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Protein data for EAF3_YEAST:

Description:
Chromatin modification-related protein EAF3 (ESA1-associated factor3).

Molecular weight: 45203

View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):

DNA repair( GO:0006281 )


Important dates:
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
07-MAR-2006, entry version 45.

Phylogenetic order:
Eukaryota Fungi Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces.

To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html

Links to references in other databases for protein EAF3_YEAST:

DatabasePointerAdd. info#1Add. info#2
EMBLZ71255CAA95019.1-
EMBLZ49274CAA89277.1-
PIRS54497S54497.
IntActQ12432-.1
GermOnline144288-.1
EnsemblYPR023CSaccharomyces cerevisiae.1
GenomeReviewsU00094_GRYPR023C.1
SGDS000006227EAF3.
BioCycSCER-S28-01:SCER-S28-01-006168-MONOMER-.1
LinkHubQ12432-.1
GOGO:0043189C:H4/H2A histone acetyltransferase complexIPI.
GOGO:0004402F:histone acetyltransferase activityIDA.
GOGO:0005515F:protein bindingIPI.
GOGO:0016573P:histone acetylationIDA.
GOGO:0006357P:regulation of transcription from RNA polyme...IMP.
InterProIPR000953Chromo.
InterProIPR008676MRG.
PANTHERPTHR10880MRG.11.
PfamPF05712MRG1.
SMARTSM00298CHROMO1.

General information about the databases mentioned above

Keywords:
Chromatin regulator; Complete proteome; Direct protein sequencing; DNA damage; DNA repair; Nuclear protein; Transcription; Transcription regulation.

References:
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S288c / AB972;
RX MEDLINE=97313271; PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V.,
RA Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M.,
RA Chung E., Churcher C.M., Coster F., Davis K., Davis R.W.,
RA Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A.,
RA Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A.,
RA Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W.,
RA Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K.,
RA Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J.,
RA Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D.,
RA Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V.,
RA Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W.,
RA Zollner A., Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
RP PROTEIN SEQUENCE OF 2-13; 37-54; 61-75; 86-96; 121-127; 131-143;
RP 157-170; 175-187; 201-227; 230-241; 248-260; 304-311 AND 316-333,
RP IDENTIFICATION IN THE NUA4 COMPLEX, AND FUNCTION.
RX PubMed=11036083; DOI=10.1074/jbc.M008159200;
RA Eisen A., Utley R.T., Nourani A., Allard S., Schmidt P., Lane W.S.,
RA Lucchesi J.C., Cote J.;
RT "The yeast NuA4 and Drosophila MSL complexes contain homologous
RT subunits important for transcriptional regulation.";
RL J. Biol. Chem. 276:3483-3491(2001).
RN [3]
RP SUBCELLULAR LOCATION.
RX MEDLINE=22923954; PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION.
RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA Dephoure N., O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP FUNCTION.
RX PubMed=14701747; DOI=10.1128/MCB.24.2.757-764.2004;
RA Reid J.L., Moqtaderi Z., Struhl K.;
RT "Eaf3 regulates the global pattern of histone acetylation in
RT Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 24:757-764(2004).
RN [6]
RP IDENTIFICATION IN THE NUA4 COMPLEX, AND MASS SPECTROMETRY.
RX PubMed=15485911; DOI=10.1128/MCB.24.21.9424-9436.2004;
RA Zhang H., Richardson D.O., Roberts D.N., Utley R.T.,
RA Erdjument-Bromage H., Tempst P., Cote J., Cairns B.R.;
RT "The Yaf9 component of the SWR1 and NuA4 complexes is required for
RT proper gene expression, histone H4 acetylation, and Htz1 replacement
RT near telomeres.";
RL Mol. Cell. Biol. 24:9424-9436(2004).
RN [7]
RP FUNCTION, IDENTIFICATION IN THE NUA4 COMPLEX, AND MASS SPECTROMETRY.
RX PubMed=15045029; DOI=10.1371/journal.pbio.0020131;
RA Kobor M.S., Venkatasubrahmanyam S., Meneghini M.D., Gin J.W.,
RA Jennings J.L., Link A.J., Madhani H.D., Rine J.;
RT "A protein complex containing the conserved Swi2/Snf2-related ATPase
RT Swr1p deposits histone variant H2A.Z into euchromatin.";
RL PLoS Biol. 2:E131-E131(2004).
RN [8]
RP IDENTIFICATION IN THE NUA4 COMPLEX, AND MASS SPECTROMETRY.
RX PubMed=15353583; DOI=10.1073/pnas.0405753101;
RA Krogan N.J., Baetz K., Keogh M.-C., Datta N., Sawa C., Kwok T.C.Y.,
RA Thompson N.J., Davey M.G., Pootoolal J., Hughes T.R., Emili A.,
RA Buratowski S., Hieter P., Greenblatt J.F.;
RT "Regulation of chromosome stability by the histone H2A variant Htz1,
RT the Swr1 chromatin remodeling complex, and the histone
RT acetyltransferase NuA4.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13513-13518(2004).

Feature:
CHAIN 1 401 Chromatin modification-related protein
EAF3.
/FTId=PRO_0000088783.
COMPBIAS 148 205 Ser-rich.

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.
-!- SUBUNIT: 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.
-!- INTERACTION:
Q08649:ESA1; NbExp=2; IntAct=EBI-6281, EBI-6648;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- MISCELLANEOUS: Present with 1890 molecules/cell.
-!- SIMILARITY: Belongs to the MRG family.
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Sequence length: 401

     MVDLEQEFAL GGRCLAFHGP LMYEAKILKI WDPSSKMYTS IPNDKPGGSS QATKEIKPQK
     LGEDESIPEE IINGKCFFIH YQGWKSSWDE WVGYDRIRAY NEENIAMKKR LANEAKEAKK
     SLLEQQKKKK LSTSLGGPSN GGKRKGDSRS NASISKSTSQ SFLTSSVSGR KSGRSSANSL
     HPGSSLRSSS DQNGNDDRRR SSSLSPNMLH HIAGYPTPKI SLQIPIKLKS VLVDDWEYVT
     KDKKICRLPA DVTVEMVLNK YEHEVSQELE SPGSQSQLSE YCAGLKLYFD KCLGNMLLYR
     LERLQYDELL KKSSKDQKPL VPIRIYGAIH LLRLISVLPE LISSTTMDLQ SCQLLIKQTE
     DFLVWLLMHV DEYFNDKDPN RSDDALYVNT SSQYEGVALG M

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