Reviewed,
UniProtKB/Swiss-Prot P0C0S9 (H2A1_BOVIN)
Last modified
November 24, 2009.
Version 50.
History...
Clusters with 100%,
90%,
50% identity |
 Documents (1) |
 Third-party data |
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Names and origin
| Protein names | Recommended name: Histone H2A type 1 Alternative name(s): H2A.1b |
| Organism | Bos taurus (Bovine) |
| Taxonomic identifier | 9913 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Protein attributes
| Sequence length | 130 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | 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. |
| Subunit structure | 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. |
| Subcellular location | |
| Post-translational modification | The chromatin-associated form is phosphorylated on Thr-121 during mitosis By similarity. Monoubiquitination of Lys-120 by RING1 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3. Monoubiquitination of Lys-120 by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Monoubiquitination and ionizing radiation-induced 'Lys-63'-linked ubiquitination are distinct events By similarity. Phosphorylation on Ser-2 is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1 By similarity. Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage By similarity. |
| Miscellaneous | Ref.8 describes the first characterization of an ubiquitinated protein. |
| Sequence similarities | Belongs to the histone H2A family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Chromosomal protein Nucleosome core Nucleus |
| Ligand | DNA-binding |
| PTM | Acetylation Citrullination Isopeptide bond Methylation Phosphoprotein Ubl conjugation |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | nucleosome assembly Inferred from electronic annotation. Source: InterPro |
| Cellular component | nucleosome Inferred from electronic annotation. Source: UniProtKB-KW nucleusInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | DNA binding Inferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.2 Ref.3 | ||||||
| Chain | 2 – 130 | 129 | Histone H2A type 1 | PRO_0000055241 | |||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylserine Ref.8 | ||||||
| Modified residue | 2 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 4 | 1 | Citrulline; alternate By similarity | ||||||
| Modified residue | 4 | 1 | Symmetric dimethylarginine; alternate By similarity | ||||||
| Modified residue | 6 | 1 | N6-acetyllysine | ||||||
| Modified residue | 121 | 1 | Phosphothreonine By similarity | ||||||
| Cross-link | 120 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.8 | |||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | NIH - Mammalian Gene Collection (MGC) project Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Thymus. |
| [2] | "Covalent structure of calf-thymus ALK-histone." Sautiere P., Tyrou D., Laine B., Mizon J., Ruffin P., Biserte G. Eur. J. Biochem. 41:563-576(1974) [PubMed: 4856314] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-130. Tissue: Thymus. |
| [3] | "Homology of the amino terminal sequences of the AL and GAR calf thymus histones." Olson M.O.J., Sugano N., Yeoman L.C., Johnson B.R., Jordan J.J., Taylor C.W., Starbuck W.C., Busch H. Physiol. Chem. Phys. 4:10-16(1972) [PubMed: 4667695] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-30. Tissue: Thymus. |
| [4] | "Amino acid sequence of the center of the arginine-lysine-rich histone from calf thymus. The total sequence." Yeoman L.C., Olson M.O.J., Sugano N., Jordan J.J., Taylor C.W., Starbuck W.C., Busch H. J. Biol. Chem. 247:6018-6023(1972) [PubMed: 4568599] [Abstract] Cited for: PROTEIN SEQUENCE OF 31-82. Tissue: Thymus. |
| [5] | "Amino acid sequence of the COOH-terminal portion of the arginine-lysine-rich histone of calf thymus." Sugano N., Olson M.O.J., Yeoman L.C., Johnson B.R., Taylor C.W., Starbuck W.C., Busch H. J. Biol. Chem. 247:3589-3591(1972) [PubMed: 4555425] [Abstract] Cited for: PROTEIN SEQUENCE OF 83-130. Tissue: Thymus. |
| [6] | "Calf thymus histone H2A. Purification and tryptic peptides." Hayashi H., Iwai K. J. Biochem. 80:681-692(1976) [PubMed: 1010839] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE. |
| [7] | "Complete amino acid sequence analysis of a peptide isolated from the thymus that enhances release of growth hormone and prolactin." Badamchian M., Spangelo B.L., Damavandy T., McLeod R.M., Goldstein A.L. Endocrinology 128:1580-1588(1991) [PubMed: 1999173] [Abstract] Cited for: PROTEIN SEQUENCE OF 87-121. |
| [8] | "Isopeptide linkage between nonhistone and histone 2A polypeptides of chromosomal conjugate-protein A24." Goldknopf I.L., Busch H. Proc. Natl. Acad. Sci. U.S.A. 74:864-868(1977) [PubMed: 265581] [Abstract] Cited for: PROTEIN SEQUENCE OF 124-130, ACETYLATION AT SER-2, UBIQUITINATION AT LYS-120. |
| [9] | "Ubiquitinated histone H2B is preferentially located in transcriptionally active chromatin." Nickel B.E., Allis C.D., Davie J.R. Biochemistry 28:958-963(1989) [PubMed: 2713375] [Abstract] Cited for: UBIQUITINATION. |
Cross-references
Entry information
| Entry name | H2A1_BOVIN | ||||||||
| Accession | Primary (citable) accession number: P0C0S9 Secondary accession number(s): A5PJH1, P02261 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
