ID H4_XENLA Reviewed; 103 AA. AC P62799; P02304; P02305; Q6AZG5; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 161. DE RecName: Full=Histone H4; 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=6274702; DOI=10.1016/0014-5793(81)81211-2; RA Moorman A.F.M., de Boer P.A.J., de Laaf R.T.M., van Dongen W.M.A.M., RA Destree O.H.J.; RT "Primary structure of the histone H3 and H4 genes and their flanking RT sequences in a minor histone gene cluster of Xenopus laevis."; RL FEBS Lett. 136:45-52(1981). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6324093; DOI=10.1093/nar/11.24.8641; RA Clerc R.G., Bucher P., Strub K., Birnstiel M.L.; RT "Transcription of a cloned Xenopus laevis H4 histone gene in the homologous RT frog oocyte system depends on an evolutionary conserved sequence motif in RT the -50 region."; RL Nucleic Acids Res. 11:8641-8657(1983). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Embryo; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 17-103. RX PubMed=9305837; DOI=10.1038/38444; RA Luger K., Mader A.W., Richmond R.K., Sargent D.F., Richmond T.J.; RT "Crystal structure of the nucleosome core particle at 2.8 A resolution."; RL Nature 389:251-260(1997). RN [6] {ECO:0007744|PDB:6WZ5, ECO:0007744|PDB:6WZ9, ECO:0007744|PDB:6X0N} RP STRUCTURE BY ELECTRON MICROSCOPY (2.20 ANGSTROMS) OF 2-103 OF NUCLEOSOME RP CORE COMPLEX IN COMPLEX WITH PARP2 AND HPF1. RX PubMed=32939087; DOI=10.1038/s41586-020-2725-7; RA Bilokapic S., Suskiewicz M.J., Ahel I., Halic M.; RT "Bridging of DNA breaks activates PARP2-HPF1 to modify chromatin."; RL Nature 585:609-613(2020). RN [7] {ECO:0007744|PDB:6ZHX, ECO:0007744|PDB:6ZHY} RP STRUCTURE BY ELECTRON MICROSCOPY (2.50 ANGSTROMS) OF NUCLEOSOME CORE RP COMPLEX IN COMPLEX WITH 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 (4.80 ANGSTROMS) OF NUCLEOSOME CORE RP COMPLEX IN COMPLEX WITH 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 (2.80 ANGSTROMS) OF NUCLEOSOME CORE RP COMPLEX IN COMPLEX WITH 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. 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. CC -!- INTERACTION: CC P62799; P84233; NbExp=2; IntAct=EBI-302085, EBI-350041; CC P62799; Q16576: RBBP7; Xeno; NbExp=2; IntAct=EBI-302085, EBI-352227; CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. CC -!- PTM: Acetylation at Lys-6 (H4K5ac), Lys-9 (H4K8ac), Lys-13 (H4K12ac) CC and Lys-17 (H4K16ac) occurs in coding regions of the genome but not in CC heterochromatin. {ECO:0000250|UniProtKB:P62805}. CC -!- PTM: Citrullination at Arg-4 (H4R3ci) by PADI4 impairs methylation. CC {ECO:0000250|UniProtKB:P62805}. CC -!- PTM: Monomethylation and asymmetric dimethylation at Arg-4 (H4R3me1 and CC H4R3me2a, respectively) by PRMT1 favors acetylation at Lys-9 (H4K8ac) CC and Lys-13 (H4K12ac). Demethylation is performed by JMJD6. Symmetric CC dimethylation on Arg-4 (H4R3me2s) by the PRDM1/PRMT5 complex may play a CC crucial role in the germ-cell lineage (By similarity). CC {ECO:0000250|UniProtKB:P62805}. CC -!- PTM: Monomethylated, dimethylated or trimethylated at Lys-21 (H4K20me1, CC H4K20me2, H4K20me3). Monomethylation is performed by KMT5A/SET8. CC Trimethylation is performed by KMT5B and KMT5C and induces gene CC silencing. Monomethylated at Lys-13 (H4K12me1) by N6AMT1; H4K12me1 CC modification is present at the promoters of numerous genes encoding CC cell cycle regulators. {ECO:0000250|UniProtKB:P62805}. CC -!- PTM: Acetyl-methylated at Lys-6 and Lys-13 (H4K5acme and H4K12acme, CC respectively), acetyl-methylation is an epigenetic mark of active CC chromatin associated with increased transcriptional initiation. Acetyl- CC methylation is formed by acetylation by EP300/p300 of lysine residues CC that are already monomethylated on the same side chain. H4K5acme and CC H4K12acme marks specifically bind BRD2. {ECO:0000250|UniProtKB:P62805}. CC -!