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Q6BRG3

- H2A2_DEBHA

UniProt

Q6BRG3 - H2A2_DEBHA

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Protein

Histone H2A.2

Gene

HTA2

Organism
Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

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.

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW

GO - Biological processi

  1. DNA repair Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2A.2
Gene namesi
Name:HTA2
Ordered Locus Names:DEHA2D16588g
OrganismiDebaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii)
Taxonomic identifieri284592 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeDebaryomyces
ProteomesiUP000000599: Chromosome D

Subcellular locationi

Nucleus By similarity. Chromosome By similarity

GO - Cellular componenti

  1. nucleosome Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 131130Histone H2A.2PRO_0000228729Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei5 – 51N6-acetyllysineBy similarity
Modified residuei7 – 71N6-acetyllysineBy similarity
Modified residuei105 – 1051N5-methylglutamineBy similarity
Modified residuei128 – 1281PhosphoserineBy similarity

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 MEC1/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 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 (By similarity).By similarity
Acetylated by ESA1 to form H2AK4ac and H2AK7ac.By similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

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

STRINGi4959.Q6BRG3.

Structurei

3D structure databases

ProteinModelPortaliQ6BRG3.
SMRiQ6BRG3. Positions 13-120.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi128 – 1292[ST]-Q motif

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

eggNOGiCOG5262.
InParanoidiQ6BRG3.
KOiK11251.
OMAiAGDIRFV.
OrthoDBiEOG7GN30N.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR002119. Histone_H2A.
[Graphical view]
PfamiPF00125. Histone. 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.

Q6BRG3 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSGGKGKAGS SEKASTSRSA KAGLTFPVGR VHRLLRKGNY AQRVGSGAPV
60 70 80 90 100
YLTSVLEYLA AEILELAGNA ARDNKKSRII PRHLQLAIRN DEELNKLLGH
110 120 130
VTIAQGGVLP NIHQSLLPAK KAKAGNASQE L
Length:131
Mass (Da):13,875
Last modified:January 23, 2007 - v3
Checksum:i3013C4FA8B6DA112
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR382136 Genomic DNA. Translation: CAG87378.1.
RefSeqiXP_459207.1. XM_459207.1.

Genome annotation databases

GeneIDi2901667.
KEGGidha:DEHA2D16588g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR382136 Genomic DNA. Translation: CAG87378.1 .
RefSeqi XP_459207.1. XM_459207.1.

3D structure databases

ProteinModelPortali Q6BRG3.
SMRi Q6BRG3. Positions 13-120.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 4959.Q6BRG3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 2901667.
KEGGi dha:DEHA2D16588g.

Phylogenomic databases

eggNOGi COG5262.
InParanoidi Q6BRG3.
KOi K11251.
OMAi AGDIRFV.
OrthoDBi EOG7GN30N.

Family and domain databases

Gene3Di 1.10.20.10. 1 hit.
InterProi IPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR002119. Histone_H2A.
[Graphical view ]
Pfami PF00125. Histone. 1 hit.
[Graphical view ]
PRINTSi PR00620. HISTONEH2A.
SMARTi SM00414. H2A. 1 hit.
[Graphical view ]
SUPFAMi SSF47113. SSF47113. 1 hit.
PROSITEi PS00046. HISTONE_H2A. 1 hit.
[Graphical view ]
ProtoNeti Search...

Entry informationi

Entry nameiH2A2_DEBHA
AccessioniPrimary (citable) accession number: Q6BRG3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 72 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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-7; H2AS128ph = phosphorylated Ser-128.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3