Reviewed, UniProtKB/Swiss-Prot P43572 (EPL1_YEAST)

Names and origin

Protein names

Recommended name:
    Enhancer of polycomb-like protein 1

Gene names

Name:	EPL1
Ordered Locus Names:	YFL024C

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	832 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (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. Ref.2 Ref.4 Ref.7 Ref.9
Subunit structure	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. Ref.5
Miscellaneous	Present with 1110 molecules/cell in log phase SD medium. Ref.6
Sequence similarities	Belongs to the enhancer of polycomb family.

Ontologies

Keywords
Biological process	Cell cycle DNA damage DNA repair Transcription Transcription regulation
Cellular component	Nucleus
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	DNA repair Inferred from direct assay. Source: SGD cell cycle Inferred from electronic annotation. Source: UniProtKB-KW histone acetylation Ref.2 Inferred from direct assay. Source: SGD regulation of transcription from RNA polymerase II promoter Ref.2 Inferred from direct assay. Source: SGD transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	NuA4 histone acetyltransferase complex Ref.8 Inferred from physical interaction. Source: SGD Piccolo NuA4 histone acetyltransferase complex Ref.4 Inferred from direct assay. Source: SGD
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	P38800	1	EBI-22792,EBI-24597

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 832	832	Enhancer of polycomb-like protein 1		PRO_0000214167
Regions
	Compositional bias	419 – 428	10	Poly-Ala
	Compositional bias	447 – 451	5	Poly-Gln
	Compositional bias	454 – 461	8	Poly-Gln
	Compositional bias	476 – 481	6	Poly-Ser
	Compositional bias	777 – 795	19	Poly-Gln
Amino acid modifications
	Modified residue	42	1	Phosphoserine Ref.11
	Modified residue	51	1	Phosphoserine Ref.11

