Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Histone H2A type 1

Gene
N/A
Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2A type 1
Alternative name(s):
H2A.1b
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 23

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved3 Publications
Chaini2 – 130129Histone H2A type 1PRO_0000055241Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei2 – 21Phosphoserine; by RPS6KA5By similarity
Modified residuei4 – 41Citrulline; alternateBy similarity
Modified residuei4 – 41Symmetric dimethylarginine; by PRMT5; alternateBy similarity
Modified residuei6 – 61N6-acetyllysineBy similarity
Cross-linki14 – 14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki16 – 16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei37 – 371N6-crotonyllysineBy similarity
Modified residuei105 – 1051N5-methylglutamineBy similarity
Modified residuei119 – 1191N6-crotonyllysineBy similarity
Modified residuei120 – 1201N6-crotonyllysine; alternateBy similarity
Cross-linki120 – 120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Modified residuei121 – 1211Phosphothreonine; by VPRBPBy similarity
Modified residuei126 – 1261N6-crotonyllysineBy similarity

Post-translational modificationi

Deiminated on Arg-4 in granulocytes upon calcium entry.By similarity
Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM27 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 (H3K27me). H2AK119Ub 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. Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro. H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events.By similarity2 Publications
Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121 (H2AT120ph) by VPRBP is present in the regulatory region of many tumor suppresor genes and down-regulates their transcription.By similarity
Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage.By similarity
Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex.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

Keywords - PTMi

Acetylation, Citrullination, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP0C0S9.
PeptideAtlasiP0C0S9.
PRIDEiP0C0S9.

PTM databases

iPTMnetiP0C0S9.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

IntActiP0C0S9. 1 interaction.
MINTiMINT-1519709.
STRINGi9913.ENSBTAP00000052261.

Structurei

3D structure databases

ProteinModelPortaliP0C0S9.
SMRiP0C0S9. Positions 14-119.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H2A family.Curated

Phylogenomic databases

eggNOGiKOG1756. Eukaryota.
COG5262. LUCA.
GeneTreeiENSGT00710000106735.
ENSGT00760000118934.
ENSGT00840000129729.
HOGENOMiHOG000234652.
HOVERGENiHBG009342.
InParanoidiP0C0S9.
KOiK11251.
OMAiTETHHKA.
OrthoDBiEOG7M0NTR.
TreeFamiTF300137.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR002119. Histone_H2A.
IPR007125. Histone_H2A/H2B/H3.
IPR032454. Histone_H2A_C.
IPR032458. Histone_H2A_CS.
[Graphical view]
PfamiPF00125. Histone. 1 hit.
PF16211. Histone_H2A_C. 1 hit.
[Graphical view]
PRINTSiPR00620. HISTONEH2A.
SMARTiSM00414. H2A. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00046. HISTONE_H2A. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0C0S9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGRGKQGGK ARAKAKTRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV
60 70 80 90 100
YLAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGK
110 120 130
VTIAQGGVLP NIQAVLLPKK TESHHKAKGK
Length:130
Mass (Da):14,091
Last modified:January 23, 2007 - v2
Checksum:i48DD539793FE8256
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC142109 mRNA. Translation: AAI42110.1.
PIRiA91216. HSBO2A.
RefSeqiNP_001092190.1. NM_001098720.2.
XP_002697551.1. XM_002697505.4.
XP_005196697.1. XM_005196640.2.
XP_005223785.1. XM_005223728.2.
XP_010816763.1. XM_010818461.2.
XP_010816815.1. XM_010818513.2.
XP_010823700.1. XM_010825398.2.
XP_010823710.1. XM_010825408.2.
XP_876240.1. XM_871147.5.
UniGeneiBt.88544.

Genome annotation databases

EnsembliENSBTAT00000014123; ENSBTAP00000014123; ENSBTAG00000039492.
ENSBTAT00000033365; ENSBTAP00000033278; ENSBTAG00000024176.
ENSBTAT00000033373; ENSBTAP00000033286; ENSBTAG00000024183.
ENSBTAT00000033377; ENSBTAP00000033290; ENSBTAG00000024187.
ENSBTAT00000045035; ENSBTAP00000042461; ENSBTAG00000031758.
ENSBTAT00000045049; ENSBTAP00000042470; ENSBTAG00000031771.
ENSBTAT00000057026; ENSBTAP00000052261; ENSBTAG00000040378.
GeneIDi104968446.
104975683.
529277.
616790.
618824.
KEGGibta:104968446.
bta:104975683.
bta:529277.
bta:616790.
bta:618824.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC142109 mRNA. Translation: AAI42110.1.
PIRiA91216. HSBO2A.
RefSeqiNP_001092190.1. NM_001098720.2.
XP_002697551.1. XM_002697505.4.
XP_005196697.1. XM_005196640.2.
XP_005223785.1. XM_005223728.2.
XP_010816763.1. XM_010818461.2.
XP_010816815.1. XM_010818513.2.
XP_010823700.1. XM_010825398.2.
XP_010823710.1. XM_010825408.2.
XP_876240.1. XM_871147.5.
UniGeneiBt.88544.

3D structure databases

ProteinModelPortaliP0C0S9.
SMRiP0C0S9. Positions 14-119.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP0C0S9. 1 interaction.
MINTiMINT-1519709.
STRINGi9913.ENSBTAP00000052261.

PTM databases

iPTMnetiP0C0S9.

Proteomic databases

PaxDbiP0C0S9.
PeptideAtlasiP0C0S9.
PRIDEiP0C0S9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000014123; ENSBTAP00000014123; ENSBTAG00000039492.
ENSBTAT00000033365; ENSBTAP00000033278; ENSBTAG00000024176.
ENSBTAT00000033373; ENSBTAP00000033286; ENSBTAG00000024183.
ENSBTAT00000033377; ENSBTAP00000033290; ENSBTAG00000024187.
ENSBTAT00000045035; ENSBTAP00000042461; ENSBTAG00000031758.
ENSBTAT00000045049; ENSBTAP00000042470; ENSBTAG00000031771.
ENSBTAT00000057026; ENSBTAP00000052261; ENSBTAG00000040378.
GeneIDi104968446.
104975683.
529277.
616790.
618824.
KEGGibta:104968446.
bta:104975683.
bta:529277.
bta:616790.
bta:618824.

Organism-specific databases

CTDi8336.
8969.

Phylogenomic databases

eggNOGiKOG1756. Eukaryota.
COG5262. LUCA.
GeneTreeiENSGT00710000106735.
ENSGT00760000118934.
ENSGT00840000129729.
HOGENOMiHOG000234652.
HOVERGENiHBG009342.
InParanoidiP0C0S9.
KOiK11251.
OMAiTETHHKA.
OrthoDBiEOG7M0NTR.
TreeFamiTF300137.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR002119. Histone_H2A.
IPR007125. Histone_H2A/H2B/H3.
IPR032454. Histone_H2A_C.
IPR032458. Histone_H2A_CS.
[Graphical view]
PfamiPF00125. Histone. 1 hit.
PF16211. Histone_H2A_C. 1 hit.
[Graphical view]
PRINTSiPR00620. HISTONEH2A.
SMARTiSM00414. H2A. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00046. HISTONE_H2A. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: PROTEIN SEQUENCE OF 2-130, ACETYLATION AT SER-2.
    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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION.

Entry informationi

Entry nameiH2A1_BOVIN
AccessioniPrimary (citable) accession number: P0C0S9
Secondary accession number(s): A5PJH1, P02261
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Describes the first characterization of a ubiquitinated protein (PubMed:265581).

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.