- PTM: Phosphorylated by pak2 at Ser-48 (H4S47ph). This phosphorylation CC increases the association of H3.3-H4 with the histone chaperone HIRA, CC thus promoting nucleosome assembly of H3.3-H4 and inhibiting nucleosome CC assembly of H3.1-H4 (By similarity). {ECO:0000250|UniProtKB:P62805}. CC -!- PTM: Ubiquitinated by the CUL4-DDB-RBX1 complex in response to CC ultraviolet irradiation. This may weaken the interaction between CC histones and DNA and facilitate DNA accessibility to repair proteins. CC Monoubiquitinated at Lys-92 of histone H4 (H4K91ub1) in response to DNA CC damage. The exact role of H4K91ub1 in DNA damage response is still CC unclear but it may function as a licensing signal for additional CC histone H4 post-translational modifications such as H4 Lys-21 CC methylation (H4K20me) (By similarity). {ECO:0000250|UniProtKB:P62805}. CC -!- PTM: Sumoylated, which is associated with transcriptional repression. CC {ECO:0000250|UniProtKB:P62805}. CC -!- PTM: Butyrylation of histones marks active promoters and competes with CC histone acetylation. {ECO:0000250|UniProtKB:P62806}. CC -!- PTM: Glutarylation at Lys-92 (H4K91glu) destabilizes nucleosomes by CC promoting dissociation of the H2A-H2B dimers from nucleosomes. CC {ECO:0000250|UniProtKB:P62805}. CC -!- PTM: Ufmylated; monofmylated by UFL1 at Lys-32 (H4K31Ufm1) in response CC to DNA damage. {ECO:0000250|UniProtKB:P62805}. 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:P62805}. CC -!- SIMILARITY: Belongs to the histone H4 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; X00224; CAA25042.1; -; Genomic_DNA. DR EMBL; X03017; CAA26809.1; -; Genomic_DNA. DR EMBL; X03017; CAA26814.1; -; Genomic_DNA. DR EMBL; X03018; CAA26819.1; -; Genomic_DNA. DR EMBL; M21286; AAA49761.1; -; Genomic_DNA. DR EMBL; M21286; AAA49766.1; -; Genomic_DNA. DR EMBL; M21287; AAA49771.1; -; Genomic_DNA. DR EMBL; BC078038; AAH78038.1; -; mRNA. DR PIR; A02641; HSXL4. DR RefSeq; NP_001087926.1; NM_001094457.1. DR RefSeq; XP_018095104.1; XM_018239615.1. DR RefSeq; XP_018095605.1; XM_018240116.1. DR RefSeq; XP_018095606.1; XM_018240117.1. DR RefSeq; XP_018095629.1; XM_018240140.1. DR RefSeq; XP_018096302.1; XM_018240813.1. DR RefSeq; XP_018097458.1; XM_018241969.1. DR RefSeq; XP_018098137.1; XM_018242648.1. DR RefSeq; XP_018118237.1; XM_018262748.1. DR RefSeq; XP_018120359.1; XM_018264870.1. DR RefSeq; XP_018120360.1; XM_018264871.1. DR PDB; 1AOI; X-ray; 2.80 A; B/F=17-103. DR PDB; 1KX3; X-ray; 2.00 A; B/F=2-103. DR PDB; 1KX4; X-ray; 2.60 A; B/F=2-103. DR PDB; 1KX5; X-ray; 1.94 A; B/F=2-103. DR PDB; 1M18; X-ray; 2.45 A; B/F=2-103. DR PDB; 1M19; X-ray; 2.30 A; B/F=2-103. DR PDB; 1M1A; X-ray; 2.65 A; B/F=2-103. DR PDB; 1P34; X-ray; 2.70 A; B/F=2-103. DR PDB; 1P3A; X-ray; 3.00 A; B/F=2-103. DR PDB; 1P3B; X-ray; 3.00 A; B/F=2-103. DR PDB; 1P3F; X-ray; 2.90 A; B/F=2-103. DR PDB; 1P3G; X-ray; 2.70 A; B/F=2-103. DR PDB; 1P3I; X-ray; 2.30 A; B/F=2-103. DR PDB; 1P3K; X-ray; 2.90 A; B/F=2-103. DR PDB; 1P3L; X-ray; 2.40 A; B/F=2-103. DR PDB; 1P3M; X-ray; 2.90 A; B/F=2-103. DR PDB; 1P3O; X-ray; 2.75 A; B/F=2-103. DR PDB; 1P3P; X-ray; 2.70 A; B/F=2-103. DR PDB; 1S32; X-ray; 2.05 A; B/F=2-103. DR PDB; 1ZBB; X-ray; 9.00 A; B/F/b/f=2-103. DR PDB; 1ZLA; X-ray; 2.90 A; B/F=2-103. DR PDB; 2F8N; X-ray; 2.90 A; B/F=1-103. DR PDB; 2FJ7; X-ray; 3.20 A; B/F=2-103. DR PDB; 2HUE; X-ray; 1.70 A; C=21-103. DR PDB; 2IO5; X-ray; 2.70 A; C=2-103. DR PDB; 2NZD; X-ray; 2.65 A; B/F=2-103. DR PDB; 3B6F; X-ray; 3.45 A; B/F=2-103. DR PDB; 3B6G; X-ray; 3.45 A; B/F=2-103. DR PDB; 3C1B; X-ray; 2.20 A; B/F=2-103. DR PDB; 3C1C; X-ray; 3.15 A; B/F=2-103. DR PDB; 3KUY; X-ray; 2.90 A; B/F=2-103. DR PDB; 3KWQ; X-ray; 3.50 A; B/F=21-103. DR PDB; 3KXB; X-ray; 3.20 A; B/F=2-103. DR PDB; 3LEL; X-ray; 2.95 A; B/F/L/P=2-103. DR PDB; 3LJA; X-ray; 2.75 A; B/F=2-103. DR PDB; 3LZ0; X-ray; 2.50 A; B/F=2-103. DR PDB; 3LZ1; X-ray; 2.50 A; B/F=2-103. DR PDB; 3MGP; X-ray; 2.44 A; B/F=2-103. DR PDB; 3MGQ; X-ray; 2.65 A; B/F=2-103. DR PDB; 3MGR; X-ray; 2.30 A; B/F=2-103. DR PDB; 3MGS; X-ray; 3.15 