Reviewed,
UniProtKB/Swiss-Prot P39984 (HAT2_YEAST)
Last modified
June 16, 2009.
Version 89.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Histone acetyltransferase type B subunit 2 EC=2.3.1.48 | ||||
| Gene names |
| ||||
| Organism | Saccharomyces cerevisiae (Baker's yeast) [Complete proteome] | ||||
| Taxonomic identifier | 4932 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces |
Protein attributes
| Sequence length | 401 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Component of the histone acetylase B (HAT-B) complex. The complex acetylates 'Lys-12' of histone H4 which is required for telomeric silencing. HAT2 is required for high affinity binding of the acetyltransferase to histone H4, for the nuclear location of HAT1 and for the HAT1-HIF1 interaction. Alone, it is unable to bind to H4, requiring HAT1 for high affinity interaction with the histone tail. HAT2 has also a HAT1 independent function in life-span regulation. Ref.5 Ref.6 Ref.7 Ref.8 |
| Catalytic activity | Acetyl-CoA + histone = CoA + acetylhistone. |
| Subunit structure | Component of the HAT-B complex composed of at least HAT1 and HAT2. In the cytoplasm, this complex binds to the histone H4 tail. In the nucleus, the HAT-B complex has an additional component, the histone H3/H4 chaperone HIF1. |
| Subcellular location | Cytoplasm. Nucleus. Note: The nuclear location requires the presence of HAT2. Ref.6 Ref.7 |
| Induction | Repressed in presence of farnesol, probably through a intracellular decrease of diacylglycerol. Ref.4 |
| Sequence similarities | Belongs to the WD repeat RBAP46/RBAP48/MSI1 family. Contains 6 WD repeats. |
Ontologies
| Keywords | |
|---|---|
| Biological process | DNA damage DNA repair |
| Cellular component | Cytoplasm Nucleus |
| Domain | Repeat WD repeat |
| Molecular function | Acyltransferase Chromatin regulator Transferase |
| Technical term | Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | DNA repair Inferred from electronic annotation. Source: UniProtKB-KW chromatin assembly or disassembly Ref.1Inferred from direct assay. Source: SGD chromatin silencing at telomere Ref.5Inferred from genetic interaction. Source: SGD histone acetylation Ref.1 Ref.3Inferred from direct assay. Source: SGD |
| Cellular component | cytoplasm Ref.1 Ref.3 Inferred from direct assay. Source: SGD histone acetyltransferase complex Ref.1 Ref.3 Ref.6Inferred from direct assay. Source: SGD |
| Molecular function | histone acetyltransferase activity Inferred from electronic annotation. Source: EC histone binding Ref.1Inferred from direct assay. Source: SGD |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 401 | 401 | Histone acetyltransferase type B subunit 2 | PRO_0000051014 | |||||
Regions | |||||||||
| Repeat | 116 – 147 | 32 | WD 1 | ||||||
| Repeat | 158 – 189 | 32 | WD 2 | ||||||
| Repeat | 206 – 237 | 32 | WD 3 | ||||||
| Repeat | 249 – 280 | 32 | WD 4 | ||||||
| Repeat | 293 – 324 | 32 | WD 5 | ||||||
| Repeat | 350 – 381 | 32 | WD 6 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The major cytoplasmic histone acetyltransferase in yeast: links to chromatin replication and histone metabolism." Parthun M.R., Widom J., Gottschling D.E. Cell 87:85-94(1996) [PubMed: 8858151] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 83-105, ACETYLATION OF HISTONE H4, INTERACTION WITH HAT1 AND HISTONE H4. |
| [2] | "The nucleotide sequence of Saccharomyces cerevisiae chromosome V." Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. Davis R.W.Nature 387:78-81(1997) [PubMed: 9169868] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972. |
