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Protein

Histone H2A

Gene

hh2a

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed-Annotation score: -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.

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-6; H2AK7ac = acetylated Lys-10; H2AS128ph = phosphorylated Ser-131.Curated

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDNA-binding
Biological processDNA damage, DNA repair

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2A
Gene namesi
Name:hh2a
Synonyms:hta-1
ORF Names:NCU02437
OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Taxonomic identifieri367110 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
Proteomesi
  • UP000001805 Componenti: Chromosome 7, Linkage Group VII

Organism-specific databases

EuPathDBiFungiDB:NCU02437

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000553232 – 134Histone H2AAdd BLAST133

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei6N6-acetyllysineBy similarity1
Modified residuei10N6-acetyllysineBy similarity1
Modified residuei107N5-methylglutamineBy similarity1
Modified residuei131PhosphoserineBy similarity1

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 mec-1/ATR and tel-1/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 esa-1 to form H2AK4ac and H2AK7ac.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei121Not ubiquitinatedCurated1

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

PRIDEiQ8X132

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.

GO - Molecular functioni

Protein-protein interaction databases

DIPiDIP-59935N
IntActiQ8X132, 1 interactor

Structurei

3D structure databases

ProteinModelPortaliQ8X132
SMRiQ8X132
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi131 – 132[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
InParanoidiQ8X132
KOiK11251
OMAiVMPNVQA
OrthoDBiEOG092C5QJX

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.

Q8X132-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTGGGKSGGK ASGSKNAQSR SSKAGLAFPV GRVHRLLRKG NYAQRVGAGA
60 70 80 90 100
PVYLAAVLEY LAAEILELAG NAARDNKKTR IIPRHLQLAI RNDEELNKLL
110 120 130
GHVTIAQGGV LPNIHQNLLP KKTGKTGKNA SQEL
Length:134
Mass (Da):14,154
Last modified:January 23, 2007 - v3
Checksum:iEE093088EC4850F8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY062171 Genomic DNA Translation: AAL38970.1
CM002242 Genomic DNA Translation: EAA30206.1
RefSeqiXP_959442.1, XM_954349.3

Genome annotation databases

EnsemblFungiiEAA30206; EAA30206; NCU02437
GeneIDi3875589
KEGGincr:NCU02437

Similar proteinsi

Entry informationi

Entry nameiH2A_NEUCR
AccessioniPrimary (citable) accession number: Q8X132
Secondary accession number(s): Q7S3Y4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 111 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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