Similar to other histones, H2A has a positively charged N-terminus (residues 1-21) that extends into the extranucleosomal space (8, 11). H2A is unique, however, in that its C-terminus (amino acids 121-132) also extends outside the nucleosome. Both termini contain modifiable residues with roles in different cellular processes, such as telomere position effect (TPE) and double-strand break (DSB) repair (8, 13). Differential acetylation and deacetylation of lysines 5 and 8 appears to regulate telomeric silencing, and phosphorylation of threonine 126 is also required for proper TPE (8). Phosphorylation of serine 122 is necessary for survival in the presence of DNA damage, and also for sporulation, indicating a possible role in homologous recombination (13). Phosphorylation of serine 129 is crucial for G1 DNA damage checkpoint regulation, chromatin remodeling, and DSB repair through the recruitment of repair components (15, 17, 6, 20). Following DSB damage, Tel1p phosphorylates S129, which is situated within a conserved SQE consensus target motif, over a large domain encompassing many kilobases surrounding the DSB (15, 17, 6). The Rad9p checkpoint protein is recruited to this domain and phosphorylated by Mec1p, which activates the checkpoint kinase Rad53p and induces a G1 delay (15). Binding of the NuA4 nucleosomal histone acetyltransferase complex to phosphorylated H2A results in acetylation of H4, followed by recruitment of the SWR and INO80 chromatin remodeling complexes (21, 23). SWR catalyzes exchange of histone H2A for the variant H2A.Z (Htz1p), while INO80 displaces histone octamers and facilitates resection to form ssDNA at DSBs (26, 27, 28, 29, 30, 31, 32). Deletion of either the N- or C-terminus of H2A reduces TPE efficiency, and deletion of the N-terminus or lack of T126 phosphorylation reduces non-homologous end joining (8). Mutants lacking phosphorylation at S122 exhibit impaired sporulation (13). Mutants lacking phosphorylation at S129 show defects in the G1 checkpoint response, including attenuated cell cycle delay, decreased Rad53p kinase activation, and reduced Rad9p phosphorylation and recruitment to damaged sites (15).", "date_edited": "2007-07-30"}, "literature_overview": {"primary_count": 160, "additional_count": 259, "review_count": 143, "go_count": 2, "phenotype_count": 4, "disease_count": 0, "interaction_count": 126, "regulation_count": 11, "ptm_count": 12, "funComplement_count": 0, "htp_count": 15, "total_count": 666}, "disease_overview": {"manual_disease_terms": [], "htp_disease_terms": [], "computational_annotation_count": 0, "date_last_reviewed": null}, "ecnumbers": [], "URS_ID": null, "main_strain": "S288C", "genetic_position": 0.2, "regulation_overview": {"regulator_count": 21, "target_count": 0, "paragraph": {"text": "HTA2 promoter is bound by Fkh2p, Reb1p, Uga3p, and Yap5p in response to heat; HTA2 transcription is upregulated by SAGA, Spt10p, and Spt21p; HTA2 transcription is downregulated by Hst2p, Nhp6ap, Nhp6bp, and Yta7p; Hta2 protein activity is regulated by Bub1p, Cka1p, Glc7p, Mec1p, and Tel1p", "date_edited": "2025-02-18", "references": [{"id": 2395011, "display_name": "Wang D, et al. (2022)", "citation": "Wang D, et al. (2022) Global profiling of regulatory elements in the histone benzoylation pathway. Nat Commun 13(1):1369", "pubmed_id": 35296687, "link": "/reference/S000314507", "year": 2022, "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1038/s41467-022-29057-2"}, {"display_name": "PMC full text", "link": "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8927147/"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/35296687"}]}, {"id": 487915, "display_name": "Gradolatto A, et al. (2008)", "citation": "Gradolatto A, et al. (2008) Saccharomyces cerevisiae Yta7 regulates histone gene expression. Genetics 179(1):291-304", "pubmed_id": 18493054, "link": "/reference/S000126475", "year": 2008, "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1534/genetics.107.086520"}, {"display_name": "PMC full text", "link": "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2390607/"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/18493054"}, {"display_name": "Reference supplement", "link": "http://www.genetics.org/cgi/content/full/179/1/291/DC1"}]}, {"id": 1443414, "display_name": "Durano D, et al. (2017)", "citation": "Durano D, et al. (2017) A novel role for Nhp6 proteins in histone gene regulation in Saccharomyces cerevisiae. Int J Biochem Cell Biol 83:76-83", "pubmed_id": 28025045, "link": "/reference/S000185713", "year": 2017, "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1016/j.biocel.2016.12.012"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/28025045"}]}, {"id": 414327, "display_name": "Venters BJ, et al. (2011)", "citation": "Venters BJ, et al. (2011) A comprehensive genomic binding map of gene and chromatin regulatory proteins in Saccharomyces. Mol Cell 41(4):480-92", "pubmed_id": 21329885, "link": "/reference/S000145602", "year": 2011, "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1016/j.molcel.2011.01.015"}, {"display_name": "PMC full text", "link": "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3057419/"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/21329885"}]}, {"id": 423931, "display_name": "Kitada T, et al. (2011)", "citation": "Kitada T, et al. (2011) \u03b3H2A is a component of yeast heterochromatin required for telomere elongation. Cell Cycle 10(2):293-300", "pubmed_id": 21212735, "link": "/reference/S000142780", "year": 2011, "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.4161/cc.10.2.14536"}, {"display_name": "PMC full