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 acetyltransferase type B subunit 2

Gene

HAT2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulatory subunit 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.5 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei266 – 2661Important for interaction with HAT11 Publication

GO - Molecular functioni

  1. histone binding Source: SGD

GO - Biological processi

  1. chromatin assembly or disassembly Source: SGD
  2. chromatin silencing at telomere Source: SGD
  3. histone acetylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Enzyme and pathway databases

BioCyciYEAST:G3O-30174-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase type B subunit 2
Gene namesi
Name:HAT2
Ordered Locus Names:YEL056W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome V

Organism-specific databases

CYGDiYEL056w.
SGDiS000000782. HAT2.

Subcellular locationi

Cytoplasm. Nucleus
Note: The nuclear location requires the presence of HAT2.

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. histone acetyltransferase complex Source: SGD
  3. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi266 – 2661L → E: Abolishes interaction with HAT1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 401401Histone acetyltransferase type B subunit 2PRO_0000051014Add
BLAST

Proteomic databases

MaxQBiP39984.
PaxDbiP39984.
PeptideAtlasiP39984.

Expressioni

Inductioni

Repressed in presence of farnesol, probably through a intracellular decrease of diacylglycerol.1 Publication

Gene expression databases

GenevestigatoriP39984.

Interactioni

Subunit structurei

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 HIF1.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HAT1Q123415EBI-8185,EBI-8176
HIF1Q123733EBI-8185,EBI-31911

Protein-protein interaction databases

BioGridi36673. 69 interactions.
DIPiDIP-2363N.
IntActiP39984. 7 interactions.
MINTiMINT-654148.
STRINGi4932.YEL056W.

Structurei

Secondary structure

1
401
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 189Combined sources
Helixi21 – 244Combined sources
Beta strandi25 – 328Combined sources
Beta strandi40 – 423Combined sources
Beta strandi48 – 503Combined sources
Turni51 – 533Combined sources
Beta strandi54 – 618Combined sources
Beta strandi71 – 8111Combined sources
Helixi82 – 843Combined sources
Beta strandi109 – 11911Combined sources
Beta strandi121 – 1277Combined sources
Beta strandi130 – 1389Combined sources
Beta strandi143 – 1475Combined sources
Turni148 – 1503Combined sources
Beta strandi151 – 1566Combined sources
Beta strandi165 – 1684Combined sources
Beta strandi170 – 1723Combined sources
Beta strandi175 – 1795Combined sources
Beta strandi185 – 1895Combined sources
Beta strandi191 – 1944Combined sources
Beta strandi200 – 2067Combined sources
Beta strandi211 – 2166Combined sources
Beta strandi223 – 2286Combined sources
Beta strandi231 – 2377Combined sources
Beta strandi244 – 2496Combined sources
Beta strandi254 – 2596Combined sources
Beta strandi264 – 2718Combined sources
Beta strandi276 – 2805Combined sources
Beta strandi288 – 2914Combined sources
Beta strandi298 – 3036Combined sources
Beta strandi305 – 3073Combined sources
Beta strandi310 – 3156Combined sources
Beta strandi320 – 3245Combined sources
Helixi325 – 3273Combined sources
Turni334 – 3385Combined sources
Beta strandi344 – 3485Combined sources
Beta strandi355 – 3606Combined sources
Beta strandi362 – 3643Combined sources
Beta strandi367 – 3726Combined sources
Turni373 – 3753Combined sources
Beta strandi376 – 3827Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4PSWX-ray2.10B7-390[»]
4PSXX-ray2.51B/E8-389[»]
ProteinModelPortaliP39984.
SMRiP39984. Positions 7-390.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati116 – 14732WD 1Add
BLAST
Repeati158 – 18932WD 2Add
BLAST
Repeati206 – 23732WD 3Add
BLAST
Repeati249 – 28032WD 4Add
BLAST
Repeati293 – 32432WD 5Add
BLAST
Repeati350 – 38132WD 6Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni335 – 3395Interaction with the histone H4 N-terminus1 Publication

