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Protein

Chromatin modification-related protein EAF3

Gene

EAF3

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

Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair.3 Publications

GO - Biological processi

  • DNA repair Source: SGD
  • histone acetylation Source: SGD
  • histone deacetylation Source: SGD
  • negative regulation of antisense RNA transcription Source: SGD
  • negative regulation of transcription, DNA-templated Source: SGD
  • regulation of DNA-dependent DNA replication initiation Source: SGD
  • regulation of transcription from RNA polymerase II promoter Source: SGD
  • transcription elongation from RNA polymerase II promoter Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

DNA damage, DNA repair, Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-34183-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Chromatin modification-related protein EAF3
Alternative name(s):
ESA1-associated factor 3
Gene namesi
Name:EAF3
Ordered Locus Names:YPR023C
ORF Names:YP9367.03C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPR023C.
SGDiS000006227. EAF3.

Subcellular locationi

GO - Cellular componenti

  • histone acetyltransferase complex Source: SGD
  • NuA4 histone acetyltransferase complex Source: SGD
  • Rpd3S complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 401401Chromatin modification-related protein EAF3PRO_0000088783Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei201 – 2011PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ12432.
PeptideAtlasiQ12432.

PTM databases

iPTMnetiQ12432.

Interactioni

Subunit structurei

Component of the NuA4 histone acetyltransferase complex composed of at least ACT1, ARP4, YAF9, VID21, SWC4, EAF3, EAF5, EAF6, EAF7, EPL1, ESA1, TRA1 and YNG2.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ESA1Q0864912EBI-6281,EBI-6648
SIN3P225799EBI-6281,EBI-17160

Protein-protein interaction databases

BioGridi36200. 254 interactions.
DIPiDIP-2871N.
IntActiQ12432. 39 interactions.
MINTiMINT-663128.

Structurei

Secondary structure

1
401
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 64Combined sources
Beta strandi13 – 186Combined sources
Beta strandi21 – 3212Combined sources
Turni33 – 364Combined sources
Beta strandi37 – 404Combined sources
Beta strandi47 – 504Combined sources
Beta strandi54 – 563Combined sources
Turni69 – 735Combined sources
Beta strandi76 – 816Combined sources
Helixi86 – 883Combined sources
Beta strandi90 – 923Combined sources
Turni94 – 963Combined sources
Beta strandi97 – 1004Combined sources
Helixi102 – 11312Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K3XNMR-A1-113[»]
2K3YNMR-A1-115[»]
3E9FX-ray1.80A1-113[»]
3E9GX-ray2.50A/B1-124[»]
ProteinModelPortaliQ12432.
SMRiQ12432. Positions 1-113, 220-378.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12432.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini216 – 399184MRGPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi148 – 20558Ser-richAdd
BLAST

Sequence similaritiesi

Belongs to the MRG family.Curated
Contains 1 MRG domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00530000063018.
HOGENOMiHOG000190863.
InParanoidiQ12432.
KOiK11339.
OMAiRPYNDEN.
OrthoDBiEOG7B31XP.

Family and domain databases

InterProiIPR000953. Chromo/shadow_dom.
IPR016197. Chromodomain-like.
IPR008676. MRG.
IPR026541. MRG_dom.
IPR025995. Tudor-knot.
[Graphical view]
PANTHERiPTHR10880. PTHR10880. 3 hits.
PfamiPF05712. MRG. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]
SMARTiSM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 3 hits.
PROSITEiPS51640. MRG. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q12432-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVDLEQEFAL GGRCLAFHGP LMYEAKILKI WDPSSKMYTS IPNDKPGGSS
60 70 80 90 100
QATKEIKPQK LGEDESIPEE IINGKCFFIH YQGWKSSWDE WVGYDRIRAY
110 120 130 140 150
NEENIAMKKR LANEAKEAKK SLLEQQKKKK LSTSLGGPSN GGKRKGDSRS
160 170 180 190 200
NASISKSTSQ SFLTSSVSGR KSGRSSANSL HPGSSLRSSS DQNGNDDRRR
210 220 230 240 250
SSSLSPNMLH HIAGYPTPKI SLQIPIKLKS VLVDDWEYVT KDKKICRLPA
260 270 280 290 300
DVTVEMVLNK YEHEVSQELE SPGSQSQLSE YCAGLKLYFD KCLGNMLLYR
310 320 330 340 350
LERLQYDELL KKSSKDQKPL VPIRIYGAIH LLRLISVLPE LISSTTMDLQ
360 370 380 390 400
SCQLLIKQTE DFLVWLLMHV DEYFNDKDPN RSDDALYVNT SSQYEGVALG

M
Length:401
Mass (Da):45,203
Last modified:November 1, 1996 - v1
Checksum:i63758DE9510D70DC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z71255 Genomic DNA. Translation: CAA95019.1.
Z49274 Genomic DNA. Translation: CAA89277.1.
BK006949 Genomic DNA. Translation: DAA11449.1.
PIRiS54497.
RefSeqiNP_015348.1. NM_001184120.1.

Genome annotation databases

EnsemblFungiiYPR023C; YPR023C; YPR023C.
GeneIDi856134.
KEGGisce:YPR023C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z71255 Genomic DNA. Translation: CAA95019.1.
Z49274 Genomic DNA. Translation: CAA89277.1.
BK006949 Genomic DNA. Translation: DAA11449.1.
PIRiS54497.
RefSeqiNP_015348.1. NM_001184120.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K3XNMR-A1-113[»]
2K3YNMR-A1-115[»]
3E9FX-ray1.80A1-113[»]
3E9GX-ray2.50A/B1-124[»]
ProteinModelPortaliQ12432.
SMRiQ12432. Positions 1-113, 220-378.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36200. 254 interactions.
DIPiDIP-2871N.
IntActiQ12432. 39 interactions.
MINTiMINT-663128.

PTM databases

iPTMnetiQ12432.

Proteomic databases

MaxQBiQ12432.
PeptideAtlasiQ12432.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPR023C; YPR023C; YPR023C.
GeneIDi856134.
KEGGisce:YPR023C.

Organism-specific databases

EuPathDBiFungiDB:YPR023C.
SGDiS000006227. EAF3.

Phylogenomic databases

GeneTreeiENSGT00530000063018.
HOGENOMiHOG000190863.
InParanoidiQ12432.
KOiK11339.
OMAiRPYNDEN.
OrthoDBiEOG7B31XP.

Enzyme and pathway databases

BioCyciYEAST:G3O-34183-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ12432.
NextBioi981233.
PROiQ12432.

Family and domain databases

InterProiIPR000953. Chromo/shadow_dom.
IPR016197. Chromodomain-like.
IPR008676. MRG.
IPR026541. MRG_dom.
IPR025995. Tudor-knot.
[Graphical view]
PANTHERiPTHR10880. PTHR10880. 3 hits.
PfamiPF05712. MRG. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]
SMARTiSM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 3 hits.
PROSITEiPS51640. MRG. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
    , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
    Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "The yeast NuA4 and Drosophila MSL complexes contain homologous subunits important for transcriptional regulation."
    Eisen A., Utley R.T., Nourani A., Allard S., Schmidt P., Lane W.S., Lucchesi J.C., Cote J.
    J. Biol. Chem. 276:3484-3491(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-13; 37-54; 61-75; 86-96; 121-127; 131-143; 157-170; 175-187; 201-227; 230-241; 248-260; 304-311 AND 316-333, IDENTIFICATION IN THE NUA4 COMPLEX, FUNCTION.
  4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "Eaf3 regulates the global pattern of histone acetylation in Saccharomyces cerevisiae."
    Reid J.L., Moqtaderi Z., Struhl K.
    Mol. Cell. Biol. 24:757-764(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "The Yaf9 component of the SWR1 and NuA4 complexes is required for proper gene expression, histone H4 acetylation, and Htz1 replacement near telomeres."
    Zhang H., Richardson D.O., Roberts D.N., Utley R.T., Erdjument-Bromage H., Tempst P., Cote J., Cairns B.R.
    Mol. Cell. Biol. 24:9424-9436(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE NUA4 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  8. "A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p deposits histone variant H2A.Z into euchromatin."
    Kobor M.S., Venkatasubrahmanyam S., Meneghini M.D., Gin J.W., Jennings J.L., Link A.J., Madhani H.D., Rine J.
    PLoS Biol. 2:587-599(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE NUA4 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  9. "Regulation of chromosome stability by the histone H2A variant Htz1, the Swr1 chromatin remodeling complex, and the histone acetyltransferase NuA4."
    Krogan N.J., Baetz K., Keogh M.-C., Datta N., Sawa C., Kwok T.C.Y., Thompson N.J., Davey M.G., Pootoolal J., Hughes T.R., Emili A., Buratowski S., Hieter P., Greenblatt J.F.
    Proc. Natl. Acad. Sci. U.S.A. 101:13513-13518(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE NUA4 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  10. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiEAF3_YEAST
AccessioniPrimary (citable) accession number: Q12432
Secondary accession number(s): D6W433
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1890 molecules/cell in log phase SD medium.1 Publication

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 XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: 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.