Chromatin modification-related protein EAF3 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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Q12432 (EAF3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 102. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Chromatin modification-related protein EAF3

Alternative name(s):
ESA1-associated factor 3

Gene names

Name:	EAF3
Ordered Locus Names:	YPR023C
ORF Names:	YP9367.03C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	401 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.3 Ref.6 Ref.8
Subunit structure	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.
Subcellular location	Nucleus Ref.4.
Miscellaneous	Present with 1890 molecules/cell in log phase SD medium. Ref.5
Sequence similarities	Belongs to the MRG family.

Ontologies

Keywords
Biological process	DNA damage DNA repair Transcription Transcription regulation
Cellular component	Nucleus
Molecular function	Chromatin regulator
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	DNA repair Inferred from direct assay. Source: SGD histone deacetylation Inferred from mutant phenotype. Source: SGD negative regulation of antisense RNA transcription Inferred from mutant phenotype. Source: SGD regulation of DNA-dependent DNA replication initiation Inferred from mutant phenotype. Source: SGD regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype Ref.3. Source: SGD transcription elongation from RNA polymerase II promoter Inferred from genetic interaction. Source: SGD
Cellular component	NuA4 histone acetyltransferase complex Inferred from physical interaction Ref.7. Source: SGD Rpd3L complex Inferred from direct assay. Source: SGD Rpd3S complex Inferred from direct assay. Source: SGD
Molecular function	histone acetyltransferase activity Inferred from direct assay Ref.3. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ESA1	Q08649	11	EBI-6281,EBI-6648

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 401

401

Chromatin modification-related protein EAF3

PRO_0000088783

Regions

Compositional bias

148 – 205

Ser-rich

Amino acid modifications

Modified residue

Phosphoserine Ref.11

Modified residue

Phosphoserine Ref.10 Ref.11

Modified residue

157

Phosphoserine Ref.11

Secondary structure

401

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q12432 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 63758DE9510D70DC
Show »

FASTA

401

45,203

        10         20         30         40         50         60 
MVDLEQEFAL GGRCLAFHGP LMYEAKILKI WDPSSKMYTS IPNDKPGGSS QATKEIKPQK 

        70         80         90        100        110        120 
LGEDESIPEE IINGKCFFIH YQGWKSSWDE WVGYDRIRAY NEENIAMKKR LANEAKEAKK 

       130        140        150        160        170        180 
SLLEQQKKKK LSTSLGGPSN GGKRKGDSRS NASISKSTSQ SFLTSSVSGR KSGRSSANSL 

       190        200        210        220        230        240 
HPGSSLRSSS DQNGNDDRRR SSSLSPNMLH HIAGYPTPKI SLQIPIKLKS VLVDDWEYVT 

       250        260        270        280        290        300 
KDKKICRLPA DVTVEMVLNK YEHEVSQELE SPGSQSQLSE YCAGLKLYFD KCLGNMLLYR 

       310        320        330        340        350        360 
LERLQYDELL KKSSKDQKPL VPIRIYGAIH LLRLISVLPE LISSTTMDLQ SCQLLIKQTE 

       370        380        390        400 
DFLVWLLMHV DEYFNDKDPN RSDDALYVNT SSQYEGVALG M

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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. Hani J. Nature 387:103-105(1997) [PubMed: 9169875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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: 11036083] [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]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[5]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] 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: 14701747] [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: 15485911] [Abstract] Cited for: IDENTIFICATION IN THE NUA4 COMPLEX, 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: 15045029] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE NUA4 COMPLEX, 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: 15353583] [Abstract] Cited for: IDENTIFICATION IN THE NUA4 COMPLEX, MASS SPECTROMETRY.
[10]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, MASS SPECTROMETRY.
[11]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-50 AND SER-157, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z71255 Genomic DNA. Translation: CAA95019.1.
Z49274 Genomic DNA. Translation: CAA89277.1.
BK006949 Genomic DNA. Translation: DAA11449.1.

PIR

S54497.

RefSeq

NP_015348.1. NM_001184120.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2K3X	NMR	-	A	1-113	[»]
2K3Y	NMR	-	A	1-115	[»]
3E9F	X-ray	1.80	A	1-113	[»]
3E9G	X-ray	2.50	A/B	1-124	[»]

ProteinModelPortal

Q12432.

SMR

Q12432. Positions 1-113, 220-397.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2871N.

IntAct

Q12432. 36 interactions.

MINT

MINT-663128.

STRING

Q12432.

Proteomic databases

PeptideAtlas

Q12432.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YPR023C; YPR023C; YPR023C.

GeneID

856134.

KEGG

sce:YPR023C.

NMPDR

fig|4932.3.peg.6483.

Organism-specific databases

CYGD

YPR023c.

SGD

S000006227. EAF3.

Phylogenomic databases

eggNOG

fuNOG10518.

GeneTree

EFGT00050000004743.

HOGENOM

HBG396389.

OMA

NEENIAM.

OrthoDB

EOG496329.

Gene expression databases

ArrayExpress

Q12432.

Genevestigator

Q12432.

GermOnline

YPR023C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR008676. MRG.
[Graphical view]

K11339.

PANTHER

PTHR10880. MRG. 1 hit.

Pfam

PF05712. MRG. 1 hit.
[Graphical view]

SMART

SM00298. CHROMO. 1 hit.
[Graphical view]

SUPFAM

SSF54160. Chromodomain-like. 1 hit.

ProtoNet

Search...

Other

NextBio

981233.

Entry information

Entry name

EAF3_YEAST

Accession

Primary (citable) accession number: Q12432
Secondary accession number(s): D6W433

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1996
Last modified:	December 14, 2011
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents