Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P39984 (HAT2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone acetyltransferase type B subunit 2
Gene names
Name:HAT2
Ordered Locus Names:YEL056W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length401 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.7 Ref.8 Ref.9

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. Ref.7 Ref.8

Subcellular location

Cytoplasm. Nucleus. Note: The nuclear location requires the presence of HAT2. Ref.7 Ref.8

Induction

Repressed in presence of farnesol, probably through a intracellular decrease of diacylglycerol. Ref.5

Sequence similarities

Belongs to the WD repeat RBAP46/RBAP48/MSI1 family.

Contains 6 WD repeats.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HAT1Q123415EBI-8185,EBI-8176
HIF1Q123733EBI-8185,EBI-31911

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 401401Histone acetyltransferase type B subunit 2
PRO_0000051014

Regions

Repeat116 – 14732WD 1
Repeat158 – 18932WD 2
Repeat206 – 23732WD 3
Repeat249 – 28032WD 4
Repeat293 – 32432WD 5
Repeat350 – 38132WD 6

Sequences

Sequence LengthMass (Da)Tools
P39984 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: C27A91C99D9FCAB7

FASTA40145,060
        10         20         30         40         50         60 
MENQEKPLSV DEEYDLWKSN VPLMYDFVSE TRLTWPSLTV QWLPTPVQEL DGGFIKQELI 

        70         80         90        100        110        120 
IGTHTSGEEE NYLKFAEINL PKEILSNEDP QEEAGEEYQS SLPAPRSNIR ITAKYEHEEE 

       130        140        150        160        170        180 
ITRARYMPQD PNIVATINGQ GTVFLYSRSE GLQSTLKFHK DNGYALSFST LVKGRLLSGS 

       190        200        210        220        230        240 
DDHTVALWEV GSGGDPTKPV RTWNDLHSDI INDNKWHNFN KDLFGTVSED SLLKINDVRA 

       250        260        270        280        290        300 
NNTTIDTVKC PQPFNTLAFS HHSSNLLAAA GMDSYVYLYD LRNMKEPLHH MSGHEDAVNN 

       310        320        330        340        350        360 
LEFSTHVDGV VVSSGSDNRL MMWDLKQIGA EQTPDDAEDG VPELIMVHAG HRSSVNDFDL 

       370        380        390        400 
NPQIPWLVAS AEEENILQVW KCSHSLPIVG GPPKVNKDII S 

« Hide

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] [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]"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. expand/collapse author list , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.
Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U18795 Genomic DNA. Translation: AAB65031.1.
BK006939 Genomic DNA. Translation: DAA07598.1.
PIRS50533.
RefSeqNP_010858.3. NM_001178871.3.

3D structure databases

ProteinModelPortalP39984.
SMRP39984. Positions 10-386.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36673. 68 interactions.
DIPDIP-2363N.
IntActP39984. 7 interactions.
MINTMINT-654148.
STRING4932.YEL056W.

Proteomic databases

MaxQBP39984.
PaxDbP39984.
PeptideAtlasP39984.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYEL056W; YEL056W; YEL056W.
GeneID856654.
KEGGsce:YEL056W.

Organism-specific databases

CYGDYEL056w.
SGDS000000782. HAT2.

Phylogenomic databases

eggNOGCOG2319.
GeneTreeENSGT00570000079069.
HOGENOMHOG000160330.
KOK10752.
OMAVLYDLVI.
OrthoDBEOG7D865N.

Enzyme and pathway databases

BioCycYEAST:G3O-30174-MONOMER.

Gene expression databases

GenevestigatorP39984.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR022052. Histone-bd_RBBP4_N.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamPF12265. CAF1C_H4-bd. 1 hit.
PF00400. WD40. 2 hits.
[Graphical view]
SMARTSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
PROSITEPS00678. WD_REPEATS_1. 2 hits.
PS50082. WD_REPEATS_2. 2 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio982637.
PROP39984.

Entry information

Entry nameHAT2_YEAST
AccessionPrimary (citable) accession number: P39984
Secondary accession number(s): D3DLJ4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 9, 2014
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome V

Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families