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Description:
Enhancer of polycomb-like protein 1.
Molecular weight: 96738
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-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
07-MAR-2006, entry version 32.
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 EPL1_YEAST:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | D50617 | BAA09214.1 | - |
| PIR | S56230 | S56230. | |
| IntAct | P43572 | -.1 | |
| GermOnline | 140131 | -.1 | |
| Ensembl | YFL024C | Saccharomyces cerevisiae.1 | |
| GenomeReviews | D50617_GR | YFL024C.1 | |
| SGD | S000001870 | EPL1. | |
| BioCyc | SCER-S28-01:SCER-S28-01-001895-MONOMER | -.1 | |
| LinkHub | P43572 | -.1 | |
| GO | GO:0043189 | C:H4/H2A histone acetyltransferase complex | IPI. |
| GO | GO:0004402 | F:histone acetyltransferase activity | IDA. |
| GO | GO:0016573 | P:histone acetylation | IDA. |
| GO | GO:0006357 | P:regulation of transcription from RNA polyme... | IDA. |
Keywords:
Cell cycle; 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=95400292; PubMed=7670463;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M.,
RA Sasanuma S., Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K.,
RA Yamazaki M., Tashiro H., Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from
RT Saccharomyces cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
RN [2]
RP PROTEIN SEQUENCE OF 2-16; 86-96; 101-116; 136-149; 151-178; 227-235;
RP 275-280; 283-296; 346-367; 381-407; 471-491; 497-512; 529-569;
RP 575-587; 594-600; 605-612; 617-632; 653-698; 711-721; 729-740; 772-794
RP AND 811-821, IDENTIFICATION IN THE NUA4 COMPLEX, AND FUNCTION.
RX PubMed=10911987; DOI=10.1016/S1097-2765(00)80258-0;
RA Galarneau L., Nourani A., Boudreault A.A., Zhang Y., Heliot L.,
RA Allard S., Savard J., Lane W.S., Stillman D.J., Cote J.;
RT "Multiple links between the NuA4 histone acetyltransferase complex and
RT epigenetic control of transcription.";
RL Mol. Cell 5:927-937(2000).
RN [3]
RP GENE NAME.
RX MEDLINE=98407961; PubMed=9735366;
RA Stankunas K., Berger J., Ruse C., Sinclair D.A.R., Randazzo F.,
RA Brock H.W.;
RT "The enhancer of polycomb gene of Drosophila encodes a chromatin
RT protein conserved in yeast and mammals.";
RL Development 125:4055-4066(1998).
RN [4]
RP FUNCTION, IDENTIFICATION IN THE NUA4 COMPLEX, AND MASS SPECTROMETRY.
RX PubMed=12782659; DOI=10.1101/gad.1056603;
RA Boudreault A.A., Cronier D., Selleck W., Lacoste N., Utley R.T.,
RA Allard S., Savard J., Lane W.S., Tan S., Cote J.;
RT "Yeast enhancer of polycomb defines global Esa1-dependent acetylation
RT of chromatin.";
RL Genes Dev. 17:1415-1428(2003).
RN [5]
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 [6]
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 [7]
RP FUNCTION.
RX PubMed=14966276; DOI=10.1128/MCB.24.5.1956-1967.2004;
RA Oki M., Valenzuela L., Chiba T., Ito T., Kamakaka R.T.;
RT "Barrier proteins remodel and modify chromatin to restrict silenced
RT domains.";
RL Mol. Cell. Biol. 24:1956-1967(2004).
RN [8]
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 [9]
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 [10]
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 1 832 Enhancer of polycomb-like protein 1.
/FTId=PRO_0000214167.
COMPBIAS 419 428 Poly-Ala.
COMPBIAS 447 451 Poly-Gln.
COMPBIAS 454 461 Poly-Gln.
COMPBIAS 476 481 Poly-Ser.
COMPBIAS 777 795 Poly-Gln.
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. Involved in gene
silencing by neighboring heterochromatin, blockage of the
silencing spreading along the chromosome, and required for cell
cycle progression through G2/M.
-!- 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 1110 molecules/cell.
-!- SIMILARITY: Belongs to the enhancer of polycomb family.
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Sequence length: 832
MPTPSNAIEI NDGSHKSGRS TRRSGSRSAH DDGLDSFSKG DSGAGASAGS SNSRFRHRKI
SVKQHLKIYL PNDLKHLDKD ELQQREVVEI ETGVEKNEEK EVHLHRILQM GSGHTKHKDY
IPTPDASMTW NEYDKFYTGS FQETTSYIKF SATVEDCCGT NYNMDERDET FLNEQVNKGS
SDILTEDEFE ILCSSFEHAI HERQPFLSMD PESILSFEEL KPTLIKSDMA DFNLRNQLNH
EINSHKTHFI TQFDPVSQMN TRPLIQLIEK FGSKIYDYWR ERKIEVNGYE IFPQLKFERP
GEKEEIDPYV CFRRREVRHP RKTRRIDILN SQRLRALHQE LKNAKDLALL VAKRENVSLN
WINDELKIFD QRVKIKNLKR SLNISGEDDD LINHKRKRPT IVTVEQREAE LRKAELKRAA
AAAAAAKAKN NKRNNQLEDK SSRLTKQQQQ QLLQQQQQQQ QNALKTENGK QLANASSSST
SQPITSHVYV KLPSSKIPDI VLEDVDALLN SKEKNARKFV QEKMEKRKIE DADVFFNLTD
DPFNPVFDMS LPKNFSTSNV PFASIASSKF QIDRSFYSSH LPEYLKGISD DIRIYDSNGR
SRNKDNYNLD TKRIKKTELY DPFQENLEIH SREYPIKFRK RVGRSNIKYV DRMPNFTTSS
TKSACSLMDF VDFDSIEKEQ YSREGSNDTD SINVYDSKYD EFVRLYDKWK YDSPQNEYGI
KFSDEPARLN QISNDTQVIR FGTMLGTKSY EQLREATIKY RRDYITRLKQ KHIQHLQQQQ
QQQQQQQQQA QQQKQKSQNN NSNSSNSLKK LNDSLINSEA KQNSSITQKN SS