A; B/F=2-103. DR PDB; 3MNN; X-ray; 2.50 A; B/F=2-103. DR PDB; 3MVD; X-ray; 2.90 A; B/F=2-103. DR PDB; 3O62; X-ray; 3.22 A; B/F=2-103. DR PDB; 3REH; X-ray; 2.50 A; B/F=2-103. DR PDB; 3REI; X-ray; 2.65 A; B/F=2-103. DR PDB; 3REJ; X-ray; 2.55 A; B/F=2-103. DR PDB; 3REK; X-ray; 2.60 A; B/F=2-103. DR PDB; 3REL; X-ray; 2.70 A; B/F=2-103. DR PDB; 3TU4; X-ray; 3.00 A; B/F=2-103. DR PDB; 3UT9; X-ray; 2.20 A; B/F=2-103. DR PDB; 3UTA; X-ray; 2.07 A; B/F=2-103. DR PDB; 3UTB; X-ray; 2.20 A; B/F=2-103. DR PDB; 4EO5; X-ray; 2.35 A; C=21-103. DR PDB; 4J8U; X-ray; 2.38 A; B/F=2-103. DR PDB; 4J8V; X-ray; 2.58 A; B/F=2-103. DR PDB; 4J8W; X-ray; 2.41 A; B/F=2-103. DR PDB; 4J8X; X-ray; 2.87 A; B/F=2-103. DR PDB; 4KGC; X-ray; 2.69 A; B/F=1-103. DR PDB; 4LD9; X-ray; 3.31 A; B/F=1-103. DR PDB; 4R8P; X-ray; 3.28 A; B/F=2-103. DR PDB; 4WU8; X-ray; 2.45 A; B/F=2-103. DR PDB; 4WU9; X-ray; 2.60 A; B/F=2-103. DR PDB; 4XUJ; X-ray; 3.18 A; B/F=2-103. DR PDB; 4XZQ; X-ray; 2.40 A; B/F=25-103. DR PDB; 4YS3; X-ray; 3.00 A; B/F=25-103. DR PDB; 4Z66; X-ray; 2.50 A; B/F=22-103. DR PDB; 4ZBJ; X-ray; 2.25 A; C=21-103. DR PDB; 4ZUX; X-ray; 3.82 A; B/F/L/P=1-103. DR PDB; 5BS7; X-ray; 3.30 A; C/D=2-103. DR PDB; 5BSA; X-ray; 4.61 A; C/D=2-103. DR PDB; 5CP6; X-ray; 2.60 A; B/F=2-103. DR PDB; 5DNM; X-ray; 2.81 A; B/F=2-103. DR PDB; 5DNN; X-ray; 2.80 A; B/F=2-103. DR PDB; 5E5A; X-ray; 2.81 A; B/F=1-103. DR PDB; 5F99; X-ray; 2.63 A; B/F=1-103. DR PDB; 5HQ2; X-ray; 4.50 A; B=2-103. DR PDB; 5KGF; EM; 4.54 A; B/F=1-103. DR PDB; 5MLU; X-ray; 2.80 A; B/F=20-103. DR PDB; 5NL0; X-ray; 5.40 A; B/F/L=2-103. DR PDB; 5O9G; EM; 4.80 A; B/F=1-103. DR PDB; 5OMX; X-ray; 2.32 A; B/F=1-103. DR PDB; 5ONG; X-ray; 2.80 A; B/F=1-103. DR PDB; 5ONW; X-ray; 2.80 A; B/F=1-103. DR PDB; 5OXV; X-ray; 6.72 A; B/F/L/P=2-103. DR PDB; 5OY7; X-ray; 5.77 A; B/F/J/N/R/V/Z/d=2-103. DR PDB; 5X0X; EM; 3.97 A; B/F=1-103. DR PDB; 5X0Y; EM; 3.97 A; B/F=2-103. DR PDB; 5XF6; X-ray; 2.63 A; B/F=2-103. DR PDB; 5Z3L; EM; 4.31 A; B/F=2-103. DR PDB; 5Z3O; EM; 3.62 A; B/F=2-103. DR PDB; 5Z3U; EM; 4.31 A; B/F=2-103. DR PDB; 5Z3V; EM; 4.22 A; B/F=2-103. DR PDB; 6ESF; EM; 3.70 A; B/F=2-103. DR PDB; 6ESG; EM; 5.40 A; B/F=2-103. DR PDB; 6ESH; EM; 5.10 A; B/F=2-103. DR PDB; 6ESI; EM; 6.30 A; B/F=2-103. DR PDB; 6FQ5; EM; 3.80 A; B=19-102, F=19-103. DR PDB; 6FQ6; EM; 4.00 A; B/F=19-103. DR PDB; 6FQ8; EM; 4.80 A; B/F=18-103. DR PDB; 6FTX; EM; 4.50 A; B/F=1-103. DR PDB; 6G0L; EM; 4.50 A; B/F=1-103. DR PDB; 6GYT; X-ray; 2.50 A; C=10-17. DR PDB; 6I84; EM; 4.40 A; O/U=1-103. DR PDB; 6IRO; EM; 3.40 A; B/F=2-103. DR PDB; 6IY2; EM; 3.47 A; B/F=16-103. DR PDB; 6IY3; EM; 3.67 A; B/F=16-103. DR PDB; 6J99; EM; 4.10 A; B/F=1-103. DR PDB; 6JM9; EM; 7.30 A; B/F=17-103. DR PDB; 6JMA; EM; 6.80 A; B/F=17-103. DR PDB; 6JYL; EM; 3.37 A; B/F=2-103. DR PDB; 6K1P; EM; 3.87 A; B/F=2-103. DR PDB; 6KIU; EM; 3.20 A; B/F=2-103. DR PDB; 6KIV; EM; 4.00 A; B/F=2-103. DR PDB; 6KIW; EM; 4.00 A; B/F=2-103. DR PDB; 6KIX; EM; 4.10 A; B/F=2-103. DR PDB; 6KIZ; EM; 4.50 A; B/F=2-103. DR PDB; 6KW3; EM; 7.13 A; B/R=1-103. DR PDB; 6KW4; EM; 7.55 A; B/R=1-103. DR PDB; 6KW5; EM; 10.13 A; S/W=1-103. DR PDB; 6LTJ; EM; 3.70 A; B/F=1-103. DR PDB; 6NE3; EM; 3.90 A; B/F=1-103. DR PDB; 6NJ9; EM; 2.96 A; B/F=2-103. DR PDB; 6NN6; EM; 3.90 A; B/F=2-103. DR PDB; 6NOG; EM; 3.90 A; B/F=2-103. DR PDB; 6NQA; EM; 3.54 A; B/F=2-103. DR PDB; 6NZO; EM; 3.80 A; B/F=1-103. DR PDB; 6O22; Other; -; F=1-103. DR PDB; 6O96; EM; 3.50 A; B/F=1-103. DR PDB; 6OM3; X-ray; 3.30 A; B/F/N/R=1-103. DR PDB; 6PA7; EM; 2.94 A; B/F=1-103. DR PDB; 6PWV; EM; 6.20 A; H/L=1-103. DR PDB; 6PWW; EM; 4.40 A; H/L=1-103. DR PDB; 6PWX; EM; 4.20 A; H/L=1-103. DR PDB; 6PX1; EM; 3.30 A; B/F=1-103. DR PDB; 6PX3; EM; 4.10 A; B/F=1-103. DR PDB; 6R1T; EM; 3.70 A; B/F=17-103. DR PDB; 6R1U; EM; 4.36 A; B/F=2-103. DR PDB; 6R25; EM; 4.61 A; B/F=2-103. DR PDB; 6RYR; EM; 3.10 A; B/F=1-103. DR PDB; 6RYU; EM; 4.00 A; B/F=1-103. DR PDB; 6S01; EM; 3.20 A; B/F=2-103. DR PDB; 6T9L; EM; 3.60 