Histone H2A type 1 - Bos taurus (Bovine)

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P0C0S9 (H2A1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 67. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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	Nucleus. Chromosome.
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. Ref.8 Ref.9 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	Chromosome Nucleosome core Nucleus
Ligand	DNA-binding
PTM	Acetylation Citrullination Isopeptide bond Methylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	nucleosome assembly Inferred from electronic annotation. Source: InterPro
Cellular component	nucleosome Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred 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

Removed Ref.2 Ref.3

Chain

2 – 130

129

Histone H2A type 1

PRO_0000055241

Amino acid modifications

Modified residue

N-acetylserine Ref.8

Modified residue

Phosphoserine; by RPS6KA5 By similarity

Modified residue

Citrulline; alternate By similarity

Modified residue

Symmetric dimethylarginine; alternate By similarity

Modified residue

N6-acetyllysine

Modified residue

121

Phosphothreonine By similarity

Cross-link

120

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.8

Sequences

Sequence

Length

Mass (Da)

Tools

P0C0S9 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 48DD539793FE8256
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FASTA

130

14,091

        10         20         30         40         50         60 
MSGRGKQGGK ARAKAKTRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV YLAAVLEYLT 

        70         80         90        100        110        120 
AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGK VTIAQGGVLP NIQAVLLPKK 

       130 
TESHHKAKGK

« Hide

References

	« Hide 'large scale' referencesShow '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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC142109 mRNA. Translation: AAI42110.1.
IPI	IPI00715438.
PIR	HSBO2A. A91216.
RefSeq	NP_001092190.1. NM_001098720.1. XP_001250731.1. XM_001250730.3. XP_002697508.1. XM_002697462.1. XP_002697512.1. XM_002697466.1. XP_002697545.1. XM_002697499.1. XP_002697551.1. XM_002697505.1. XP_002697562.1. XM_002697516.1. XP_002702930.1. XM_002702884.1. XP_607721.2. XM_607721.5. XP_870241.2. XM_865148.4. XP_873767.1. XM_868674.1. XP_876240.1. XM_871147.2.
UniGene	Bt.88544.
3D structure databases
ProteinModelPortal	P0C0S9.
SMR	P0C0S9. Positions 14-119.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-1519709.
Proteomic databases
PRIDE	P0C0S9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSBTAT00000014123; ENSBTAP00000014123; ENSBTAG00000039492. ENSBTAT00000033365; ENSBTAP00000033278; ENSBTAG00000024176. ENSBTAT00000033373; ENSBTAP00000033286; ENSBTAG00000024183. ENSBTAT00000033377; ENSBTAP00000033290; ENSBTAG00000024187. ENSBTAT00000045035; ENSBTAP00000042461; ENSBTAG00000031758. ENSBTAT00000045049; ENSBTAP00000042470; ENSBTAG00000031771. ENSBTAT00000055068; ENSBTAP00000048654; ENSBTAG00000038515. ENSBTAT00000057026; ENSBTAP00000052261; ENSBTAG00000040378.
GeneID	100294773. 529277. 613926. 616611. 616790. 618824. 786163.
KEGG	bta:100294773. bta:529277. bta:613926. bta:616611. bta:616790. bta:618824. bta:786163.
Organism-specific databases
CTD	8969.
Phylogenomic databases
eggNOG	maNOG19405.
GeneTree	ENSGT00600000084241.
HOVERGEN	HBG009342.
InParanoid	P0C0S9.
OMA	GVAGRAY.
OrthoDB	EOG4CC42V. EOG4TXBTD.
PhylomeDB	P0C0S9.
Family and domain databases
InterPro	IPR009072. Histone-fold. IPR007125. Histone_core_D. IPR002119. Histone_H2A. [Graphical view]
Gene3D	G3DSA:1.10.20.10. Histone-fold. 1 hit.
KO	K11251.
Pfam	PF00125. Histone. 1 hit. [Graphical view]
PRINTS	PR00620. HISTONEH2A.
SMART	SM00414. H2A. 1 hit. [Graphical view]
SUPFAM	SSF47113. Histone-fold. 1 hit.
PROSITE	PS00046. HISTONE_H2A. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

H2A1_BOVIN

Accession

Primary (citable) accession number: P0C0S9
Secondary accession number(s): A5PJH1, P02261

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 67 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents