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P43572 (EPL1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Enhancer of polycomb-like protein 1
Gene names
Name:EPL1
Ordered Locus Names:YFL024C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length832 AA.
Sequence statusComplete.
Protein existenceEvidence 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.3 Ref.5 Ref.8 Ref.10

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. Ref.3 Ref.5 Ref.9 Ref.10 Ref.11

Subcellular location

Nucleus Ref.6.

Miscellaneous

Present with 1110 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the enhancer of polycomb family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

YNG2P388064EBI-22792,EBI-24622

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 832832Enhancer of polycomb-like protein 1
PRO_0000214167

Regions

Compositional bias419 – 42810Poly-Ala
Compositional bias447 – 4515Poly-Gln
Compositional bias454 – 4618Poly-Gln
Compositional bias476 – 4816Poly-Ser
Compositional bias777 – 79519Poly-Gln

Amino acid modifications

Modified residue421Phosphoserine Ref.12
Modified residue511Phosphoserine Ref.12

Sequences

Sequence LengthMass (Da)Tools
P43572 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: E08689465F84ABA8

FASTA83296,738
        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 

« Hide

References

« Hide '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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"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] [Europe PMC] [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.
[4]"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] [Europe PMC] [Abstract]
Cited for: GENE NAME.
[5]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE NUA4 COMPLEX, MASS SPECTROMETRY.
[6]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]"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] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE NUA4 COMPLEX, MASS SPECTROMETRY.
[10]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE NUA4 COMPLEX, MASS SPECTROMETRY.
[11]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE NUA4 COMPLEX, MASS SPECTROMETRY.
[12]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 AND SER-51, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D50617 Genomic DNA. Translation: BAA09214.1.
BK006940 Genomic DNA. Translation: DAA12416.1.
PIRS56230.
RefSeqNP_116629.1. NM_001179942.1.

3D structure databases

ProteinModelPortalP43572.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-5904N.
IntActP43572. 29 interactions.
MINTMINT-624154.
STRING4932.YFL024C.

Proteomic databases

PaxDbP43572.
PeptideAtlasP43572.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYFL024C; YFL024C; YFL024C.
GeneID850520.
KEGGsce:YFL024C.

Organism-specific databases

CYGDYFL024c.
SGDS000001870. EPL1.

Phylogenomic databases

eggNOGNOG304124.
GeneTreeENSGT00390000013262.
HOGENOMHOG000094341.
KOK11322.
OMAFRQRKIS.
OrthoDBEOG45TGWG.

Gene expression databases

GenevestigatorP43572.
GermOnlineYFL024C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR024943. Enhancer_polycomb.
IPR019542. Enhancer_polycomb-like_N.
[Graphical view]
PANTHERPTHR14898. PTHR14898. 1 hit.
PfamPF10513. EPL1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio966251.

Entry information

Entry nameEPL1_YEAST
AccessionPrimary (citable) accession number: P43572
Secondary accession number(s): D6VTK6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 1, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome VI

Yeast (Saccharomyces cerevisiae) chromosome VI: entries and gene names

SIMILARITY comments

Index of protein domains and families