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Q0U1A1

- H2A_PHANO

UniProt

Q0U1A1 - H2A_PHANO

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Protein

Histone H2A

Gene
HTA1, SNOG_14611
Organism
Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume blotch fungus) (Septoria nodorum)
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
Sitei121 – 1211Not 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:SNOG_14611
OrganismiPhaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume blotch fungus) (Septoria nodorum)
Taxonomic identifieri321614 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesPleosporomycetidaePleosporalesPleosporineaePhaeosphaeriaceaeParastagonospora
ProteomesiUP000001055: 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 – 134133Histone H2APRO_0000297737Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51N6-acetyllysine By similarity
Modified residuei9 – 91N6-acetyllysine By similarity
Modified residuei107 – 1071N5-methylglutamine By similarity
Modified residuei131 – 1311Phosphoserine 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.

Structurei

3D structure databases

ProteinModelPortaliQ0U1A1.
SMRiQ0U1A1. Positions 18-125.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi131 – 1322[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

KOiK11251.
OMAiTKNAQSR.
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.

Q0U1A1-1 [UniParc]FASTAAdd to Basket

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MTGGKSGGKA SGSKSSAQSR SSKAGLAFPV GRVHRLLRKG NYAQRVGAGA    50
PVYLAAVLEY LAAEILELAG NAARDNKKTR IIPRHLQLAI RNDEELNKLL 100
GHVTIAQGGV LPNIHQNLLP KKTAKPGKGP SQEL 134
Length:134
Mass (Da):14,136
Last modified:September 5, 2006 - v1
Checksum:i35B522A89B04EDFA
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CH445356 Genomic DNA. Translation: EAT78151.1.
RefSeqiXP_001804793.1. XM_001804741.1.

Genome annotation databases

EnsemblFungiiSNOT_14611; SNOT_14611; SNOG_14611.
GeneIDi5981718.
KEGGipno:SNOG_14611.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CH445356 Genomic DNA. Translation: EAT78151.1 .
RefSeqi XP_001804793.1. XM_001804741.1.

3D structure databases

ProteinModelPortali Q0U1A1.
SMRi Q0U1A1. Positions 18-125.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii SNOT_14611 ; SNOT_14611 ; SNOG_14611 .
GeneIDi 5981718.
KEGGi pno:SNOG_14611.

Phylogenomic databases

KOi K11251.
OMAi TKNAQSR.
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. "Dothideomycete-plant interactions illuminated by genome sequencing and EST analysis of the wheat pathogen Stagonospora nodorum."
    Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L., Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E., Torriani S.F.F., McDonald B.A., Oliver R.P.
    Plant Cell 19:3347-3368(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SN15 / ATCC MYA-4574 / FGSC 10173.

Entry informationi

Entry nameiH2A_PHANO
AccessioniPrimary (citable) accession number: Q0U1A1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: September 5, 2006
Last modified: February 19, 2014
This is version 51 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-131.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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