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Protein

Protein EAP1

Gene

EAP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Can regulate translation through binding to eIF4E. Competes with eIF4G and p20 for binding to eIF4E in vivo and inhibits cap-dependent translation in vitro. Plays a role in cell growth and is implicated in the TOR signaling cascade. Functions independently of eIF4E to maintain genetic stability and to attenuate GCN4 translation upon TOR inactivation.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi440 – 4478ATPSequence Analysis

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • eukaryotic initiation factor 4E binding Source: UniProtKB

GO - Biological processi

  • deadenylation-dependent decapping of nuclear-transcribed mRNA Source: SGD
  • mRNA catabolic process Source: SGD
  • negative regulation of translation Source: SGD
  • regulation of growth Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Growth regulation, Translation regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-31963-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein EAP1
Alternative name(s):
eIF4E-associated protein 1
Gene namesi
Name:EAP1
Ordered Locus Names:YKL204W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XI

Organism-specific databases

CYGDiYKL204w.
EuPathDBiFungiDB:YKL204W.
SGDiS000001687. EAP1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic stress granule Source: SGD
  • mRNA cap binding complex Source: SGD
  • polysome Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi109 – 1091Y → A: Abolishes interaction with eIF4E; when associated with A-114. 2 Publications
Mutagenesisi114 – 1141L → A: Abolishes interaction with eIF4E; when associated with A-109. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 632632Protein EAP1PRO_0000203133Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei30 – 301Phosphoserine1 Publication
Modified residuei281 – 2811Phosphoserine1 Publication
Modified residuei282 – 2821Phosphoserine2 Publications
Modified residuei327 – 3271Phosphoserine2 Publications
Modified residuei344 – 3441Phosphoserine1 Publication
Modified residuei387 – 3871Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP36041.
PaxDbiP36041.
PeptideAtlasiP36041.

Interactioni

Subunit structurei

Interacts with SMY2, SYH1 and eIF4E.2 Publications

Protein-protein interaction databases

BioGridi33919. 70 interactions.
DIPiDIP-1778N.
IntActiP36041. 11 interactions.
MINTiMINT-394822.
STRINGi4932.YKL204W.

Structurei

3D structure databases

ProteinModelPortaliP36041.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiNOG12793.
InParanoidiP36041.
KOiK15908.
OMAiNDERRMS.
OrthoDBiEOG7J18CB.

Sequencei

Sequence statusi: Complete.

P36041-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELNDPSIIS SSQFSGELSD SDTAAATHKS QQAISNLFQK LAKKGREEKP
60 70 80 90 100
IGSVESSTDS SNISVATSGN NKESNKKKNK KTAMLNFSSL TDPITNYKPM
110 120 130 140 150
DLQYKTYAYS MNELYHLKPS LASASYEEDP LISELVRSLP KRKFWRLRMG
160 170 180 190 200
PPDQKHANNH HFNGNNGGGS WKAGYKNGKN DERRMSRTKN MQGGKRRSQQ
210 220 230 240 250
DDEEKKIDQE MLEMDKNLQL GGDVGHSIAD FEDWKAKMKE LELKKLSKSK
260 270 280 290 300
GISNSTAIAP RESASHETPT DLRPVIPRGP SSITDFLNLK RQDKKEESSQ
310 320 330 340 350
QTPGIPVGQP SLSKTSIEQV NELETNSDLG KSSSSRFSSF FNKSATSLPS
360 370 380 390 400
LDNNNQVPSS NVSVVNNDGN STPHQSGSRL MSFFKESRSS TPNAESQLLS
410 420 430 440 450
ASDKDNGKMQ TLPQFQQQPQ QMQPMAFTQH PPNNNAFFNG LLNKGKSETS
460 470 480 490 500
TPPPPPPGLI AHQGPQFPVM GVPPNFPQRM MPPPPGLVQF QKDSKDVNKK
510 520 530 540 550
EDRQLRQNKN PNGTRNSKGK QEETATPDLP QQQYMPPPPP PGFFPMHPNF
560 570 580 590 600
PNGPMPPLPQ GFPIPPNGML PVTGQQPQPP YPNMMLQGNF PPNFQQGFGS
610 620 630
NSPMPIPSII NANGKNVTNQ LPPGLNSKKN IK
Length:632
Mass (Da):69,762
Last modified:June 1, 1994 - v1
Checksum:i775F73F57BB0EF2B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z28204 Genomic DNA. Translation: CAA82049.1.
BK006944 Genomic DNA. Translation: DAA08965.1.
PIRiS38042.
RefSeqiNP_012718.1. NM_001179769.1.

Genome annotation databases

EnsemblFungiiYKL204W; YKL204W; YKL204W.
GeneIDi853631.
KEGGisce:YKL204W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z28204 Genomic DNA. Translation: CAA82049.1.
BK006944 Genomic DNA. Translation: DAA08965.1.
PIRiS38042.
RefSeqiNP_012718.1. NM_001179769.1.

3D structure databases

ProteinModelPortaliP36041.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33919. 70 interactions.
DIPiDIP-1778N.
IntActiP36041. 11 interactions.
MINTiMINT-394822.
STRINGi4932.YKL204W.

Proteomic databases

MaxQBiP36041.
PaxDbiP36041.
PeptideAtlasiP36041.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYKL204W; YKL204W; YKL204W.
GeneIDi853631.
KEGGisce:YKL204W.

Organism-specific databases

CYGDiYKL204w.
EuPathDBiFungiDB:YKL204W.
SGDiS000001687. EAP1.

Phylogenomic databases

eggNOGiNOG12793.
InParanoidiP36041.
KOiK15908.
OMAiNDERRMS.
OrthoDBiEOG7J18CB.

Enzyme and pathway databases

BioCyciYEAST:G3O-31963-MONOMER.

Miscellaneous databases

NextBioi974508.
PROiP36041.

Family and domain databases

ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete DNA sequence of yeast chromosome XI."
    Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
    , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
    Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "Yeast Eap1p, an eIF4E-associated protein, has a separate function involving genetic stability."
    Chial H.J., Stemm-Wolf A.J., McBratney S., Winey M.
    Curr. Biol. 10:1519-1522(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "Eap1p, a novel eukaryotic translation initiation factor 4E-associated protein in Saccharomyces cerevisiae."
    Cosentino G.P., Schmelzle T., Haghighat A., Helliwell S.B., Hall M.N., Sonenberg N.
    Mol. Cell. Biol. 20:4604-4613(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EIF4E, MUTAGENESIS OF TYR-109.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "The yeast eIF4E-associated protein Eap1p attenuates GCN4 translation upon TOR-inactivation."
    Matsuo R., Kubota H., Obata T., Kito K., Ota K., Kitazono T., Ibayashi S., Sasaki T., Iida M., Ito T.
    FEBS Lett. 579:2433-2438(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF TYR-109 AND LEU-114.
  8. "GYF domain proteomics reveals interaction sites in known and novel target proteins."
    Kofler M., Motzny K., Freund C.
    Mol. Cell. Proteomics 4:1797-1811(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SMY2 AND SYH1.
  9. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  10. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-281; SER-282; SER-327; SER-344 AND SER-387, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282 AND SER-327, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiEAP1_YEAST
AccessioniPrimary (citable) accession number: P36041
Secondary accession number(s): D6VWZ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: June 24, 2015
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 3240 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.