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Q1E5N1

- H2A_COCIM

UniProt

Q1E5N1 - H2A_COCIM

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Protein

Histone H2A

Gene

HTA1

Organism
Coccidioides immitis (strain RS) (Valley fever fungus)
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 ubiquitinatedCurated

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
Gene namesi
Name:HTA1
ORF Names:CIMG_02132
OrganismiCoccidioides immitis (strain RS) (Valley fever fungus)
Taxonomic identifieri246410 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesmitosporic OnygenalesCoccidioides
ProteomesiUP000001261: Unassembled WGS sequence

Subcellular locationi

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 – 133132Histone H2APRO_0000297733Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51N6-acetyllysineBy similarity
Modified residuei9 – 91N6-acetyllysineBy similarity
Modified residuei106 – 1061N5-methylglutamineBy similarity
Modified residuei130 – 1301PhosphoserineBy 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

Proteomic databases

PRIDEiQ1E5N1.

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

ProteinModelPortaliQ1E5N1.
SMRiQ1E5N1. Positions 14-121.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi130 – 1312[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

InParanoidiQ1E5N1.
KOiK11251.
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.

Q1E5N1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTGGKSGGKA SGSKSSQSRS SKAGLAFPVG RVHRLLRKGN YAQRVGAGAP
60 70 80 90 100
VYLAAVLEYL AAEILELAGN AARDNKKTRI IPRHLQLAIR NDEELNKLLG
110 120 130
HVTIAQGGVM PYIHQNLLPK KTPKTGKNPS QEL
Length:133
Mass (Da):14,219
Last modified:July 11, 2006 - v1
Checksum:iAA0FA27D95C01F8D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GG704911 Genomic DNA. Translation: EAS36936.2.
RefSeqiXP_001248361.1. XM_001248360.1.
XP_001248519.1. XM_001248518.1.

Genome annotation databases

GeneIDi4568059.
4568207.
KEGGicim:CIMG_02132.
cim:CIMG_02290.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GG704911 Genomic DNA. Translation: EAS36936.2 .
RefSeqi XP_001248361.1. XM_001248360.1.
XP_001248519.1. XM_001248518.1.

3D structure databases

ProteinModelPortali Q1E5N1.
SMRi Q1E5N1. Positions 14-121.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q1E5N1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 4568059.
4568207.
KEGGi cim:CIMG_02132.
cim:CIMG_02290.

Phylogenomic databases

InParanoidi Q1E5N1.
KOi K11251.
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

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: RS.
  2. Cited for: GENOME REANNOTATION.
    Strain: RS.

Entry informationi

Entry nameiH2A_COCIM
AccessioniPrimary (citable) accession number: Q1E5N1
Secondary accession number(s): J3KL19
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: July 11, 2006
Last modified: October 29, 2014
This is version 52 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.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-130.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3