A; B/F=2-103. DR PDB; 6TDA; EM; 15.00 A; B/F=2-103. DR PDB; 6TEM; EM; 3.90 A; B/F=1-103. DR PDB; 6UGM; EM; 3.70 A; B/F=2-103. DR PDB; 6UH5; EM; 3.50 A; B/F=2-103. DR PDB; 6UXW; EM; 8.96 A; S/W=2-103. DR PDB; 6VEN; EM; 3.37 A; B/F=2-103. DR PDB; 6VYP; X-ray; 4.99 A; B/F/b/f=2-103. DR PDB; 6VZ4; EM; 3.90 A; B/F=1-103. DR PDB; 6W5I; EM; 6.90 A; H/L=1-103. DR PDB; 6W5M; EM; 4.60 A; H/L=1-103. DR PDB; 6W5N; EM; 6.00 A; H/L=1-103. DR PDB; 6WKR; EM; 3.50 A; J/Q=1-103. DR PDB; 6WZ5; EM; 2.20 A; B/F=2-103. DR PDB; 6WZ9; EM; 2.80 A; B/F=2-103. DR PDB; 6X0N; EM; 10.00 A; B/F/b/f=2-103. DR PDB; 6YN1; X-ray; 2.35 A; D/I/N/S/X/c/h/m=21-103. DR PDB; 6ZHX; EM; 2.50 A; B/F=1-103. DR PDB; 6ZHY; EM; 3.00 A; B/F=1-103. DR PDB; 7AT8; EM; 4.40 A; E/I=2-103. DR PDB; 7CRO; EM; 3.75 A; B/F=2-103. DR PDB; 7CRP; EM; 3.20 A; B/F=2-103. DR PDB; 7CRQ; EM; 3.15 A; B/F=2-103. DR PDB; 7CRR; EM; 3.48 A; B/F=2-103. DR PDB; 7E8I; EM; 3.10 A; B/F=2-103. DR PDB; 7EA5; EM; 3.30 A; B/F=25-102. DR PDB; 7EA8; EM; 3.10 A; B/F=25-102. DR PDB; 7EG6; EM; 3.10 A; B/F=2-103. DR PDB; 7EGP; EM; 6.90 A; P/T=2-103. DR PDB; 7ENN; EM; 2.80 A; F/L=2-103. DR PDB; 7K6P; EM; 3.20 A; B/F=14-103. DR PDB; 7K6Q; EM; 3.10 A; B/F=12-103. DR PDB; 7KBD; EM; 3.38 A; B/F=1-103. DR PDB; 7KBE; EM; 3.50 A; B/F=1-103. DR PDB; 7KBF; EM; 4.42 A; B/F=1-103. DR PDB; 7KTQ; EM; 3.30 A; B/F=25-103. DR PDB; 7M1X; EM; 3.70 A; B/F=1-103. DR PDB; 7MBM; EM; -; H/L=1-103. DR PDB; 7MBN; EM; -; H/L=1-103. DR PDB; 7NKX; EM; 2.90 A; b/f=1-103. DR PDB; 7NKY; EM; 3.20 A; b/f=1-103. DR PDB; 7OH9; EM; 3.00 A; B/F=2-103. DR PDB; 7OHA; EM; 2.90 A; B/F=2-103. DR PDB; 7OHB; EM; 3.40 A; B/F=2-103. DR PDB; 7OHC; EM; 2.50 A; B/F=2-103. DR PDB; 7OTQ; EM; 4.80 A; B/F=1-103. DR PDB; 7SSA; EM; 3.20 A; B/F=1-103. DR PDB; 7SWY; EM; 2.60 A; B/F=2-103. DR PDB; 7TN2; EM; 2.30 A; B/F=2-103. DR PDB; 7UD5; EM; 4.25 A; B/F=1-103. DR PDB; 7UNC; EM; 3.00 A; b/f=1-103. DR PDB; 7UND; EM; 3.00 A; b/f=1-103. DR PDB; 7UNK; EM; 3.45 A; E=1-103. DR PDB; 7UX9; EM; 3.20 A; G/H=1-103. DR PDB; 7VDT; EM; 2.80 A; B/F=1-103. DR PDB; 7VDV; EM; 3.40 A; B/F=1-103. DR PDB; 7VVU; EM; 3.40 A; B/Q=1-103. DR PDB; 7VVZ; EM; 8.80 A; B/Q=1-103. DR PDB; 7X3T; EM; 5.40 A; B/F/L/P=1-103. DR PDB; 7X3V; EM; 3.09 A; B/F=1-103. DR PDB; 7X3W; EM; 3.10 A; B/F=1-103. DR PDB; 7X3X; EM; 3.20 A; B/F=1-103. DR PDB; 7XFC; EM; 2.90 A; B/F=1-103. DR PDB; 7XFH; EM; 2.90 A; B/F=1-103. DR PDB; 7XFI; EM; 2.90 A; B/F=1-103. DR PDB; 7XFJ; EM; 3.00 A; B/F=1-103. DR PDB; 7XFL; EM; 2.80 A; B/F=1-103. DR PDB; 7XFM; EM; 3.10 A; B/F=1-103. DR PDB; 7XFN; EM; 2.80 A; B/F=1-103. DR PDB; 7XNP; EM; 2.90 A; B/F=1-103. DR PDB; 7XPX; EM; 3.20 A; B/F=2-103. DR PDB; 7YI1; EM; 2.80 A; B/F=2-103. DR PDB; 7YI4; EM; 3.96 A; H/L=2-103. DR PDB; 7YI5; EM; 3.96 A; H/L=2-103. DR PDB; 7ZS9; EM; 3.10 A; b/f=2-103. DR PDB; 7ZSA; EM; 4.00 A; b/f=2-103. DR PDB; 7ZSB; EM; 6.60 A; b/f=2-103. DR PDB; 8B0A; EM; 3.00 A; B/F=1-103. DR PDB; 8BVW; EM; 4.00 A; b/f=1-103. DR PDB; 8BYQ; EM; 4.10 A; b/f=1-103. DR PDB; 8BZ1; EM; 3.80 A; b/f=1-103. DR PDB; 8CBQ; EM; 4.00 A; B/F=2-103. DR PDB; 8CEO; EM; 3.60 A; s/w=2-103. DR PDB; 8CWW; EM; 2.74 A; B/F=2-103. DR PDB; 8CZE; EM; 2.58 A; B/F=2-103. DR PDB; 8DU4; EM; 3.55 A; B/F=1-103. DR PDB; 8ETT; EM; 6.68 A; B/F=1-103. DR PDB; 8EU2; EM; 2.93 A; L/P=24-103. DR PDB; 8EUE; EM; 3.48 A; B/F=23-103. DR PDB; 8EUJ; EM; 3.36 A; O/h=23-103. DR PDB; 8F86; EM; 3.10 A; B/F=2-103. DR PDB; 8G57; EM; 3.07 A; B/F=19-103. DR PDB; 8G86; EM; 2.30 A; B/F=2-103. DR PDB; 8G88; EM; 4.80 A; B/F=2-103. DR PDB; 8G8B; EM; 4.30 A; B/F=2-103. DR PDB; 8G8G; EM; 3.20 A; B/F=2-103. DR PDB; 8GPN; EM; 3.20 A; B/F=1-103. DR PDB; 8GXQ; EM; 5.04 A; NB/NF=1-103. DR PDB; 8GXS; EM; 4.16 A; NB/NF=1-103. DR PDB; 8KD2; EM; 3.02 A; P/T=2-103. DR PDB; 8KD3; EM; 2.90 A; P/T=2-103. DR PDB; 8KD4; EM; 2.93 A; P/T=2-103. DR PDB; 8KD5; EM; 2.90 A; P/T=2-103. DR PDB; 8KD6; EM; 3.07 A; P/T=2-103. DR PDB; 8KD7; EM; 3.09 A; P/T=2-103. DR PDB; 8OF4; EM; 2.94 A; B/F=1-103. DR PDB; 8PC5; EM; 3.04 A; B/F=2-103. DR PDB; 8PC6; EM; 3.04 A; B/F=2-103. DR PDB; 8PEO; EM; 2.69 A; B/F=2-103. DR PDB; 8PEP; EM; 3.33 A; B/F=2-103. DR PDB; 8SVF; EM; 3.20 A; B/F=1-103. DR PDB; 8T3T; EM; 3.21 A; B/F=2-103. DR PDB; 8T3W; EM; 3.25 A; B/F=2-103. DR PDB; 8T3Y; EM; 3.47 A; B/F=2-103. DR PDBsum; 1AOI; -. DR PDBsum; 1KX3; -. DR PDBsum; 1KX4; -. DR PDBsum; 1KX5; -. DR PDBsum; 1M18; -. DR PDBsum; 1M19; -. DR PDBsum; 1M1A; -. DR PDBsum; 1P34; -. DR PDBsum; 1P3A; -. DR PDBsum; 1P3B; -. DR PDBsum; 1P3F; -. DR PDBsum; 1P3G; -. DR PDBsum; 1P3I; -. DR PDBsum; 1P3K; -. DR PDBsum; 1P3L; -. DR PDBsum; 1P3M; -. DR PDBsum; 1P3O; -. DR PDBsum; 1P3P; -. DR PDBsum; 1S32; -. DR PDBsum; 1ZBB; -. DR PDBsum; 1ZLA; -. DR PDBsum; 2F8N; -. DR PDBsum; 2FJ7; -. DR PDBsum; 2HUE; -. DR PDBsum; 2IO5; -. DR PDBsum; 2NZD; -. DR PDBsum; 3B6F; -. DR PDBsum; 3B6G; -. DR PDBsum; 3C1B; -. DR PDBsum; 3C1C; -. DR PDBsum; 3KUY; -. DR PDBsum; 3KWQ; -. DR PDBsum; 3KXB; -. DR PDBsum; 3LEL; -. DR PDBsum; 3LJA; -. DR PDBsum; 3LZ0; -. DR PDBsum; 3LZ1; -. DR PDBsum; 3MGP; -. DR PDBsum; 3MGQ; -. DR PDBsum; 3MGR; -. DR PDBsum; 3MGS; -. DR PDBsum; 3MNN; -. DR PDBsum; 3MVD; -. DR PDBsum; 3O62; -. DR PDBsum; 3REH; -. DR PDBsum; 3REI; -. DR PDBsum; 3REJ; -. DR PDBsum; 3REK; -. DR PDBsum; 3REL; -. DR PDBsum; 3TU4; -. DR PDBsum; 3UT9; -. DR PDBsum; 3UTA; -. DR PDBsum; 3UTB; -. DR PDBsum; 4EO5; -. DR PDBsum; 4J8U; -. DR PDBsum; 4J8V; -. DR PDBsum; 4J8W; -. DR PDBsum; 4J8X; -. DR PDBsum; 4KGC; -. DR PDBsum; 4LD9; -. DR PDBsum; 4R8P; -. DR PDBsum; 4WU8; -. DR PDBsum; 4WU9; -. DR PDBsum; 4XUJ; -. DR PDBsum; 4XZQ; -. DR PDBsum; 4YS3; -. DR PDBsum; 4Z66; -. DR PDBsum; 4ZBJ; -. DR PDBsum; 4ZUX; -. DR PDBsum; 5BS7; -. DR PDBsum; 5BSA; -. DR PDBsum; 5CP6; -. DR PDBsum; 5DNM; -. DR PDBsum; 5DNN; -. DR PDBsum; 5E5A; -. DR PDBsum; 5F99; -. DR PDBsum; 5HQ2; -. DR PDBsum; 5KGF; -. DR PDBsum; 5MLU; -. DR PDBsum; 5NL0; -. DR PDBsum; 5O9G; -. DR PDBsum; 5OMX; -. DR PDBsum; 5ONG; -. DR PDBsum; 5ONW; -. DR PDBsum; 5OXV; -. DR PDBsum; 5OY7; -. DR PDBsum; 5X0X; -. DR PDBsum; 5X0Y; -. DR PDBsum; 5XF6; -. DR PDBsum; 5Z3L; -. DR PDBsum; 5Z3O; -. DR PDBsum; 5Z3U; -. DR PDBsum; 5Z3V; -. DR PDBsum; 6ESF; -. DR PDBsum; 6ESG; -. DR PDBsum; 6ESH; -. DR PDBsum; 6ESI; -. DR PDBsum; 6FQ5; -. DR PDBsum; 6FQ6; -. DR PDBsum; 6FQ8; -. DR PDBsum; 6FTX; -. DR PDBsum; 6G0L; -. DR PDBsum; 6GYT; -. DR PDBsum; 6I84; -. DR PDBsum; 6IRO; -. DR PDBsum; 6IY2; -. DR PDBsum; 6IY3; -. DR PDBsum; 6J99; -. DR PDBsum; 6JM9; -. DR PDBsum; 6JMA; -. DR PDBsum; 6JYL; -. DR PDBsum; 6K1P; -. DR PDBsum; 6KIU; -. DR PDBsum; 6KIV; -. DR PDBsum; 6KIW; -. DR PDBsum; 6KIX; -. DR PDBsum; 6KIZ; -. DR PDBsum; 6KW3; -. DR PDBsum; 6KW4; -. DR PDBsum; 6KW5; -. DR PDBsum; 6LTJ; -. DR PDBsum; 6NE3; -. DR PDBsum; 6NJ9; -. DR PDBsum; 6NN6; -. DR PDBsum; 6NOG; -. DR PDBsum; 6NQA; -. DR PDBsum; 6NZO; -. DR PDBsum; 6O22; -. DR PDBsum; 6O96; -. DR PDBsum; 6OM3; -. DR PDBsum; 6PA7; -. DR PDBsum; 6PWV; -. DR PDBsum; 6PWW; -. DR PDBsum; 6PWX; -. DR PDBsum; 6PX1; -. DR PDBsum; 6PX3; -. DR PDBsum; 6R1T; -. DR PDBsum; 6R1U; -. DR PDBsum; 6R25; -. DR PDBsum; 6RYR; -. DR PDBsum; 6RYU; -. DR PDBsum; 6S01; -. DR PDBsum; 6T9L; -. DR PDBsum; 6TDA; -. DR PDBsum; 6TEM; -. DR PDBsum; 6UGM; -. DR PDBsum; 6UH5; -. DR PDBsum; 6UXW; -. DR PDBsum; 6VEN; -. DR PDBsum; 6VYP; -. DR PDBsum; 6VZ4; -. DR PDBsum; 6W5I; -. DR PDBsum; 6W5M; -. DR PDBsum; 6W5N; -. DR PDBsum; 6WKR; -. DR PDBsum; 6WZ5; -. DR PDBsum; 6WZ9; -. DR PDBsum; 6X0N; -. DR PDBsum; 6YN1; -. DR PDBsum; 6ZHX; -. DR PDBsum; 6ZHY; -. DR PDBsum; 7AT8; -. DR PDBsum; 7CRO; -. DR PDBsum; 7CRP; -. DR PDBsum; 7CRQ; -. DR PDBsum; 7CRR; -. DR PDBsum; 7E8I; -. DR PDBsum; 7EA5; -. DR PDBsum; 7EA8; -. DR PDBsum; 7EG6; -. DR PDBsum; 7EGP; -. DR PDBsum; 7ENN; -. DR PDBsum; 7K6P; -. DR PDBsum; 7K6Q; -. DR PDBsum; 7KBD; -. DR PDBsum; 7KBE; -. DR PDBsum; 7KBF; -. DR PDBsum; 7KTQ; -. DR PDBsum; 7M1X; -. DR PDBsum; 7MBM; -. DR PDBsum; 7MBN; -. DR PDBsum; 7NKX; -. DR PDBsum; 7NKY; -. DR PDBsum; 7OH9; -. DR