Chromatin modification-related protein EAF3 - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot Q12432 (EAF3_YEAST)

Last modified June 16, 2009. Version 75. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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 (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	401 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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.2 Ref.5 Ref.7
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.3
Miscellaneous	Present with 1890 molecules/cell in log phase SD medium. Ref.4
Sequence similarities	Belongs to the MRG family.

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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
Gene Ontology (GO)
Biological process	DNA repair Inferred from direct assay. Source: SGD chromatin assembly or disassembly Inferred from electronic annotation. Source: InterPro histone acetylation Ref.2 Inferred from direct assay. Source: SGD histone deacetylation Inferred from direct assay. Source: SGD negative regulation of transcription, DNA-dependent Inferred from mutant phenotype. Source: SGD negative regulation of transposition, RNA-mediated Inferred from mutant phenotype. Source: SGD regulation of transcription from RNA polymerase II promoter Ref.2 Inferred from mutant phenotype. Source: SGD transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	NuA4 histone acetyltransferase complex Ref.6 Inferred from physical interaction. Source: SGD Rpd3/Clr6 histone deacetylase complex II' Inferred from direct assay. Source: SGD
Molecular function	chromatin binding Inferred from electronic annotation. Source: InterPro histone acetyltransferase activity Ref.2 Inferred from direct assay. Source: SGD protein binding Ref.2 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
ESA1	Q08649	2	EBI-6281,EBI-6648

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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.10

Modified residue

Phosphoserine Ref.10 Ref.9

Modified residue

157

Phosphoserine Ref.10

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Sequences

Sequence

Length

Mass (Da)

Tools

Q12432-1 [UniParc].

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

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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]	"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.
[3]	"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].
[4]	"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].
[5]	"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.
[6]	"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.
[7]	"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.
[8]	"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.
[9]	"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.
[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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-50 AND SER-157, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

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

PIR

S54497.

RefSeq

NP_015348.1.

3D structure databases

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	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:2871N.

IntAct

Q12432. 30 interactions.

Proteomic databases

PeptideAtlas

Q12432.

Genome annotation databases

Ensembl

YPR023C. Saccharomyces cerevisiae. [Contig view]

GeneID

856134.

GenomeReviews

Gene locus YPR023C in contig U00094_GR.

KEGG

sce:YPR023C.

NMPDR

fig|4932.3.peg.6483.

Organism-specific databases

CYGD

YPR023c.

SGD

S000006227. EAF3.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

Q12432.

OMA

Q12432. IHYQGWK.

Gene expression databases

ArrayExpress

Q12432.

GermOnline

YPR023C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR000953. Chromodomain.
IPR008676. MRG.
[Graphical view]

PANTHER

PTHR10880. MRG. 1 hit.

Pfam

PF05712. MRG. 1 hit.
[Graphical view]

SMART

SM00298. CHROMO. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

981233.

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Entry information

Entry name

EAF3_YEAST

Accession

Primary (citable) accession number: Q12432

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Yeast

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

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

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents