S. cerevisiae Gene HTA2 (YBL003C)
  Description: Histone H2A, core histone protein required for chromatin assembly and chromosome function one of two nearly identical (see also HTA1) subtypes DNA damage-dependent phosphorylation by Mec1p facilitates DNA repair acetylated by Nat4p
Transcript (Including UTRs)
   Position: sacCer3 chrII:235,394-235,792 Size: 399 Total Exon Count: 1 Strand: -
Coding Region
   Position: sacCer3 chrII:235,394-235,792 Size: 399 Coding Exon Count: 1 

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GO AnnotationsOther NamesMethods
Data last updated at UCSC: 2011-08-29

-  Sequence and Links to Tools and Databases
 
Genomic Sequence (chrII:235,394-235,792)mRNAProtein (132 aa)
Gene SorterGenome BrowserOther Species FASTAAlphaFoldSGDUniProtKB

-  Comments and Description Text from UniProtKB
  ID: H2A2_YEAST
DESCRIPTION: RecName: Full=Histone H2A.2;
FUNCTION: 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.
SUBUNIT: 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. Interacts with NAP1.
SUBCELLULAR LOCATION: Nucleus. Chromosome.
DOMAIN: The [ST]-Q motif constitutes a recognition sequence for kinases from the PI3/PI4-kinase family.
PTM: 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 interacts with ARP4, a shared component of the NuA4 histone acetyltransferase complex and the INO80 and SWR1 chromatin remodeling complexes, and serves to recruit first NuA4, mediating histone H4 acetylation, and subsequently the INO80/SWR1 complexes, facilitating DNA resection, to DSB sites. Gamma-H2A is required for sequestering cohesin around the break site, which is important for efficient post-replicative double-strand break repair by homologous recombination, holding the damaged chromatid close to its undamaged sister template. Gamma-H2A is removed from the DNA prior to the strand invasion-primer extension step of the repair process and subsequently dephosphorylated by PPH3, a component of the histone H2A phosphatase complex (HTP-C). Dephosphorylation is necessary for efficient recovery from the DNA damage checkpoint.
PTM: N-acetylated by NAT4.
PTM: Acetylated by ESA1, a component of the NuA4 histone acetyltransferase (HAT) complex, to form H2AK4ac and H2AK7ac.
PTM: Sumoylated to from H2AK126su. May lead to transcriptional repression.
MISCELLANEOUS: In contrast to vertebrates and insects, its C- terminus is not monoubiquitinated (Probable).
MISCELLANEOUS: Present with 32100 molecules/cell in log phase SD medium.
SIMILARITY: Belongs to the histone H2A family.
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-8; H2AK126su = sumoylated Lys-127; H2AS128ph = phosphorylated Ser-129.

-  Primer design for this transcript
 

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To design primers for a non-coding sequence, zoom to a region of interest and select from the drop-down menu: View > In External Tools > Primer3


-  Protein Domain and Structure Information
  InterPro Domains: Graphical view of domain structure
IPR009072 - Histone-fold
IPR007125 - Histone_core_D
IPR002119 - Histone_H2A

Pfam Domains:
PF00125 - Core histone H2A/H2B/H3/H4

ModBase Predicted Comparative 3D Structure on P04912
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-  Orthologous Genes in Other Species
  Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
HumanMouseRatZebrafishD. melanogasterC. elegans
No orthologNo orthologNo orthologNo orthologGenome BrowserGenome Browser
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-  Gene Ontology (GO) Annotations with Structured Vocabulary
  Molecular Function:
GO:0003677 DNA binding
GO:0046982 protein heterodimerization activity

Biological Process:
GO:0006281 DNA repair
GO:0006333 chromatin assembly or disassembly
GO:0006342 chromatin silencing
GO:0006974 cellular response to DNA damage stimulus

Cellular Component:
GO:0000786 nucleosome
GO:0000788 nuclear nucleosome
GO:0005634 nucleus
GO:0005694 chromosome
GO:0031298 replication fork protection complex


-  Other Names for This Gene
  UCSC ID: YBL003C
Protein: P04912 (aka H2A2_YEAST)

-  SGD Genes Methods, Credits, and Data Use Restrictions
  Click here for details on how this gene model was made and data restrictions if any.