PDBsum; 7OHA; -. DR PDBsum; 7OHB; -. DR PDBsum; 7OHC; -. DR PDBsum; 7OTQ; -. DR PDBsum; 7SSA; -. DR PDBsum; 7SWY; -. DR PDBsum; 7TN2; -. DR PDBsum; 7UD5; -. DR PDBsum; 7UNC; -. DR PDBsum; 7UND; -. DR PDBsum; 7UNK; -. DR PDBsum; 7UX9; -. DR PDBsum; 7VDT; -. DR PDBsum; 7VDV; -. DR PDBsum; 7VVU; -. DR PDBsum; 7VVZ; -. DR PDBsum; 7X3T; -. DR PDBsum; 7X3V; -. DR PDBsum; 7X3W; -. DR PDBsum; 7X3X; -. DR PDBsum; 7XFC; -. DR PDBsum; 7XFH; -. DR PDBsum; 7XFI; -. DR PDBsum; 7XFJ; -. DR PDBsum; 7XFL; -. DR PDBsum; 7XFM; -. DR PDBsum; 7XFN; -. DR PDBsum; 7XNP; -. DR PDBsum; 7XPX; -. DR PDBsum; 7YI1; -. DR PDBsum; 7YI4; -. DR PDBsum; 7YI5; -. DR PDBsum; 7ZS9; -. DR PDBsum; 7ZSA; -. DR PDBsum; 7ZSB; -. DR PDBsum; 8B0A; -. DR PDBsum; 8BVW; -. DR PDBsum; 8BYQ; -. DR PDBsum; 8BZ1; -. DR PDBsum; 8CBQ; -. DR PDBsum; 8CEO; -. DR PDBsum; 8CWW; -. DR PDBsum; 8CZE; -. DR PDBsum; 8DU4; -. DR PDBsum; 8ETT; -. DR PDBsum; 8EU2; -. DR PDBsum; 8EUE; -. DR PDBsum; 8EUJ; -. DR PDBsum; 8F86; -. DR PDBsum; 8G57; -. DR PDBsum; 8G86; -. DR PDBsum; 8G88; -. DR PDBsum; 8G8B; -. DR PDBsum; 8G8G; -. DR PDBsum; 8GPN; -. DR PDBsum; 8GXQ; -. DR PDBsum; 8GXS; -. DR PDBsum; 8KD2; -. DR PDBsum; 8KD3; -. DR PDBsum; 8KD4; -. DR PDBsum; 8KD5; -. DR PDBsum; 8KD6; -. DR PDBsum; 8KD7; -. DR PDBsum; 8OF4; -. DR PDBsum; 8PC5; -. DR PDBsum; 8PC6; -. DR PDBsum; 8PEO; -. DR PDBsum; 8PEP; -. DR PDBsum; 8SVF; -. DR PDBsum; 8T3T; -. DR PDBsum; 8T3W; -. DR PDBsum; 8T3Y; -. DR AlphaFoldDB; P62799; -. DR EMDB; EMD-0458; -. DR EMDB; EMD-0468; -. DR EMDB; EMD-0480; -. DR EMDB; EMD-0559; -. DR EMDB; EMD-0693; -. DR EMDB; EMD-0694; -. DR EMDB; EMD-0695; -. DR EMDB; EMD-0777; -. DR EMDB; EMD-0778; -. DR EMDB; EMD-0779; -. DR EMDB; EMD-0974; -. DR EMDB; EMD-10058; -. DR EMDB; EMD-10059; -. DR EMDB; EMD-10069; -. DR EMDB; EMD-10415; -. DR EMDB; EMD-10465; -. DR EMDB; EMD-11220; -. DR EMDB; EMD-11221; -. 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-15777; -. DR EMDB; EMD-16549; -. DR EMDB; EMD-16842; -. DR EMDB; EMD-16845; -. DR EMDB; EMD-17594; -. DR EMDB; EMD-17595; -. DR EMDB; EMD-17633; -. DR EMDB; EMD-17634; -. DR EMDB; EMD-17944; -. DR EMDB; EMD-20281; -. DR EMDB; EMD-20512; -. DR EMDB; EMD-20513; -. DR EMDB; EMD-20514; -. DR EMDB; EMD-20516; -. DR EMDB; EMD-20517; -. DR EMDB; EMD-20765; -. DR EMDB; EMD-20767; -. DR EMDB; EMD-20934; -. DR EMDB; EMD-21157; -. DR EMDB; EMD-21484; -. 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-23026; -. DR EMDB; EMD-23626; -. DR EMDB; EMD-23738; -. DR EMDB; EMD-23739; -. DR EMDB; EMD-26454; -. DR EMDB; EMD-26620; -. DR EMDB; EMD-26621; -. DR EMDB; EMD-26625; -. DR EMDB; EMD-26855; -. DR EMDB; EMD-27715; -. DR EMDB; EMD-28598; -. DR EMDB; EMD-28600; -. DR EMDB; EMD-28602; -. DR EMDB; EMD-29837; -. DR EMDB; EMD-29843; -. DR EMDB; EMD-29845; -. DR EMDB; EMD-29850; -. DR EMDB; EMD-30453; -. DR EMDB; EMD-30455; -. DR EMDB; EMD-30456; -. DR EMDB; EMD-30457; -. DR EMDB; EMD-31020; -. DR EMDB; EMD-31039; -. DR EMDB; EMD-31040; -. DR EMDB; EMD-31106; -. DR EMDB; EMD-31137; -. DR EMDB; EMD-31217; -. DR EMDB; EMD-31925; -. DR EMDB; EMD-31926; -. DR EMDB; EMD-32148; -. DR EMDB; EMD-32150; -. DR EMDB; EMD-32992; -. DR EMDB; EMD-32994; -. DR EMDB; EMD-32995; -. DR EMDB; EMD-32996; -. 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-33848; -. DR EMDB; EMD-33851; -. DR EMDB; EMD-33852; -. DR EMDB; EMD-34359; -. DR EMDB; EMD-34360; -. DR EMDB; EMD-37122; -. DR EMDB; EMD-37123; -. DR EMDB; EMD-37124; -. DR EMDB; EMD-37125; -. DR EMDB; EMD-37126; -. DR EMDB; EMD-37127; -. DR EMDB; EMD-3765; -. DR EMDB; EMD-3947; -. DR EMDB; EMD-3948; -. DR EMDB; EMD-3949; -. DR EMDB; EMD-3950; -. DR EMDB; EMD-40789; -. DR EMDB; EMD-41011; -. DR EMDB; EMD-41015; -. DR EMDB; EMD-41016; -. DR EMDB; EMD-4297; -. DR EMDB; EMD-4298; -. DR EMDB; EMD-4299; -. DR EMDB; EMD-4318; -. DR EMDB; EMD-4336; -. DR EMDB; EMD-4429; -. DR EMDB; EMD-4705; -. DR EMDB; EMD-4710; -. 