Sequences

	Sequence		Length	Mass (Da)
	P43572-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: E08689465F84ABA8	FASTA	832	96,738
	10 20 30 40 50 60 MPTPSNAIEI NDGSHKSGRS TRRSGSRSAH DDGLDSFSKG DSGAGASAGS SNSRFRHRKI 70 80 90 100 110 120 SVKQHLKIYL PNDLKHLDKD ELQQREVVEI ETGVEKNEEK EVHLHRILQM GSGHTKHKDY 130 140 150 160 170 180 IPTPDASMTW NEYDKFYTGS FQETTSYIKF SATVEDCCGT NYNMDERDET FLNEQVNKGS 190 200 210 220 230 240 SDILTEDEFE ILCSSFEHAI HERQPFLSMD PESILSFEEL KPTLIKSDMA DFNLRNQLNH 250 260 270 280 290 300 EINSHKTHFI TQFDPVSQMN TRPLIQLIEK FGSKIYDYWR ERKIEVNGYE IFPQLKFERP 310 320 330 340 350 360 GEKEEIDPYV CFRRREVRHP RKTRRIDILN SQRLRALHQE LKNAKDLALL VAKRENVSLN 370 380 390 400 410 420 WINDELKIFD QRVKIKNLKR SLNISGEDDD LINHKRKRPT IVTVEQREAE LRKAELKRAA 430 440 450 460 470 480 AAAAAAKAKN NKRNNQLEDK SSRLTKQQQQ QLLQQQQQQQ QNALKTENGK QLANASSSST 490 500 510 520 530 540 SQPITSHVYV KLPSSKIPDI VLEDVDALLN SKEKNARKFV QEKMEKRKIE DADVFFNLTD 550 560 570 580 590 600 DPFNPVFDMS LPKNFSTSNV PFASIASSKF QIDRSFYSSH LPEYLKGISD DIRIYDSNGR 610 620 630 640 650 660 SRNKDNYNLD TKRIKKTELY DPFQENLEIH SREYPIKFRK RVGRSNIKYV DRMPNFTTSS 670 680 690 700 710 720 TKSACSLMDF VDFDSIEKEQ YSREGSNDTD SINVYDSKYD EFVRLYDKWK YDSPQNEYGI 730 740 750 760 770 780 KFSDEPARLN QISNDTQVIR FGTMLGTKSY EQLREATIKY RRDYITRLKQ KHIQHLQQQQ 790 800 810 820 830 QQQQQQQQQA QQQKQKSQNN NSNSSNSLKK LNDSLINSEA KQNSSITQKN SS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of the nucleotide sequence of chromosome VI from Saccharomyces cerevisiae." Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S., Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H., Eki T. Nat. Genet. 10:261-268(1995) [PubMed: 7670463] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	"Multiple links between the NuA4 histone acetyltransferase complex and epigenetic control of transcription." Galarneau L., Nourani A., Boudreault A.A., Zhang Y., Heliot L., Allard S., Savard J., Lane W.S., Stillman D.J., Cote J. Mol. Cell 5:927-937(2000) [PubMed: 10911987] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-16; 86-96; 101-116; 136-149; 151-178; 227-235; 275-280; 283-296; 346-367; 381-407; 471-491; 497-512; 529-569; 575-587; 594-600; 605-612; 617-632; 653-698; 711-721; 729-740; 772-794 AND 811-821, IDENTIFICATION IN THE NUA4 COMPLEX, FUNCTION.
[3]	"The enhancer of polycomb gene of Drosophila encodes a chromatin protein conserved in yeast and mammals." Stankunas K., Berger J., Ruse C., Sinclair D.A.R., Randazzo F., Brock H.W. Development 125:4055-4066(1998) [PubMed: 9735366] [Abstract] Cited for: GENE NAME.
[4]	"Yeast enhancer of polycomb defines global Esa1-dependent acetylation of chromatin." Boudreault A.A., Cronier D., Selleck W., Lacoste N., Utley R.T., Allard S., Savard J., Lane W.S., Tan S., Cote J. Genes Dev. 17:1415-1428(2003) [PubMed: 12782659] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE NUA4 COMPLEX, MASS SPECTROMETRY.
[5]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"Barrier proteins remodel and modify chromatin to restrict silenced domains." Oki M., Valenzuela L., Chiba T., Ito T., Kamakaka R.T. Mol. Cell. Biol. 24:1956-1967(2004) [PubMed: 14966276] [Abstract] Cited for: FUNCTION.
[8]	"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: 15485911] [Abstract] Cited for: IDENTIFICATION IN THE NUA4 COMPLEX, MASS SPECTROMETRY.
[9]	"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: 15045029] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE NUA4 COMPLEX, MASS SPECTROMETRY.
[10]	"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: 15353583] [Abstract] Cited for: IDENTIFICATION IN THE NUA4 COMPLEX, MASS SPECTROMETRY.
[11]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 AND SER-51, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D50617 Genomic DNA. Translation: BAA09214.1.
PIR	S56230.
RefSeq	NP_116629.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:5904N.
IntAct	P43572. 26 interactions.
STRING	P43572.
Proteomic databases
PeptideAtlas	P43572.
PRIDE	P43572.
Genome annotation databases
Ensembl	YFL024C; YFL024C; YFL024C; Saccharomyces cerevisiae. [Genome view]
GeneID	850520.
GenomeReviews	Gene locus YFL024C in contig D50617_GR.
KEGG	sce:YFL024C.
NMPDR	fig|4932.3.peg.2256.
Organism-specific databases
CYGD	YFL024c.
SGD	S000001870. EPL1.
Phylogenomic databases
HOGENOM	P43572.
OMA	IPTPDAS.
Gene expression databases
ArrayExpress	P43572.
Genevestigator	P43572.
GermOnline	YFL024C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR019542. Enhancer_of_polycomb-like. [Graphical view]
Pfam	PF10513. EPL1. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	966251.

Entry information

Entry name

EPL1_YEAST

Accession

Primary (citable) accession number: P43572

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	November 3, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)