text", "link": "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3033431/"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/21212735"}]}, {"id": 466312, "display_name": "Bazzi M, et al. (2010)", "citation": "Bazzi M, et al. (2010) Dephosphorylation of gamma H2A by Glc7/protein phosphatase 1 promotes recovery from inhibition of DNA replication. Mol Cell Biol 30(1):131-45", "pubmed_id": 19884341, "link": "/reference/S000132094", "year": 2010, "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1128/MCB.01000-09"}, {"display_name": "PMC full text", "link": "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2798293/"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/19884341"}]}, {"id": 362076, "display_name": "Basnet H, et al. (2014)", "citation": "Basnet H, et al. (2014) Tyrosine phosphorylation of histone H2A by CK2 regulates transcriptional elongation. Nature 516(7530):267-71", "pubmed_id": 25252977, "link": "/reference/S000177299", "year": 2014, "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1038/nature13736"}, {"display_name": "PMC full text", "link": "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4461219/"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/25252977"}]}, {"id": 1972011, "display_name": "Ishiguro T, et al. (2018)", "citation": "Ishiguro T, et al. (2018) Malonylation of histone H2A at lysine 119 inhibits Bub1-dependent H2A phosphorylation and chromosomal localization of shugoshin proteins. Sci Rep 8(1):7671", "pubmed_id": 29769606, "link": "/reference/S000216883", "year": 2018, "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1038/s41598-018-26114-z"}, {"display_name": "PMC full text", "link": "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5956101/"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/29769606"}]}, {"id": 2355830, "display_name": "Bhagwat M, et al. (2021)", "citation": "Bhagwat M, et al. (2021) Replication stress inhibits synthesis of histone mRNAs in yeast by removing Spt10p and Spt21p from the histone promoters. J Biol Chem 297(5):101246", "pubmed_id": 34582893, "link": "/reference/S000307548", "year": 2021, "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1016/j.jbc.2021.101246"}, {"display_name": "PMC full text", "link": "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8551654/"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/34582893"}]}]}}, "reference_mapping": {"609576": 1, "362076": 2, "595813": 3, "622880": 4, "579626": 5, "591193": 6, "548932": 7, "551751": 8, "525910": 9, "618194": 10, "498562": 11, "568795": 12, "533280": 13, "501032": 14, "513521": 15, "525380": 16, "504152": 17, "530228": 18, "501029": 19, "508938": 20, "498559": 21, "501026": 22, "536000": 23, "633866": 24, "501023": 25, "543656": 26, "552194": 27, "545808": 28, "535973": 29, "535970": 30, "549809": 31, "526619": 32}, "history": [{"category": "Name", "history_type": "LSP", "note": "Name: H2A2", "date_created": "2010-02-16", "references": [{"id": 595813, "display_name": "Choe J, et al. (1982)", "citation": "Choe J, et al. (1982) The two yeast histone H2A genes encode similar protein subtypes. Proc Natl Acad Sci U S A 79(5):1484-7", "pubmed_id": 7041122, "link": "/reference/S000057330", "year": 1982, "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1073/pnas.79.5.1484"}, {"display_name": "PMC full text", "link": "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC345998/"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/7041122"}]}]}, {"category": "Name", "history_type": "LSP", "note": "Name: HTA2", "date_created": "2000-05-19", "references": [{"id": 609576, "display_name": "Kolodrubetz D, et al. (1982)", "citation": "Kolodrubetz D, et al. (1982) Histone H2A subtypes associate interchangeably in vivo with histone H2B subtypes. Proc Natl Acad Sci U S A 79(24):7814-8", "pubmed_id": 6760203, "link": "/reference/S000052654", "year": 1982, "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1073/pnas.79.24.7814"}, {"display_name": "PMC full text", "link": "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC347439/"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/6760203"}]}]}, {"category": "Mapping", "history_type": "SEQUENCE", "note": "Mapping: Edition 14: There are two copies of histones H2A and H2B. The TRT1 locus consists of HTA1-HTB1 divergently transcribed and the TRT2 locus consists of HTA2-HTB2 divergently transcribed.", "date_created": "1997-10-20", "references": [{"id": 587084, "display_name": "Cherry JM, et al. (1997)", "citation": "Cherry JM, et al. (1997) Genetic and physical maps of Saccharomyces cerevisiae. Nature 387(6632 Suppl):67-73", "pubmed_id": 9169866, "link": "/reference/S000060841", "year": 1997, "urls": [{"display_name": "PMC full text", "link": "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3057085/"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/9169866"}]}]}], "complexes": [{"format_name": "CPX-1611", "display_name": "Nucleosome, variant HTA2-HTB1"}, {"format_name": "CPX-1610", "display_name": "Nucleosome, variant HTA2-HTB2"}]},
tabs: {"id": 1285629, "protein_tab": true, "interaction_tab": true, "summary_tab": true, "go_tab": true, "sequence_section": true, "expression_tab": true, "phenotype_tab": true, "literature_tab": true, "wiki_tab": false, "regulation_tab": true, "sequence_tab": true, "history_tab": true, "homology_tab": true, "disease_tab": false}
};
The S. cerevisiae Reference Genome sequence is derived from laboratory strain
S288C. Download DNA or protein sequence, view genomic context and
coordinates. Click "Sequence Details" to view all sequence information for this locus, including that
for other strains.