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-8246; -. DR EMDB; EMD-9356; -. DR EMDB; EMD-9384; -. DR EMDB; EMD-9718; -. DR EMDB; EMD-9719; -. DR EMDB; EMD-9720; -. DR EMDB; EMD-9748; -. DR EMDB; EMD-9783; -. DR EMDB; EMD-9843; -. DR EMDB; EMD-9844; -. DR EMDB; EMD-9998; -. DR EMDB; EMD-9999; -. DR SASBDB; P62799; -. DR SMR; P62799; -. DR BioGRID; 104647; 16. DR DIP; DIP-37429N; -. DR IntAct; P62799; 14. DR MoonProt; P62799; -. DR DNASU; 447787; -. DR GeneID; 108703479; -. DR GeneID; 108703798; -. DR GeneID; 108703799; -. DR GeneID; 108703833; -. DR GeneID; 108704306; -. DR GeneID; 108705162; -. DR GeneID; 108705878; -. DR GeneID; 108717647; -. DR GeneID; 108717648; -. DR GeneID; 447787; -. DR KEGG; xla:108703479; -. DR KEGG; xla:108703798; -. DR KEGG; xla:108703799; -. DR KEGG; xla:108703833; -. DR KEGG; xla:108704306; -. DR KEGG; xla:108705162; -. DR KEGG; xla:108705878; -. DR KEGG; xla:108717647; -. DR KEGG; xla:108717648; -. DR KEGG; xla:447787; -. DR AGR; Xenbase:XB-GENE-6493984; -. DR CTD; 447787; -. DR Xenbase; XB-GENE-6493984; h4c1.L. DR OrthoDB; 4019611at2759; -. DR EvolutionaryTrace; P62799; -. DR Proteomes; UP000186698; Chromosome 3S. DR Proteomes; UP000186698; Chromosome 5S. DR Proteomes; UP000186698; Chromosome 9_10L. DR Proteomes; UP000186698; Chromosome 9_10S. DR Bgee; 108703479; Expressed in oocyte and 11 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:0046982; F:protein heterodimerization activity; IEA:InterPro. DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro. DR CDD; cd00076; H4; 1. DR DisProt; DP01390; -. DR Gene3D; 1.10.20.10; Histone, subunit A; 1. DR IDEAL; IID50145; -. DR InterPro; IPR035425; CENP-T/H4_C. DR InterPro; IPR009072; Histone-fold. DR InterPro; IPR001951; Histone_H4. DR InterPro; IPR019809; Histone_H4_CS. DR InterPro; IPR004823; TAF_TATA-bd_Histone-like_dom. DR PANTHER; PTHR10484; HISTONE H4; 1. DR PANTHER; PTHR10484:SF0; HISTONE H4; 1. DR Pfam; PF15511; CENP-T_C; 1. DR PRINTS; PR00623; HISTONEH4. DR SMART; SM00417; H4; 1. DR SMART; SM00803; TAF; 1. DR SUPFAM; SSF47113; Histone-fold; 1. DR PROSITE; PS00047; HISTONE_H4; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Chromosome; Citrullination; DNA-binding; KW Hydroxylation; Isopeptide bond; Methylation; Nucleosome core; Nucleus; KW Phosphoprotein; Reference proteome; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..103 FT /note="Histone H4" FT /id="PRO_0000158376" FT DNA_BIND 17..21 FT REGION 1..20 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 2 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 4 FT /note="Asymmetric dimethylarginine; by PRMT1; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 4 FT /note="Citrulline; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 4 FT /note="Omega-N-methylarginine; by PRMT1; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 4 FT /note="Symmetric dimethylarginine; by PRMT5 and PRMT7; FT alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 6 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 6 FT /note="N6-acetyl-N6-methyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 6 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 6 FT /note="N6-butyryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 6 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 6 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 9 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 9 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 9 FT /note="N6-butyryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 9 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 9 FT /note="N6-propionyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 13 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 13 FT /note="N6-acetyl-N6-methyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 13 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 13 FT /note="N6-butyryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 13 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 13 