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Protein data for EAF5_YEAST:

Description:
Chromatin modification-related protein EAF5 (ESA1-associated factor5).

Molecular weight: 31644

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:
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
07-MAR-2006, entry version 30.

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 EAF5_YEAST:

DatabasePointerAdd. info#1Add. info#2
EMBLU18530AAB64495.1-
PIRS50441S50441.
IntActP39995-.1
GermOnline139022-.1
EnsemblYEL018WSaccharomyces cerevisiae.1
GenomeReviewsU00092_GRYEL018W.1
SGDS000000744EAF5.
BioCycSCER-S28-01:SCER-S28-01-001595-MONOMER-.1
LinkHubP39995-.1
GOGO:0043189C:H4/H2A histone acetyltransferase complexIPI.
GOGO:0005634C:nucleusIDA.
GOGO:0005515F:protein bindingIPI.

General information about the databases mentioned above

Keywords:
Chromatin regulator; Complete proteome; 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=97313264; PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G.,
RA Hunicke-Smith S., Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H.,
RA Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P.,
RA Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T.,
RA Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [2]
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 [3]
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 [4]
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 [5]
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 1 279 Chromatin modification-related protein
EAF5.
/FTId=PRO_0000086892.

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:
P21264:ADE2; NbExp=1; IntAct=EBI-22312, EBI-14252;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- MISCELLANEOUS: Present with 937 molecules/cell.
-!- SIMILARITY: Belongs to the EAF5 family.
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Sequence length: 279

     MDKEVSELVV LQLIHTLISN KNEELVRNGG GINMIGNNLR ISLVKLTNEI QNNLLINELT
     NLRRQSNVAN GNRKLGINDI LTIVKNLFPE YRTTLNDGQL SLHGLEMHDI EKLLDEKYDR
     FKKTQVEQIR MMEDEILKNG IKTGASQLQP HANAGKSGSA GTSATITTTT PHMAHSMDPK
     REKLLKLYRD TVLNKLESKT GNFQKLFKSP DGSIIKNEIN YEDIKNETPG SVHELQLILQ
     KSITDGVMRK VIGTDDWKLA RQVQFELDDT VQFMRRALE

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