BLASTN |
BLASTP |
Design Primers |
Restriction Fragment Map |
Restriction Fragment Sizes |
Six-Frame Translation
BLASTN vs. fungi |
BLASTP at NCBI |
BLASTP vs. fungi
Basic sequence-derived (length, molecular weight, isoelectric point) and experimentally-determined (median abundance, median absolute deviation) protein information. Click "Protein Details" for further information about the protein such as half-life, abundance, domains, domains shared with other proteins, protein sequence retrieval for various strains, physico-chemical properties, protein modification sites, and external identifiers for the protein.
Curated mutant alleles for the specified gene, listed alphabetically. Click on the allele name to open the allele page. Click "SGD search" to view all alleles in search results.
View all HTA2 alleles in SGD search
GO Annotations consist of four mandatory components: a gene product, a term from one of the three
Gene Ontology (GO) controlled vocabularies
(Molecular Function,
Biological Process, and
Cellular Component), a reference, and an
evidence code. SGD has manually curated and high-throughput GO Annotations, both derived from the
literature, as well as computational, or predicted, annotations. Click "Gene Ontology Details" to view
all GO information and evidence for this locus as well as biological processes it shares with other genes.
View computational annotations
Macromolecular complex annotations are imported from the Complex Portal. These annotations have been derived from physical molecular interaction evidence extracted from the literature and cross-referenced in the entry, or by curator inference from information on homologs in closely related species or by inference from scientific background.
Phenotype annotations for a gene are curated single mutant phenotypes that require an observable
(e.g., "cell shape"), a qualifier (e.g., "abnormal"), a mutant type (e.g., null), strain background,
and a reference. In addition, annotations are classified as classical genetics or high-throughput
(e.g., large scale survey, systematic mutation set). Whenever possible, allele information and
additional details are provided. Click "Phenotype Details" to view all phenotype annotations and
evidence for this locus as well as phenotypes it shares with other genes.
Interaction annotations are curated by BioGRID and include physical
or genetic interactions observed
between at least two genes. An interaction annotation is composed of the interaction type, name of the
interactor, assay type (e.g., Two-Hybrid), annotation type (e.g., manual or high-throughput), and a
reference, as well as other experimental details. Click "Interaction Details" to view all interaction
annotations and evidence for this locus, including an interaction visualization.
569 total interactions for 361 unique genes
The number of putative Regulators (genes that regulate it) and Targets (genes it regulates) for the
given locus, based on experimental evidence. This evidence includes data generated through
high-throughput techniques. Click "Regulation Details" to view all regulation annotations, shared GO
enrichment among regulation Targets, and a regulator/target diagram for the locus.
Expression data are derived from records contained in the
Gene Expression Omnibus (GEO), and are first log2
transformed and normalized. Referenced datasets may contain one or more condition(s), and as a result
there may be a greater number of conditions than datasets represented in a single clickable histogram
bar. The histogram division at 0.0 separates the down-regulated (green) conditions and datasets from
those that are up-regulated (red). Click "Expression Details" to view all expression annotations and
details for this locus, including a visualization of genes that share a similar expression pattern.
A summary of the locus, written by SGD Biocurators following a thorough review of the literature. Links
to gene names and curated GO terms are included within the Summary Paragraphs.
Last Updated: 2007-07-30
All manually curated literature for the specified gene, organized into topics according to their
relevance to the gene (Primary Literature, Additional Literature, or Review). Click "Literature Details"
to view all literature information for this locus, including shared literature between genes.
HTA2 / YBL003C Overview
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