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Protein

Chromatin modification-related protein EAF1

Gene

EAF1

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.2 Publications

GO - Molecular functioni

GO - Biological processi

  • cellular protein complex assembly Source: SGD
  • chromatin modification Source: SGD
  • DNA repair Source: SGD
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator

Keywords - Biological processi

DNA damage, DNA repair, Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-29910-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Chromatin modification-related protein EAF1
Alternative name(s):
ESA1-associated factor 1
Vacuolar import and degradation protein 21
Gene namesi
Name:EAF1
Synonyms:VID21
Ordered Locus Names:YDR359C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR359C.
SGDiS000002767. EAF1.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 982982Chromatin modification-related protein EAF1PRO_0000065825Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei841 – 8411PhosphoserineCombined sources
Modified residuei971 – 9711PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ06337.
PeptideAtlasiQ06337.

PTM databases

iPTMnetiQ06337.

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 YNG2.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ESA1Q086497EBI-35867,EBI-6648
SWC4P532014EBI-35867,EBI-23061
YAF9P539302EBI-35867,EBI-28841

Protein-protein interaction databases

BioGridi32415. 465 interactions.
DIPiDIP-6330N.
IntActiQ06337. 26 interactions.
MINTiMINT-600777.

Structurei

3D structure databases

ProteinModelPortaliQ06337.
SMRiQ06337. Positions 649-704.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini346 – 42580HSAPROSITE-ProRule annotationAdd
BLAST
Domaini642 – 70463Myb-likePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi825 – 942118Gln-richAdd
BLAST

Sequence similaritiesi

Belongs to the EAF1 family.Curated
Contains 1 HSA domain.PROSITE-ProRule annotation
Contains 1 Myb-like domain.PROSITE-ProRule annotation

Phylogenomic databases

InParanoidiQ06337.
KOiK11397.
OMAiNRRNHYL.
OrthoDBiEOG7RBZHR.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
InterProiIPR009057. Homeodomain-like.
IPR014012. HSA_dom.
IPR017877. Myb-like_dom.
IPR001005. SANT/Myb.
[Graphical view]
PfamiPF07529. HSA. 1 hit.
[Graphical view]
SMARTiSM00573. HSA. 1 hit.
SM00717. SANT. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.
PROSITEiPS51204. HSA. 1 hit.
PS50090. MYB_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q06337-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSRPSSAVP NSASLSEDQS SDRSKFPKAD DLIDERDRKL TELYCVSRLN
60 70 80 90 100
QLLELTDENK LRKEIDAFLK KNDIRRGIRF DEASLPKLLH TAATPITKKK
110 120 130 140 150
LKDVNLINVP NQRLSDSKMS RELPENSENV SVKSESHFVP SHDNSIRENM
160 170 180 190 200
MDSLRPAEKT GGMWNKRPLE STMGGEEERH EKRQKMQSQS LESSNNSEMA
210 220 230 240 250
SLPISPRPPV PNALAHYTYY ENIEYPPADP TEVQPAVKFK DPLIKNIMAK
260 270 280 290 300
EIDTSDHYNE NNVDALETVF LLMNDYIPSK IPQALPLAEL KYMSQTLPLI
310 320 330 340 350
NLIPRAHKAL TTNIINNALN EARITVVGSR IEELRRLGLW SLRQPKRFID
360 370 380 390 400
PWKQHNTHQN ILLEEAKWMQ ADFKEGHKYK VAICTAMAQA IKDYWTYGEI
410 420 430 440 450
CCVKRKTLLP GKENKLSDDG RISEKSGRPS DTSRNDSDIS IAGKDDIGII
460 470 480 490 500
ANVDDITEKE SAAANDNDEN GKNEAGAKSD FDFADGLLSQ EGAHDQIISS
510 520 530 540 550
IDTKLLLKKP SSSSEVVLIQ HEVAASSALI ETEESKKELA PPFKLSIFVD
560 570 580 590 600
ELNTFEKTLI QDLPLYNGIN EERPKKDDSL PFIPISKSVV SLDDNGFYKL
610 620 630 640 650
LERQLIDEEP SISQLSKRRG MFYGNRRNHY LRPPAVPSLR YLQNRTPTIW
660 670 680 690 700
LSEDDQELVK NINTYGYNWE LISAHMTHRL TYSYLSNIER RTPWQCFERF
710 720 730 740 750
VQLNERFNFS DLKGPRAHSA QQWLIEAHKF QQRQNRRISP LGVNTESIQR
760 770 780 790 800
GHRRLRWASM FEAIRKCMKK RENTPRPNPT QPRKPLDCKN MKVPTPAEMS
810 820 830 840 850
LLKAQRDEAL RRDIQLRRTV KNRLQQRQQQ SQQAHSSRAQ SPIPSNGKSS
860 870 880 890 900
SNLARNGQAS APRPNQKQYT EQDIIESYSR KLLEQKPDIG PEMALKAAKN
910 920 930 940 950
YYRTLREQQQ QLKQHQIQQQ RQQLQEESSH VQQLQQLQPG SQAPPPKSSP
960 970 980
SQSSLSNISN INSAPRIKSP TPQEILQRFQ KQ
Length:982
Mass (Da):112,502
Last modified:August 30, 2005 - v2
Checksum:i75F0C9594EF4ED8D
GO

