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Protein

Histone H2A-beta

Gene

hta2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. 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.1 Publication

Miscellaneous

In contrast to vertebrates and insects, its C-terminus is not monoubiquitinated.Curated

Caution

To ensure consistency between histone entries, we follow the 'Brno' nomenclature for histone modifications, with positions referring to those used in the literature for the 'closest' model organism. Due to slight variations in histone sequences between organisms and to the presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the actual positions of modified amino acids in the sequence generally differ. In this entry the following conventions are used: H2AK4ac = acetylated Lys-5; H2AK7ac = acetylated Lys-9; H2AS128ph = phosphorylated Ser-128.Curated

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDNA-binding
Biological processDNA damage, DNA repair

Enzyme and pathway databases

ReactomeiR-SPO-2299718 Condensation of Prophase Chromosomes
R-SPO-2559580 Oxidative Stress Induced Senescence
R-SPO-3214815 HDACs deacetylate histones
R-SPO-3214858 RMTs methylate histone arginines
R-SPO-427359 SIRT1 negatively regulates rRNA expression
R-SPO-5578749 Transcriptional regulation by small RNAs
R-SPO-5689880 Ub-specific processing proteases
R-SPO-5693565 Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2A-beta
Alternative name(s):
H2A.2
Gene namesi
Name:hta2
ORF Names:SPAC19G12.06c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC19G12.06c
PomBaseiSPAC19G12.06c hta2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi128S → A: Causes hypersensitivity to DNA-damage-inducing agents and impairs recruitment of crb2 to DSB sites. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000553252 – 131Histone H2A-betaAdd BLAST130

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei5N6-acetyllysineBy similarity1
Modified residuei9N6-acetyllysineBy similarity1
Modified residuei106N5-methylglutamine1 Publication1
Modified residuei128Phosphoserine1 Publication1

Post-translational modificationi

Phosphorylated to form H2AS128ph (gamma-H2A) in response to DNA double-strand breaks (DSBs) generated by exogenous genotoxic agents and by stalled replication forks. Phosphorylation is dependent on the DNA damage checkpoint kinases rad3/ATR and tel1/ATM, spreads on either side of a detected DSB site and may mark the surrounding chromatin for recruitment of proteins required for DNA damage signaling and repair. Gamma-H2A is required for recruiting crb2, a modulator of DNA damage checkpoint signaling, to DSB sites. Gamma-H2A is removed from the DNA prior to the strand invasion-primer extension step of the repair process and subsequently dephosphorylated. Dephosphorylation is necessary for efficient recovery from the DNA damage checkpoint.1 Publication
Acetylated by esa1 to form H2AK4ac and H2AK7ac.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei120Not ubiquitinatedCurated1

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

PaxDbiP04910
PRIDEiP04910

PTM databases

iPTMnetiP04910
SwissPalmiP04910

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.

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi278699, 20 interactors
DIPiDIP-59186N
IntActiP04910, 2 interactors
STRINGi4896.SPAC19G12.06c.1

Structurei

3D structure databases

ProteinModelPortaliP04910
SMRiP04910
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi128 – 129[ST]-Q motif2

Domaini

The [ST]-Q motif constitutes a recognition sequence for kinases from the PI3/PI4-kinase family.

Sequence similaritiesi

Belongs to the histone H2A family.Curated

Phylogenomic databases

HOGENOMiHOG000234652
InParanoidiP04910
KOiK11251
OMAiMPNIHQT
OrthoDBiEOG092C5QJX
PhylomeDBiP04910

Family and domain databases

CDDicd00074 H2A, 1 hit
Gene3Di1.10.20.10, 1 hit
InterProiView protein in InterPro
IPR009072 Histone-fold
IPR002119 Histone_H2A
IPR007125 Histone_H2A/H2B/H3
IPR032454 Histone_H2A_C
IPR032458 Histone_H2A_CS
PfamiView protein in Pfam
PF00125 Histone, 1 hit
PF16211 Histone_H2A_C, 1 hit
PRINTSiPR00620 HISTONEH2A
SMARTiView protein in SMART
SM00414 H2A, 1 hit
SUPFAMiSSF47113 SSF47113, 1 hit
PROSITEiView protein in PROSITE
PS00046 HISTONE_H2A, 1 hit

Sequencei

Sequence statusi: Complete.

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

P04910-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSGGKSGGKA AVAKSAQSRS AKAGLAFPVG RVHRLLRKGN YAQRVGAGAP
60 70 80 90 100
VYLAAVLEYL AAEILELAGN AARDNKKTRI IPRHLQLAIR NDEELNKLLG
110 120 130
HVTIAQGGVV PNINAHLLPK QSGKGKPSQE L
Length:131
Mass (Da):13,776
Last modified:January 23, 2007 - v2
Checksum:i44ECF1A2AE992A04
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11500 Genomic DNA Translation: AAA35310.1
X05221 Genomic DNA Translation: CAA28849.1
CU329670 Genomic DNA Translation: CAB10117.1
PIRiC27399 HSZPA3
RefSeqiNP_594421.1, NM_001019850.2

Genome annotation databases

EnsemblFungiiSPAC19G12.06c.1; SPAC19G12.06c.1:pep; SPAC19G12.06c
GeneIDi2542226
KEGGispo:SPAC19G12.06c

Similar proteinsi

Entry informationi

Entry nameiH2A2_SCHPO
AccessioniPrimary (citable) accession number: P04910
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: June 20, 2018
This is version 146 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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