H4_XENLA
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 03-AUG-2022, entry version 153.
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).
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: 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}.
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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; 7SWY; EM; 2.60 A; B/F=2-103.
DR PDB; 7TN2; EM; 2.30 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; 7SWY; -.
DR PDBsum; 7TN2; -.
DR AlphaFoldDB; P62799; -.
DR SASBDB; P62799; -.
DR SMR; P62799; -.
DR BioGRID; 104647; 16.
DR DIP; DIP-37429N; -.
DR IntAct; P62799; 14.
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 CTD; 447787; -.
DR Xenbase; XB-GENE-6493984; h4c1.L.
DR OrthoDB; 1564596at2759; -.
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 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 GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR CDD; cd00076; H4; 1.
DR DisProt; DP01390; -.
DR Gene3D; 1.10.20.10; -; 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 Pfam; PF15511; CENP-T_C; 1.
DR PRINTS; PR00623; HISTONEH4.
DR SMART; SM00417; H4; 1.
DR SMART; SM00803; TAF; 1.
DR SUPFAM; SSF47113; SSF47113; 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-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-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:5ONW"
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
