H4_ORENI
ID H4_ORENI Reviewed; 103 AA.
AC P62796; P02304; P02305;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Histone H4;
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Englander E., Moav B., Tabachnik M., Shuali Y., Graur D.;
RT "An unusual histone H4 gene from Tilapia nilotica exhibiting
RT characteristics of both a replication-dependent histone and a basal-
RT expression histone: evolutionary considerations.";
RL J. Evol. Biol. 6:129-137(1993).
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
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; X54078; CAA38015.1; -; Genomic_DNA.
DR RefSeq; XP_003451199.1; XM_003451151.4.
DR RefSeq; XP_003454720.1; XM_003454672.4.
DR RefSeq; XP_003458488.1; XM_003458440.4.
DR RefSeq; XP_003459140.1; XM_003459092.4.
DR RefSeq; XP_003459577.1; XM_003459529.4.
DR RefSeq; XP_003459580.1; XM_003459532.4.
DR RefSeq; XP_005455914.1; XM_005455857.3.
DR RefSeq; XP_005462225.1; XM_005462168.3.
DR RefSeq; XP_005465169.1; XM_005465112.3.
DR RefSeq; XP_005466235.1; XM_005466178.3.
DR RefSeq; XP_013129005.1; XM_013273551.2.
DR RefSeq; XP_013130408.1; XM_013274954.2.
DR RefSeq; XP_019206828.1; XM_019351283.1.
DR RefSeq; XP_019209876.1; XM_019354331.1.
DR AlphaFoldDB; P62796; -.
DR SMR; P62796; -.
DR STRING; 8128.ENSONIP00000026073; -.
DR Ensembl; ENSONIT00000026094; ENSONIP00000026073; ENSONIG00000020768.
DR GeneID; 100691120; -.
DR GeneID; 100693547; -.
DR GeneID; 100694299; -.
DR GeneID; 100694836; -.
DR GeneID; 100695624; -.
DR GeneID; 100700428; -.
DR GeneID; 100702755; -.
DR GeneID; 100702942; -.
DR GeneID; 100707512; -.
DR GeneID; 100711673; -.
DR GeneID; 100712429; -.
DR GeneID; 109198966; -.
DR KEGG; onl:100691120; -.
DR KEGG; onl:100693547; -.
DR KEGG; onl:100694299; -.
DR KEGG; onl:100694836; -.
DR KEGG; onl:100695624; -.
DR KEGG; onl:100700428; -.
DR KEGG; onl:100702755; -.
DR KEGG; onl:100702942; -.
DR KEGG; onl:100707512; -.
DR KEGG; onl:100711673; -.
DR KEGG; onl:100712429; -.
DR KEGG; onl:109198966; -.
DR eggNOG; KOG3467; Eukaryota.
DR GeneTree; ENSGT01050000244867; -.
DR HOGENOM; CLU_109117_2_3_1; -.
DR OMA; QKEHING; -.
DR OrthoDB; 1594208at2759; -.
DR Proteomes; UP000005207; Linkage group LG17.
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 Gene3D; 1.10.20.10; -; 1.
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 3: Inferred from homology;
KW Acetylation; Chromosome; Citrullination; DNA-binding; Hydroxylation;
KW Isopeptide bond; Methylation; Nucleosome core; Nucleus; Phosphoprotein;
KW 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_0000158339"
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-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"
SQ SEQUENCE 103 AA; 11367 MW; A9E5DFD3F8B97598 CRC64;
MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK
VFLENVIRDA VTYTEHAKRK TVTAMDVVYA LKRQGRTLYG FGG
