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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

Enzyme and pathway databases

ReactomeiR-BTA-3214815. HDACs deacetylate histones.
R-BTA-3214858. RMTs methylate histone arginines.
R-BTA-5689603. UCH proteinases.
R-BTA-5689880. Ub-specific processing proteases.
R-BTA-5689901. Metalloprotease DUBs.

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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved3 Publications
ChainiPRO_00000552412 – 130Histone H2A type 1Add BLAST129

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine2 Publications1
Modified residuei2Phosphoserine; by RPS6KA5By similarity1
Modified residuei4Citrulline; alternateBy similarity1
Modified residuei4Symmetric dimethylarginine; by PRMT5; alternateBy similarity1
Modified residuei6N6-acetyllysineBy similarity1
Cross-linki14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei37N6-crotonyllysineBy similarity1
Modified residuei105N5-methylglutamineBy similarity1
Modified residuei119N6-crotonyllysineBy similarity1
Modified residuei120N6-crotonyllysine; alternateBy similarity1
Cross-linki120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Modified residuei121Phosphothreonine; by VPRBPBy similarity1
Modified residuei126N6-crotonyllysineBy similarity1

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.

Expressioni

Gene expression databases

BgeeiENSBTAG00000024176.

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 interactor.
MINTiMINT-1519709.
STRINGi9913.ENSBTAP00000052261.

Structurei

3D structure databases

ProteinModelPortaliP0C0S9.
SMRiP0C0S9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H2A family.Curated

Phylogenomic databases

eggNOGiKOG1756. Eukaryota.
COG5262. LUCA.
GeneTreeiENSGT00760000118934.
ENSGT00860000133717.
HOGENOMiHOG000234652.
HOVERGENiHBG009342.
InParanoidiP0C0S9.
KOiK11251.
OMAiGRIVPRH.
OrthoDBiEOG091G0XGD.
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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP0C0S9. 1 interactor.
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.
GeneTreeiENSGT00760000118934.
ENSGT00860000133717.
HOGENOMiHOG000234652.
HOVERGENiHBG009342.
InParanoidiP0C0S9.
KOiK11251.
OMAiGRIVPRH.
OrthoDBiEOG091G0XGD.
TreeFamiTF300137.

Enzyme and pathway databases

ReactomeiR-BTA-3214815. HDACs deacetylate histones.
R-BTA-3214858. RMTs methylate histone arginines.
R-BTA-5689603. UCH proteinases.
R-BTA-5689880. Ub-specific processing proteases.
R-BTA-5689901. Metalloprotease DUBs.

Gene expression databases

BgeeiENSBTAG00000024176.

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...

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: November 30, 2016
This is version 115 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.