -. DR EMDB; EMD-43005; -. DR EMDB; EMD-43608; -. DR EMDB; EMD-43609; -. DR EMDB; EMD-44113; -. DR EMDB; EMD-44114; -. DR EMDB; EMD-44115; -. DR EMDB; EMD-4429; -. DR EMDB; EMD-45381; -. DR EMDB; EMD-45382; -. DR EMDB; EMD-45384; -. DR EMDB; EMD-45385; -. DR EMDB; EMD-45578; -. DR EMDB; EMD-46728; -. DR EMDB; EMD-46732; -. DR EMDB; EMD-46733; -. DR EMDB; EMD-46771; -. DR EMDB; EMD-46822; -. DR EMDB; EMD-46823; -. DR EMDB; EMD-4705; -. DR EMDB; EMD-47412; -. DR EMDB; EMD-47413; -. DR EMDB; EMD-47414; -. DR EMDB; EMD-47415; -. DR EMDB; EMD-47416; -. DR EMDB; EMD-47417; -. DR EMDB; EMD-47418; -. DR EMDB; EMD-47421; -. DR EMDB; EMD-47422; -. DR EMDB; EMD-47423; -. DR EMDB; EMD-47424; -. DR EMDB; EMD-47425; -. DR EMDB; EMD-47427; -. DR EMDB; EMD-47428; -. DR EMDB; EMD-48086; -. DR EMDB; EMD-48498; -. DR EMDB; EMD-49063; -. DR EMDB; EMD-49406; -. DR EMDB; EMD-49919; -. DR EMDB; EMD-50114; -. DR EMDB; EMD-51238; -. DR EMDB; EMD-51241; -. DR EMDB; EMD-51244; -. DR EMDB; EMD-51247; -. DR EMDB; EMD-51295; -. DR EMDB; EMD-51296; -. DR EMDB; EMD-51297; -. DR EMDB; EMD-51301; -. DR EMDB; EMD-51305; -. DR EMDB; EMD-52865; -. DR EMDB; EMD-52866; -. DR EMDB; EMD-52870; -. DR EMDB; EMD-52975; -. DR EMDB; EMD-53590; -. DR EMDB; EMD-53595; -. DR EMDB; EMD-53596; -. DR EMDB; EMD-54924; -. DR EMDB; EMD-54926; -. DR EMDB; EMD-54938; -. DR EMDB; EMD-55003; -. DR EMDB; EMD-55533; -. DR EMDB; EMD-55534; -. DR EMDB; EMD-65716; -. DR EMDB; EMD-65851; -. DR EMDB; EMD-65853; -. DR EMDB; EMD-6699; -. DR EMDB; EMD-6700; -. DR EMDB; EMD-6879; -. DR EMDB; EMD-6880; -. DR EMDB; EMD-6882; -. DR EMDB; EMD-6883; -. DR EMDB; EMD-71726; -. DR EMDB; EMD-72325; -. DR EMDB; EMD-72487; -. DR EMDB; EMD-8246; -. DR EMDB; EMD-9356; -. DR EMDB; EMD-9384; -. DR EMDB; EMD-9843; -. DR EMDB; EMD-9844; -. DR MDposit; P84233; -. DR SASBDB; P84233; -. DR SMR; P84233; -. DR BioGRID; 674575; 12. DR ComplexPortal; CPX-26497; Nucleosome, variant H3.2-H4-H2A.1-H2B1.1. DR DIP; DIP-37430N; -. DR IntAct; P84233; 11. DR iPTMnet; P84233; -. DR GeneID; 108695575; -. DR GeneID; 108704296; -. DR GeneID; 108704298; -. DR GeneID; 108705672; -. DR GeneID; 108716540; -. DR GeneID; 108716541; -. DR GeneID; 121393613; -. DR GeneID; 121394151; -. DR GeneID; 121398064; -. DR GeneID; 121398066; -. DR GeneID; 121399123; -. DR GeneID; 121399124; -. DR GeneID; 121402225; -. DR KEGG; xla:108695575; -. DR KEGG; xla:108704296; -. DR KEGG; xla:108704298; -. DR KEGG; xla:108705672; -. DR KEGG; xla:108716540; -. DR KEGG; xla:108716541; -. DR KEGG; xla:121393613; -. DR KEGG; xla:121394151; -. DR KEGG; xla:121398064; -. DR KEGG; xla:121398066; -. DR KEGG; xla:121399123; -. DR KEGG; xla:121399124; -. DR KEGG; xla:121402225; -. DR Xenbase; XB-GENE-866635; h3c14.L. DR OrthoDB; 9929128at2759; -. DR EvolutionaryTrace; P84233; -. DR Proteomes; UP000186698; Chromosome 3S. DR Proteomes; UP000186698; Chromosome 5L. DR Proteomes; UP000186698; Chromosome 5S. DR Proteomes; UP000186698; Chromosome 6S. DR Proteomes; UP000186698; Chromosome 9_10L. DR Proteomes; UP000186698; Chromosome 9_10S. DR Bgee; 100049126; Expressed in oocyte and 8 other cell types or tissues. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0000786; C:nucleosome; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro. DR GO; GO:0030527; F:structural constituent of chromatin; IDA:UniProtKB. DR GO; GO:0031507; P:heterochromatin formation; NAS:ComplexPortal. DR GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central. DR CDD; cd22911; HFD_H3; 1. DR DisProt; DP01389; -. DR FunFam; 1.10.20.10:FF:000078; Histone H3; 1. DR FunFam; 1.10.20.10:FF:000044; Histone H3.3; 1. DR Gene3D; 1.10.20.10; Histone, subunit A; 1. DR IDEAL; IID50147; -. DR InterPro; IPR007125; H2A/H2B/H3. DR InterPro; IPR009072; Histone-fold. DR InterPro; IPR000164; Histone_H3/CENP-A. DR PANTHER; PTHR11426; HISTONE H3; 1. DR Pfam; PF00125; Histone; 1. DR PRINTS; PR00622; HISTONEH3. DR SMART; SM00428; H3; 1. DR SUPFAM; SSF47113; Histone-fold; 1. DR PROSITE; PS00322; HISTONE_H3_1; 1. DR PROSITE; PS00959; HISTONE_H3_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ADP-ribosylation; Chromosome; Citrullination; KW DNA-binding; Hydroxylation; Isopeptide bond; Lipoprotein; Methylation; KW Nucleosome core; Nucleus; Palmitate; Phosphoprotein; Reference proteome; KW Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P84227" FT CHAIN 2..136 FT /note="Histone H3.2" FT /id="PRO_0000221265" FT REGION 1..43 