Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Histone H2A.1

Gene

HTA1

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed-Annotation score: 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.

Miscellaneous

In contrast to vertebrates and insects, its C-terminus is not monoubiquitinated.Curated

GO - Molecular functioni

  • DNA binding Source: CGD
  • protein heterodimerization activity Source: InterPro

GO - Biological processi

Keywordsi

Molecular functionDNA-binding
Biological processDNA damage, DNA repair

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2A.1
Gene namesi
Name:HTA1
Ordered Locus Names:CAALFM_C303910WA
ORF Names:CaO19.14186, CaO19.6924
OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifieri237561 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
Proteomesi
  • UP000000559 Componenti: Chromosome 3

Organism-specific databases

CGDiCAL0000179664. HTA1.

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002287252 – 132Histone H2A.1Add BLAST131

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei5N6-acetyllysineBy similarity1
Modified residuei7N6-acetyllysineBy similarity1
Modified residuei105N5-methylglutamineBy similarity1
Modified residuei129PhosphoserineBy 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 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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei119Not ubiquitinatedCurated1

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

PRIDEiQ59SU5.

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

Structurei

3D structure databases

ProteinModelPortaliQ59SU5.
SMRiQ59SU5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi129 – 130[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

InParanoidiQ59SU5.
KOiK11251.
OrthoDBiEOG092C5QJX.

Family and domain databases

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.

Q59SU5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGGKGKAGT SEKASTSRSA KAGLTFPVGR VHRLLRKGNY AQRIGSGAPV
60 70 80 90 100
YLTSVLEYLA AEILELAGNA ARDNKKSRII PRHLQLAIRN DEELNKLLGD
110 120 130
VTIAQGGVLP NIHQNLLPKK SGKGGVKASQ EL
Length:132
Mass (Da):14,009
Last modified:January 23, 2007 - v3
Checksum:i699C411612F3D621
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP017625 Genomic DNA. Translation: AOW28418.1.
RefSeqiXP_712725.1. XM_707632.2.

Genome annotation databases

GeneIDi3645658.
KEGGical:CAALFM_C303910WA.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiH2A1_CANAL
AccessioniPrimary (citable) accession number: Q59SU5
Secondary accession number(s): A0A1D8PK04
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: January 23, 2007
Last modified: June 7, 2017
This is version 77 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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-129.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Candida albicans
    Candida albicans: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families