HDA1/YNL021W Summary Help

Standard Name HDA1 1
Systematic Name YNL021W
Feature Type ORF, Verified
Description Putative catalytic subunit of a class II histone deacetylase complex; role in azole resistance via Hsp90p, and in the heat shock response; Hda1p interacts with the Hda2p-Hda3p subcomplex to form an active tetramer; deletion increases histone H2B, H3 and H4 acetylation; other members of the HDA1 histone deacetylase complex are Hda2p and Hda3p (1, 2, 3, 4, 5, 6, 7 and see Summary Paragraph)
Name Description Histone DeAcetylase 2
Chromosomal Location
ChrXIV:593227 to 595347 | ORF Map | GBrowse
Gene Ontology Annotations All HDA1 GO evidence and references
  View Computational GO annotations for HDA1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 1 genes
Classical genetics
Large-scale survey
597 total interaction(s) for 439 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 20
  • Affinity Capture-Western: 2
  • Biochemical Activity: 5
  • Co-localization: 1
  • Reconstituted Complex: 5
  • Two-hybrid: 9

Genetic Interactions
  • Dosage Growth Defect: 3
  • Dosage Lethality: 159
  • Negative Genetic: 153
  • Phenotypic Enhancement: 13
  • Phenotypic Suppression: 11
  • Positive Genetic: 41
  • Synthetic Growth Defect: 66
  • Synthetic Lethality: 20
  • Synthetic Rescue: 89

Expression Summary
Length (a.a.) 706
Molecular Weight (Da) 80,069
Isoelectric Point (pI) 5.24
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrXIV:593227 to 595347 | ORF Map | GBrowse
Last Update Coordinates: 2011-02-03 | Sequence: 1997-01-28
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..2121 593227..595347 2011-02-03 1997-01-28
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000004966

HDA1 encodes a histone deacetylase (2). Covalent modifications of histones, including acetylation and deacetylation, are implicated in transcriptional regulation in yeast and other eukaryotes, and have been reviewed in 8 and 9. Hda1p is part of a complex that also contains Hda3p (1). A second histone deactylase, Rpd3p, shows sequence similarity to Hda1p but is found in a complex distinct from the complex containing Hda1p (2); the two complexes affect transcription of distinct, partially overlapping sets of genes (2, 9). Deletion of HDA1 increases histone acetylation in vivo and increases telomeric repression of transcription (2). Three more histone deactylases, Hos1p, Hos2p, and Hos3p, have been identified in yeast; they share sequence similarity with Rpd3p and Hda1p but are less well characterized (2).

Last updated: 2000-01-10 Contact SGD

References cited on this page View Complete Literature Guide for HDA1
1) Carmen AA, et al.  (1996) HDA1 and HDA3 are components of a yeast histone deacetylase (HDA) complex. J Biol Chem 271(26):15837-44
2) Rundlett SE, et al.  (1996) HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes that regulate silencing and transcription. Proc Natl Acad Sci U S A 93(25):14503-8
3) Bernstein BE, et al.  (2000) Genomewide studies of histone deacetylase function in yeast. Proc Natl Acad Sci U S A 97(25):13708-13
4) Wu J, et al.  (2001) TUP1 utilizes histone H3/H2B-specific HDA1 deacetylase to repress gene activity in yeast. Mol Cell 7(1):117-26
5) Wu J, et al.  (2001) HDA2 and HDA3 are related proteins that interact with and are essential for the activity of the yeast histone deacetylase HDA1. Proc Natl Acad Sci U S A 98(8):4391-6
6) Robyr D, et al.  (2002) Microarray deacetylation maps determine genome-wide functions for yeast histone deacetylases. Cell 109(4):437-46
7) Robbins N, et al.  (2012) Lysine deacetylases Hda1 and Rpd3 regulate Hsp90 function thereby governing fungal drug resistance. Cell Rep 2(4):878-88
8) Mizzen C, et al.  (1998) Signaling to chromatin through histone modifications: how clear is the signal? Cold Spring Harb Symp Quant Biol 63:469-81
9) Suka N, et al.  (1998) The regulation of gene activity by histones and the histone deacetylase RPD3. Cold Spring Harb Symp Quant Biol 63():391-9