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 3 FT /note="Asymmetric dimethylarginine; by PRMT6; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 3 FT /note="Citrulline; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 4 FT /note="Phosphothreonine; by HASPIN and VRK1" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 5 FT /note="Allysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 5 FT /note="N6,N6,N6-trimethyllysine; alternate" FT /evidence="ECO:0000269|PubMed:12138181" FT MOD_RES 5 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000269|PubMed:12138181" FT MOD_RES 5 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 5 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 5 FT /note="N6-benzoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 5 FT /note="N6-crotonyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 5 FT /note="N6-methacryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 5 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000269|PubMed:12138181" FT MOD_RES 6 FT /note="5-glutamyl dopamine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 6 FT /note="5-glutamyl serotonin; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 7 FT /note="Phosphothreonine; by PKC" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 9 FT /note="Citrulline; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 9 FT /note="Symmetric dimethylarginine; by PRMT5; alternate" FT /evidence="ECO:0000250" FT MOD_RES 10 FT /note="N6,N6,N6-trimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 10 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 10 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 10 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 10 FT /note="N6-benzoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 10 FT /note="N6-crotonyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 10 FT /note="N6-isonicotinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 10 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 10 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000305|PubMed:12138181" 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:0000250|UniProtKB:Q71DI3" FT MOD_RES 12 FT /note="Phosphothreonine; by PKC" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 15 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 15 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:12138181" FT MOD_RES 15 FT /note="N6-benzoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 15 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 15 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P84228" FT MOD_RES 18 FT /note="Asymmetric dimethylarginine; by CARM1; alternate" FT /evidence="ECO:0000269|PubMed:12138181" FT MOD_RES 18 FT /note="Citrulline; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 19 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 19 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 19 FT /note="N6-benzoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 19 FT /note="N6-butyryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68433" FT MOD_RES 19 FT /note="N6-crotonyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 19 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 19 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 19 FT /note="N6-methacryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 19 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 19 FT /note="N6-propionyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 24 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 24 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 24 FT /note="N6-benzoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68433" FT MOD_RES 24 FT /note="N6-butyryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68433" FT MOD_RES 24 FT /note="N6-crotonyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 24 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 24 FT /note="N6-isonicotinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 24 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 24 FT /note="N6-methacryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 24 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 27 FT /note="Citrulline" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 28 FT /note="N6,N6,N6-trimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 28 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 28 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 