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 13 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 17 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 17 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 17 FT /note="N6-butyryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 17 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 17 FT /note="N6-propionyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 21 FT /note="N6,N6,N6-trimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 21 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 21 FT /note="N6-methylated lysine" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 21 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 32 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 32 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 32 FT /note="N6-butyryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 32 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 32 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 32 FT /note="N6-propionyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 32 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 45 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 45 FT /note="N6-butyryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 45 FT /note="N6-propionyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 48 FT /note="Phosphoserine; by PAK2" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 52 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 60 FT /note="N6-(2-hydroxyisobutyryl)lysine" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 60 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 60 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 78 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 78 FT /note="N6-butyryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 78 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 78 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 78 FT /note="N6-propionyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 78 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 80 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 80 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 80 FT /note="N6-butyryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 80 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 80 FT /note="N6-propionyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 89 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 92 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 92 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 92 FT /note="N6-butyryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 92 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 92 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 92 FT /note="N6-propionyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 92 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT CROSSLNK 32 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in UFM1); alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT CROSSLNK 92 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin); alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT STRAND 6..12 FT /evidence="ECO:0007829|PDB:1KX5" FT STRAND 13..17 FT /evidence="ECO:0007829|PDB:1M1A" FT STRAND 19..21 FT /evidence="ECO:0007829|PDB:7ENN" FT HELIX 23..26 FT /evidence="ECO:0007829|PDB:2HUE" FT HELIX 27..29 FT /evidence="ECO:0007829|PDB:3C1B" FT HELIX 32..41 FT /evidence="ECO:0007829|PDB:2HUE" FT STRAND 45..47 FT /evidence="ECO:0007829|PDB:8PEO" FT HELIX 51..76 FT /evidence="ECO:0007829|PDB:2HUE" FT STRAND 80..82 FT /evidence="ECO:0007829|PDB:2HUE" FT HELIX 84..90 FT /evidence="ECO:0007829|PDB:2HUE" FT TURN 91..94 FT /evidence="ECO:0007829|PDB:2HUE" FT STRAND 96..100 FT /evidence="ECO:0007829|PDB:2HUE" SQ SEQUENCE 103 AA; 11367 MW; A9E5DFD3F8B97598 CRC64; MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK VFLENVIRDA VTYTEHAKRK TVTAMDVVYA LKRQGRTLYG FGG //