Sequence cautioni

The sequence AAB64794.1 differs from that shown. Reason: Frameshift at position 942. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY464182 Genomic DNA. Translation: AAR27935.1.
AY464183 Genomic DNA. Translation: AAR27936.1.
U28372 Genomic DNA. Translation: AAB64794.1. Frameshift.
BK006938 Genomic DNA. Translation: DAA12198.1.
PIRiS61155.
RefSeqiNP_010646.4. NM_001180667.3.

Genome annotation databases

EnsemblFungiiYDR359C; YDR359C; YDR359C.
GeneIDi851962.
KEGGisce:YDR359C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY464182 Genomic DNA. Translation: AAR27935.1.
AY464183 Genomic DNA. Translation: AAR27936.1.
U28372 Genomic DNA. Translation: AAB64794.1. Frameshift.
BK006938 Genomic DNA. Translation: DAA12198.1.
PIRiS61155.
RefSeqiNP_010646.4. NM_001180667.3.

3D structure databases

ProteinModelPortaliQ06337.
SMRiQ06337. Positions 649-704.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32415. 465 interactions.
DIPiDIP-6330N.
IntActiQ06337. 26 interactions.
MINTiMINT-600777.

PTM databases

iPTMnetiQ06337.

Proteomic databases

MaxQBiQ06337.
PeptideAtlasiQ06337.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR359C; YDR359C; YDR359C.
GeneIDi851962.
KEGGisce:YDR359C.

Organism-specific databases

EuPathDBiFungiDB:YDR359C.
SGDiS000002767. EAF1.

Phylogenomic databases

InParanoidiQ06337.
KOiK11397.
OMAiNRRNHYL.
OrthoDBiEOG7RBZHR.

Enzyme and pathway databases

BioCyciYEAST:G3O-29910-MONOMER.

Miscellaneous databases

NextBioi970071.
PROiQ06337.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
InterProiIPR009057. Homeodomain-like.
IPR014012. HSA_dom.
IPR017877. Myb-like_dom.
IPR001005. SANT/Myb.
[Graphical view]
PfamiPF07529. HSA. 1 hit.
[Graphical view]
SMARTiSM00573. HSA. 1 hit.
SM00717. SANT. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.
PROSITEiPS51204. HSA. 1 hit.
PS50090. MYB_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Auger A., Galarneau L., Cote J.
    Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 200060 / W303 and ATCC 201388 / BY4741.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: FUNCTION.
  5. "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.
  6. "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.
  7. "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.
  8. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-841 AND THR-971, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiEAF1_YEAST
AccessioniPrimary (citable) accession number: Q06337
Secondary accession number(s): D6VSY8, Q6S6F6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: August 30, 2005
Last modified: May 11, 2016
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: 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.