P62803 (H4_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified April 16, 2014. Version 98. History...
Names and origin
|Protein names||Recommended name:|
|Organism||Bos taurus (Bovine) [Reference proteome]|
|Taxonomic identifier||9913 [NCBI]|
|Taxonomic lineage||Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos|
|Sequence length||103 AA.|
|Sequence processing||The displayed sequence is further processed into a mature form.|
|Protein existence||Evidence at protein level|
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. Ref.3
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 By similarity. Symmetric dimethylation on Arg-4 (H4R3me2s) by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage By similarity. Ref.3
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. Ref.3
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.
Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes By similarity.
Belongs to the histone H4 family.
|Technical term||Complete proteome|
Direct protein sequencing
|Gene Ontology (GO)|
|Biological_process||negative regulation of megakaryocyte differentiation|
Inferred from electronic annotation. Source: Ensemblnucleosome assembly
Inferred from electronic annotation. Source: InterPro
Inferred from electronic annotation. Source: Ensemblnucleolus
Inferred from electronic annotation. Source: Ensemblnucleoplasm
Traceable author statement. Source: Reactomenucleosome
Inferred from electronic annotation. Source: UniProtKB-KW
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 Ref.3 Ref.4|
|Chain||2 – 103||102||Histone H4||PRO_0000158289|
|DNA binding||17 – 21||5|
Amino acid modifications
|Modified residue||2||1||N-acetylserine Ref.3|
|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; alternate By similarity|
|Modified residue||6||1||N6-crotonyl-L-lysine; alternate By similarity|
|Modified residue||9||1||N6-acetyllysine; alternate By similarity|
|Modified residue||9||1||N6-crotonyl-L-lysine; alternate By similarity|
|Modified residue||13||1||N6-acetyllysine; alternate By similarity|
|Modified residue||13||1||N6-crotonyl-L-lysine; alternate By similarity|
|Modified residue||17||1||N6-acetyllysine; alternate Ref.3|
|Modified residue||17||1||N6-crotonyl-L-lysine; alternate By similarity|
|Modified residue||21||1||N6,N6,N6-trimethyllysine; alternate By similarity|
|Modified residue||21||1||N6,N6-dimethyllysine; alternate Ref.3|
|Modified residue||21||1||N6-methyllysine; alternate Ref.3|
|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||89||1||Phosphotyrosine By similarity|
|Modified residue||92||1||N6-acetyllysine; alternate By similarity|
|Modified residue||92||1||N6-succinyllysine; alternate By similarity|
|Cross-link||92||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity|
|Sequence conflict||55||1||T → A in AAI42000. Ref.2|
|||"Poly A-containing histone H4 mRNA variant (H4-v.1): isolation and sequence determination from bovine adrenal medulla."|
Gendron N., Dumont M., Gagne M.-F., Lemaire S.
Biochim. Biophys. Acta 1396:32-38(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (H4-V.1).
Tissue: Adrenal medulla.
|||NIH - Mammalian Gene Collection (MGC) project|
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Crossbred X Angus and Hereford.
Tissue: Hypothalamus, Ileum and Thymus.
|||"Structure of the glycine-rich, arginine-rich histone of the Novikoff hepatoma."|
Wilson R.K., Starbuck W.C., Taylor C.W., Jordan J.J., Busch H.
Cancer Res. 30:2942-2951(1970) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-103, ACETYLATION AT SER-2 AND LYS-17, METHYLATION AT LYS-21.
|||"Structural analysis of the glycine-rich, arginine-rich histone. 3. Sequence of the amino-terminal half of the molecule containing the modified lysine residues and the total sequence."|
Ogawa Y., Quagliarotti G., Jordan J.J., Taylor C.W., Starbuck W.C., Busch H.
J. Biol. Chem. 244:4387-4392(1969) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-50.
|||"Structural analysis of the glycine-rich, arginine-rich histone. II. Sequence of the half of the molecule containing the aromatic amino acids."|
Quagliarotti G., Ogawa Y., Taylor C.W., Sautiere P., Jordan J., Starbuck W.C., Busch H.
J. Biol. Chem. 244:1796-1802(1969) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 51-103.
|Accession||Primary (citable) accession number: P62803|
Secondary accession number(s): A5PJ80 P02305
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Chordata Protein Annotation Program|
Index of protein domains and families