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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)DescriptionActionsGraphical viewLength
Sitei266Important for interaction with HAT11 Publication1

GO - Molecular functioni

  • histone binding Source: SGD

GO - Biological processi

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

Keywords - Molecular functioni

Chromatin regulator

Enzyme and pathway databases

BioCyciYEAST:G3O-30174-MONOMER.
ReactomeiR-SCE-3214847. HATs acetylate histones.
R-SCE-3214858. RMTs methylate histone arginines.
R-SCE-349425. Autodegradation of the E3 ubiquitin ligase COP1.

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
Proteomesi
  • UP000002311 Componenti: Chromosome V

Organism-specific databases

EuPathDBiFungiDB:YEL056W.
SGDiS000000782. HAT2.

Subcellular locationi

GO - Cellular componenti

  • chromosome, telomeric region Source: GOC
  • cytoplasm Source: SGD
  • histone acetyltransferase complex Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi266L → E: Abolishes interaction with HAT1. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000510141 – 401Histone acetyltransferase type B subunit 2Add BLAST401

Proteomic databases

MaxQBiP39984.
PRIDEiP39984.

Expressioni

Inductioni

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

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

GO - Molecular functioni

  • histone binding Source: SGD

Protein-protein interaction databases

BioGridi36673. 68 interactors.
DIPiDIP-2363N.
IntActiP39984. 7 interactors.
MINTiMINT-654148.

Structurei

Secondary structure

1401
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 24Combined sources15
Beta strandi25 – 32Combined sources8
Beta strandi40 – 42Combined sources3
Beta strandi48 – 50Combined sources3
Beta strandi53 – 62Combined sources10
Beta strandi71 – 81Combined sources11
Helixi82 – 85Combined sources4
Beta strandi108 – 119Combined sources12
Beta strandi121 – 127Combined sources7
Beta strandi130 – 138Combined sources9
Beta strandi143 – 147Combined sources5
Turni148 – 150Combined sources3
Beta strandi151 – 156Combined sources6
Beta strandi165 – 168Combined sources4
Beta strandi170 – 172Combined sources3
Beta strandi175 – 179Combined sources5
Beta strandi185 – 189Combined sources5
Beta strandi191 – 194Combined sources4
Beta strandi200 – 206Combined sources7
Beta strandi211 – 216Combined sources6
Beta strandi223 – 228Combined sources6
Beta strandi231 – 237Combined sources7
Beta strandi244 – 249Combined sources6
Beta strandi254 – 259Combined sources6
Beta strandi264 – 271Combined sources8
Beta strandi276 – 280Combined sources5
Beta strandi288 – 291Combined sources4
Beta strandi298 – 303Combined sources6
Beta strandi305 – 307Combined sources3
Beta strandi310 – 315Combined sources6
Beta strandi320 – 324Combined sources5
Helixi325 – 327Combined sources3
Helixi334 – 337Combined sources4
Beta strandi344 – 348Combined sources5
Beta strandi355 – 360Combined sources6
Beta strandi362 – 364Combined sources3
Beta strandi367 – 372Combined sources6
Beta strandi375 – 382Combined sources8
Turni387 – 389Combined sources3

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati116 – 147WD 1Add BLAST32
Repeati158 – 189WD 2Add BLAST32
Repeati206 – 237WD 3Add BLAST32
Repeati249 – 280WD 4Add BLAST32
Repeati293 – 324WD 5Add BLAST32
Repeati350 – 381WD 6Add BLAST32

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni335 – 339Interaction with the histone H4 N-terminus1 Publication5

Sequence similaritiesi

Contains 6 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

GeneTreeiENSGT00570000079069.
HOGENOMiHOG000160330.
InParanoidiP39984.
KOiK10752.
OMAiFEAHDDV.
OrthoDBiEOG092C4MBO.

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. 1 hit.
[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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4PSWX-ray2.10B7-390[»]
4PSXX-ray2.51B/E8-389[»]
ProteinModelPortaliP39984.
SMRiP39984.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36673. 68 interactors.
DIPiDIP-2363N.
IntActiP39984. 7 interactors.
MINTiMINT-654148.

Proteomic databases

MaxQBiP39984.
PRIDEiP39984.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YEL056W.
SGDiS000000782. HAT2.

Phylogenomic databases

GeneTreeiENSGT00570000079069.
HOGENOMiHOG000160330.
InParanoidiP39984.
KOiK10752.
OMAiFEAHDDV.
OrthoDBiEOG092C4MBO.

Enzyme and pathway databases

BioCyciYEAST:G3O-30174-MONOMER.
ReactomeiR-SCE-3214847. HATs acetylate histones.
R-SCE-3214858. RMTs methylate histone arginines.
R-SCE-349425. Autodegradation of the E3 ubiquitin ligase COP1.

Miscellaneous databases

PROiP39984.

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. 1 hit.
[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...

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: November 2, 2016
This is version 162 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

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 one 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.