| [3] | "HAT1 and HAT2 proteins are components of a yeast nuclear histone acetyltransferase enzyme specific for free histone H4." Ruiz-Garcia A.B., Sendra R., Galiana M., Pamblanco M., Perez-Ortin J.E., Tordera V. J. Biol. Chem. 273:12599-12605(1998) [PubMed: 9575221] [Abstract] Cited for: ACETYLATION OF HISTONE H4 BY THE HAT-B COMPLEX. |
| [4] | "Farnesol-induced growth inhibition in Saccharomyces cerevisiae by a cell cycle mechanism." Machida K., Tanaka T., Yano Y., Otani S., Taniguchi M. Microbiology 145:293-299(1999) [PubMed: 10075411] [Abstract] Cited for: INDUCTION. |
| [5] | "Type B histone acetyltransferase Hat1p participates in telomeric silencing." Kelly T.J., Qin S., Gottschling D.E., Parthun M.R. Mol. Cell. Biol. 20:7051-7058(2000) [PubMed: 10982821] [Abstract] Cited for: FUNCTION, ACETYLATION OF HISTONE H4. |
| [6] | "Hif1 is a component of yeast histone acetyltransferase B, a complex mainly localized in the nucleus." Poveda A., Pamblanco M., Tafrov S., Tordera V., Sternglanz R., Sendra R. J. Biol. Chem. 279:16033-16043(2004) [PubMed: 14761951] [Abstract] Cited for: IDENTIFICATION IN THE HAT-B COMPLEX, FUNCTION OF THE HAT-B COMPLEX, INTERACTION WITH HISTONE H4, SUBCELLULAR LOCATION. |
| [7] | "The nuclear Hat1p/Hat2p complex: a molecular link between type B histone acetyltransferases and chromatin assembly." Ai X., Parthun M.R. Mol. Cell 14:195-205(2004) [PubMed: 15099519] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE HAT-B COMPLEX, MASS SPECTROMETRY, INTERACTION WITH HISTONES H3 AND H4, SUBCELLULAR LOCATION. |
| [8] | "Yeast HAT1 and HAT2 deletions have different life-span and transcriptome phenotypes." Rosaleny L.E., Antunez O., Ruiz-Garcia A.B., Perez-Ortin J.E., Tordera V. FEBS Lett. 579:4063-4068(2005) [PubMed: 16023114] [Abstract] Cited for: FUNCTION. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| U18795 Genomic DNA. Translation: AAB65031.1. | |
| PIR | S50533. |
| RefSeq | NP_010858.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP:2363N. |
| IntAct | P39984. 9 interactions. |
Proteomic databases | |
| PeptideAtlas | P39984. |
| PRIDE | P39984. |
Genome annotation databases | |
| Ensembl | YEL056W. Saccharomyces cerevisiae. [Contig view] |
| GeneID | 856654. |
| GenomeReviews | Gene locus YEL056W in contig U00092_GR. |
| KEGG | sce:YEL056W. |
| NMPDR | fig|4932.3.peg.1907. |
Organism-specific databases | |
| CYGD | YEL056w. |
| SGD | S000000782. HAT2. |
| Yeast-GFP | Search... |
Phylogenomic databases | |
| HOGENOM | P39984. |
| OMA | P39984. SNIRITA. |
Enzyme and pathway databases | |
| BRENDA | 2.3.1.48. 250. |
Gene expression databases | |
| ArrayExpress | P39984. |
| GermOnline | YEL056W. Saccharomyces cerevisiae. |
Family and domain databases | |
| InterPro | IPR015943. WD40/YVTN_repeat-like. IPR001680. WD40_repeat. IPR019782. WD40_repeat_2. IPR019775. WD40_repeat_CS. IPR017986. WD40_repeat_region. IPR019781. WD40_repeat_sg. [Graphical view] |
| Gene3D | G3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit. |
| Pfam | PF00400. WD40. 3 hits. [Graphical view] |
| SMART | SM00320. WD40. 6 hits. [Graphical view] |
| PROSITE | PS00678. WD_REPEATS_1. 2 hits. PS50082. WD_REPEATS_2. 2 hits. PS50294. WD_REPEATS_REGION. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 982637. |
Entry information
| Entry name | HAT2_YEAST | ||||||||
| Accession | Primary (citable) accession number: P39984 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |
| Yeast Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD |
| Yeast chromosome V Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names |

Clusters with