28 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 28 FT /note="N6-crotonyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 28 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 28 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 28 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" 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:0000250|UniProtKB:Q71DI3" FT MOD_RES 37 FT /note="N6,N6,N6-trimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 37 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 37 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 37 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 37 FT /note="N6-isonicotinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 37 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 38 FT /note="N6-isonicotinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" 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:Q71DI3" FT MOD_RES 57 FT /note="N6,N6,N6-trimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 57 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 57 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 57 FT /note="N6-crotonyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 57 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 57 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P84228" FT MOD_RES 57 FT /note="N6-methacryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 57 FT /note="N6-methyllysine; by EHMT2; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 57 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P84228" FT MOD_RES 58 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 65 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 65 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 80 FT /note="N6,N6,N6-trimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P84228" FT MOD_RES 80 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 80 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 80 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 80 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 80 FT /note="N6-isonicotinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 80 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 80 FT /note="N6-methacryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 80 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 80 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P84228" FT MOD_RES 81 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" 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:Q71DI3" FT MOD_RES 116 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 123 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 123 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 123 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 123 FT /note="N6-isonicotinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 123 FT /note="N6-methacryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 123 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 123 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT LIPID 111 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT CROSSLNK 15 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin); alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT CROSSLNK 19 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin); alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT CROSSLNK 24 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin); alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT STRAND 4..6 FT /evidence="ECO:0007829|PDB:8HXX" FT STRAND 7..10 FT /evidence="ECO:0007829|PDB:3GV6" FT STRAND 12..14 FT /evidence="ECO:0007829|PDB:9B2S" FT STRAND 16..18 FT /evidence="ECO:0007829|PDB:8HXX" FT STRAND 19..21 FT /evidence="ECO:0007829|PDB:1KX5" FT STRAND 27..29 FT /evidence="ECO:0007829|PDB:1KX5" FT STRAND 31..34 FT /evidence="ECO:0007829|PDB:1KX5" FT HELIX 46..57 FT /evidence="ECO:0007829|PDB:1KX5" FT HELIX 65..77 FT /evidence="ECO:0007829|PDB:2HUE" FT STRAND 80..82 FT /evidence="ECO:0007829|PDB:1KX3" FT HELIX 87..114 FT /evidence="ECO:0007829|PDB:2HUE" FT STRAND 118..120 FT /evidence="ECO:0007829|PDB:2HUE" FT HELIX 122..131 FT /evidence="ECO:0007829|PDB:2HUE" FT TURN 132..135 FT /evidence="ECO:0007829|PDB:1P3I" SQ SEQUENCE 136 AA; 15388 MW; 6FD8508EA50A0EEC CRC64; MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEASEAY LVGLFEDTNL CAIHAKRVTI MPKDIQLARR IRGERA //