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Q0CBD2

- H2A_ASPTN

UniProt

Q0CBD2 - H2A_ASPTN

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Protein
Histone H2A
Gene
hta1, ATEG_09002
Organism
Aspergillus terreus (strain NIH 2624 / FGSC A1156)
Status
Reviewed - Annotation score: 4 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei120 – 1201Not ubiquitinated Inferred

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW

GO - Biological processi

  1. DNA repair Source: UniProtKB-KW
  2. nucleosome assembly Source: InterPro
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2A
Gene namesi
Name:hta1
ORF Names:ATEG_09002
OrganismiAspergillus terreus (strain NIH 2624 / FGSC A1156)
Taxonomic identifieri341663 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000007963: Unassembled WGS sequence

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 131130Histone H2A
PRO_0000297731Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51N6-acetyllysine By similarity
Modified residuei9 – 91N6-acetyllysine By similarity
Modified residuei106 – 1061N5-methylglutamine By similarity
Modified residuei128 – 1281Phosphoserine By 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.
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

STRINGi33178.CADATEAP00007013.

Structurei

3D structure databases

ProteinModelPortaliQ0CBD2.
SMRiQ0CBD2. Positions 17-125.

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.

Phylogenomic databases

eggNOGiCOG5262.
HOGENOMiHOG000234652.
OMAiNKTESHH.
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.

Q0CBD2-1 [UniParc]FASTAAdd to Basket

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MTGGKSGGKA SGSKNAQSRS SKAGLAFPVG RVHRLLRKGN YAQRVGAGAP    50
VYLAAVLEYL AAEILELAGN AARDNKKTRI IPRHLQLAIR NDEELNKLLG 100
HVTIAQGGVL PNIHQNLLPK KTPKAKGSQE L 131
Length:131
Mass (Da):13,922
Last modified:October 17, 2006 - v1
Checksum:i13812974A5E54023
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CH476606 Genomic DNA. Translation: EAU31134.1.
RefSeqiXP_001217588.1. XM_001217587.1.

Genome annotation databases

EnsemblFungiiCADATEAT00007013; CADATEAP00007013; CADATEAG00007013.
GeneIDi4323163.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CH476606 Genomic DNA. Translation: EAU31134.1 .
RefSeqi XP_001217588.1. XM_001217587.1.

3D structure databases

ProteinModelPortali Q0CBD2.
SMRi Q0CBD2. Positions 17-125.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 33178.CADATEAP00007013.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADATEAT00007013 ; CADATEAP00007013 ; CADATEAG00007013 .
GeneIDi 4323163.

Phylogenomic databases

eggNOGi COG5262.
HOGENOMi HOG000234652.
OMAi NKTESHH.
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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NIH 2624 / FGSC A1156.

Entry informationi

Entry nameiH2A_ASPTN
AccessioniPrimary (citable) accession number: Q0CBD2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: October 17, 2006
Last modified: May 14, 2014
This is version 41 of the entry and version 1 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 Inferred.

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.

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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