Sequence similaritiesi

Contains 6 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00570000079069.
HOGENOMiHOG000160330.
InParanoidiP39984.
KOiK10752.
OMAiISQPLEW.
OrthoDBiEOG7D865N.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR022052. Histone-bd_RBBP4_N.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF12265. CAF1C_H4-bd. 1 hit.
PF00400. WD40. 2 hits.
[Graphical view]
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 2 hits.
PS50082. WD_REPEATS_2. 2 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P39984-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MENQEKPLSV DEEYDLWKSN VPLMYDFVSE TRLTWPSLTV QWLPTPVQEL
60 70 80 90 100
DGGFIKQELI IGTHTSGEEE NYLKFAEINL PKEILSNEDP QEEAGEEYQS
110 120 130 140 150
SLPAPRSNIR ITAKYEHEEE ITRARYMPQD PNIVATINGQ GTVFLYSRSE
160 170 180 190 200
GLQSTLKFHK DNGYALSFST LVKGRLLSGS DDHTVALWEV GSGGDPTKPV
210 220 230 240 250
RTWNDLHSDI INDNKWHNFN KDLFGTVSED SLLKINDVRA NNTTIDTVKC
260 270 280 290 300
PQPFNTLAFS HHSSNLLAAA GMDSYVYLYD LRNMKEPLHH MSGHEDAVNN
310 320 330 340 350
LEFSTHVDGV VVSSGSDNRL MMWDLKQIGA EQTPDDAEDG VPELIMVHAG
360 370 380 390 400
HRSSVNDFDL NPQIPWLVAS AEEENILQVW KCSHSLPIVG GPPKVNKDII

S
Length:401
Mass (Da):45,060
Last modified:February 1, 1995 - v1
Checksum:iC27A91C99D9FCAB7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18795 Genomic DNA. Translation: AAB65031.1.
BK006939 Genomic DNA. Translation: DAA07598.1.
PIRiS50533.
RefSeqiNP_010858.3. NM_001178871.3.

Genome annotation databases

EnsemblFungiiYEL056W; YEL056W; YEL056W.
GeneIDi856654.
KEGGisce:YEL056W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18795 Genomic DNA. Translation: AAB65031.1.
BK006939 Genomic DNA. Translation: DAA07598.1.
PIRiS50533.
RefSeqiNP_010858.3. NM_001178871.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4PSWX-ray2.10B7-390[»]
4PSXX-ray2.51B/E8-389[»]
ProteinModelPortaliP39984.
SMRiP39984. Positions 7-390.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36673. 69 interactions.
DIPiDIP-2363N.
IntActiP39984. 7 interactions.
MINTiMINT-654148.
STRINGi4932.YEL056W.

Proteomic databases

MaxQBiP39984.
PaxDbiP39984.
PeptideAtlasiP39984.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYEL056W; YEL056W; YEL056W.
GeneIDi856654.
KEGGisce:YEL056W.

Organism-specific databases

CYGDiYEL056w.
SGDiS000000782. HAT2.

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00570000079069.
HOGENOMiHOG000160330.
InParanoidiP39984.
KOiK10752.
OMAiISQPLEW.
OrthoDBiEOG7D865N.

Enzyme and pathway databases

BioCyciYEAST:G3O-30174-MONOMER.

Miscellaneous databases

NextBioi982637.
PROiP39984.

Gene expression databases

GenevestigatoriP39984.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR022052. Histone-bd_RBBP4_N.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF12265. CAF1C_H4-bd. 1 hit.
PF00400. WD40. 2 hits.
[Graphical view]
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 2 hits.
PS50082. WD_REPEATS_2. 2 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 83-105, ACETYLATION OF HISTONE H4, INTERACTION WITH HAT1 AND HISTONE H4.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "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] [Europe PMC] [Abstract]
    Cited for: ACETYLATION OF HISTONE H4 BY THE HAT-B COMPLEX.
  5. "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] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  6. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ACETYLATION OF HISTONE H4.
  7. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE HAT-B COMPLEX, FUNCTION OF THE HAT-B COMPLEX, INTERACTION WITH HISTONE H4, SUBCELLULAR LOCATION.
  8. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE HAT-B COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH HISTONES H3 AND H4, SUBCELLULAR LOCATION.
  9. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Hat2p recognizes the histone H3 tail to specify the acetylation of the newly synthesized H3/H4 heterodimer by the Hat1p/Hat2p complex."
    Li Y., Zhang L., Liu T., Chai C., Fang Q., Wu H., Agudelo Garcia P.A., Han Z., Zong S., Yu Y., Zhang X., Parthun M.R., Chai J., Xu R.M., Yang M.
    Genes Dev. 28:1217-1227(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 7-390 IN COMPLEXES WITH HAT1 AND HISTONE PEPTIDES, INTERACTION WITH HAT1 AND HISTONES H3 AND H4, SUBUNIT, FUNCTION, MUTAGENESIS OF LEU-266.

Entry informationi

Entry nameiHAT2_YEAST
AccessioniPrimary (citable) accession number: P39984
Secondary accession number(s): D3DLJ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: February 4, 2015
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome V
    Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

External Data

Dasty 3

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 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.