P62796 (H4_ORENI) Reviewed, UniProtKB/Swiss-Prot
Last modified May 29, 2013. Version 54. History...
Names and origin
|Protein names||Recommended name:|
|Organism||Oreochromis niloticus (Nile tilapia) (Tilapia nilotica) [Reference proteome]|
|Taxonomic identifier||8128 [NCBI]|
|Taxonomic lineage||Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Euteleostei › Neoteleostei › Acanthomorpha › Acanthopterygii › Percomorpha › Perciformes › Labroidei › Cichlidae › African cichlids › Pseudocrenilabrinae › Oreochromini › Oreochromis|
|Sequence length||103 AA.|
|Sequence processing||The displayed sequence is further processed into a mature form.|
|Protein existence||Inferred from homology|
General annotation (Comments)
Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.
Acetylation at Lys-6 (H4K5ac), Lys-9 (H4K8ac), Lys-13 (H4K12ac) and Lys-17 (H4K16ac) occurs in coding regions of the genome but not in heterochromatin By similarity.
Citrullination at Arg-4 (H4R3ci) by PADI4 impairs methylation By similarity.
Monomethylation and asymmetric dimethylation at Arg-4 (H4R3me1 and H4R3me2a, respectively) by PRMT1 favors acetylation at Lys-9 (H4K8ac) and Lys-13 (H4K12ac). Demethylation is performed by JMJD6. Symmetric dimethylation on Arg-4 (H4R3me2s) by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage By similarity.
Monomethylated, dimethylated or trimethylated at Lys-21 (H4K20me1, H4K20me2, H4K20me3). Monomethylation is performed by SET8. Trimethylation is performed by SUV420H1 and SUV420H2 and induces gene silencing By similarity.
Phosphorylated by pak2 at Ser-48 (H4S47ph). This phosphorylation increases the association of H3.3-H4 with the histone chaperone HIRA, thus promoting nucleosome assembly of H3.3-H4 and inhibiting nucleosome assembly of H3.1-H4 By similarity.
Ubiquitinated by the CUL4-DDB-RBX1 complex in response to ultraviolet irradiation. This may weaken the interaction between histones and DNA and facilitate DNA accessibility to repair proteins. Monoubiquitinated at Lys-92 of histone H4 (H4K91ub1) in response to DNA damage. The exact role of H4K91ub1 in DNA damage response is still unclear but it may function as a licensing signal for additional histone H4 post-translational modifications such as H4 Lys-21 methylation (H4K20me) By similarity.
Sumoylated, which is associated with transcriptional repression By similarity.
Belongs to the histone H4 family.
|Technical term||Complete proteome|
|Gene Ontology (GO)|
Inferred from electronic annotation. Source: InterPro
Inferred from electronic annotation. Source: UniProtKB-KWnucleus
Inferred from electronic annotation. Source: UniProtKB-SubCell
Inferred from electronic annotation. Source: UniProtKB-KW
|Complete GO annotation...|
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Initiator methionine||1||1||Removed By similarity|
|Chain||2 – 103||102||Histone H4||PRO_0000158339|
|DNA binding||17 – 21||5|
Amino acid modifications
|Modified residue||2||1||N-acetylserine By similarity|
|Modified residue||2||1||Phosphoserine By similarity|
|Modified residue||4||1||Asymmetric dimethylarginine; by PRMT1; alternate By similarity|
|Modified residue||4||1||Citrulline; alternate By similarity|
|Modified residue||4||1||Omega-N-methylarginine; by PRMT1; alternate By similarity|
|Modified residue||4||1||Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate By similarity|
|Modified residue||6||1||N6-acetyllysine By similarity|
|Modified residue||9||1||N6-acetyllysine By similarity|
|Modified residue||13||1||N6-acetyllysine By similarity|
|Modified residue||17||1||N6-acetyllysine By similarity|
|Modified residue||21||1||N6,N6,N6-trimethyllysine; alternate By similarity|
|Modified residue||21||1||N6,N6-dimethyllysine; alternate By similarity|
|Modified residue||21||1||N6-methyllysine; alternate By similarity|
|Modified residue||32||1||N6-acetyllysine By similarity|
|Modified residue||48||1||Phosphoserine; by PAK2 By similarity|
|Modified residue||52||1||Phosphotyrosine By similarity|
|Modified residue||60||1||N6-acetyllysine By similarity|
|Modified residue||80||1||N6-acetyllysine By similarity|
|Modified residue||89||1||Phosphotyrosine By similarity|
|Modified residue||92||1||N6-acetyllysine; alternate By similarity|
|Cross-link||92||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity|
|||"An unusual histone H4 gene from Tilapia nilotica exhibiting characteristics of both a replication-dependent histone and a basal-expression histone: evolutionary considerations."|
Englander E., Moav B., Tabachnik M., Shuali Y., Graur D.
J. Evol. Biol. 6:129-137(1993)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
|Accession||Primary (citable) accession number: P62796|
Secondary accession number(s): P02304, P02305
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Chordata Protein Annotation Program|
Index of protein domains and families