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Description:
Chromatin modification-related protein EAF7 (ESA1-associated factor7).
Molecular weight: 49391
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-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, 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 EAF7_YEAST:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | Z46843 | CAA86889.1 | - |
| EMBL | Z71412 | CAA96018.1 | - |
| PIR | S55147 | S55147. | |
| IntAct | P53911 | -.1 | |
| GermOnline | 143142 | -.1 | |
| Ensembl | YNL136W | Saccharomyces cerevisiae.1 | |
| GenomeReviews | Y13139_GR | YNL136W.1 | |
| SGD | S000005080 | YNL136W. | |
| BioCyc | SCER-S28-01:SCER-S28-01-004992-MONOMER | -.1 | |
| LinkHub | P53911 | -.1 | |
| GO | GO:0043189 | C:H4/H2A histone acetyltransferase complex | IPI. |
| GO | GO:0005634 | C:nucleus | IDA. |
| GO | GO:0016573 | P:histone acetylation | IPI. |
| GO | GO:0006357 | P:regulation of transcription from RNA polyme... | IMP. |
| InterPro | IPR012423 | CT20. | |
| Pfam | PF07904 | CT20 | 1. |
Keywords:
Chromatin regulator; Coiled coil; Complete proteome; DNA damage; DNA repair; Nuclear protein; Transcription; Transcription regulation.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S288c;
RX MEDLINE=96109932; PubMed=8619318;
RA Mallet L., Bussereau F., Jacquet M.;
RT "A 43.5 kb segment of yeast chromosome XIV, which contains MFA2, MEP2,
RT CAP/SRV2, NAM9, FKB1/FPR1/RBP1, MOM22 and CPT1, predicts an adenosine
RT deaminase gene and 14 new open reading frames.";
RL Yeast 11:1195-1209(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S288c / FY1679;
RX MEDLINE=97313269; PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F.,
RA Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M.,
RA Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N.,
RA Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D.,
RA Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A.,
RA Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A.,
RA Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C.,
RA Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M.,
RA Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J.,
RA Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L.,
RA Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M.,
RA Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P.,
RA Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A.,
RA Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV
RT and its evolutionary implications.";
RL Nature 387:93-98(1997).
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 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 1 425 Chromatin modification-related protein
EAF7.
/FTId=PRO_0000215882.
COILED 209 310 Potential.
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.
-!- SUBCELLULAR LOCATION: Nucleus.
-!- MISCELLANEOUS: Present with 300 molecules/cell.
-!- SIMILARITY: Belongs to the EAF7 family.
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Sequence length: 425
MVVHWTIVDE IRLLRWASEF KPAGIHKHFH MFCIVERMNS PDKYPVTLLQ KETMKLGKVF
TAKDIWDKLS QSYNLEKIDE MENTYSLEAT TESSRNGNGN GDDAEIHEET LLELNNRIRV
RKQDFTLPWE EYGELILENA RKSPNSNEEY PRVEDMNEKD STIPKESPST DLKNDNNKQE
KNATIKVKEL PEYHTEENDS PIDVQKEPIK EVQSDEKELQ REHMSEEEQK MKSTNKTAAP
VRKSQRLKRS KEVKFEDEEK EEIEEDNTKD EEQKEKKEEI QEPKITHNEE VDKEKNENEE
GDDEREKSTS YENTNGSESE GVDEGVDEEL GYESEREAEG KGKQIESEGG NLKKKTENKK
GDDQQDDTKK DSKDKNEPLA KRTRHSSSTG NTSNETSPKR KRRKAGSRKN SPPATRVSSR
LRNKK