P36041 (EAP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein EAP1

Alternative name(s):
eIF4E-associated protein 1

Gene names

Name:	EAP1
Ordered Locus Names:	YKL204W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	632 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.3 Ref.4 Ref.7
Subunit structure	Interacts with SMY2, SYH1 and eIF4E. Ref.4 Ref.9
Subcellular location	Cytoplasm Ref.5.
Miscellaneous	Present with 3240 molecules/cell in log phase SD medium. Ref.6

Ontologies

Keywords
Biological process	Growth regulation Translation regulation
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	negative regulation of translation Inferred from direct assay Ref.4. Source: SGD regulation of growth Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasmic stress granule Inferred from direct assay. Source: SGD mRNA cap binding complex Inferred from physical interaction Ref.4. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW eukaryotic initiation factor 4E binding Inferred from physical interaction Ref.4. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 632	632	Protein EAP1		PRO_0000203133
Regions
	Nucleotide binding	440 – 447	8	ATP Potential
Amino acid modifications
	Modified residue	30	1	Phosphoserine Ref.12
	Modified residue	281	1	Phosphoserine Ref.8 Ref.11 Ref.12
	Modified residue	282	1	Phosphoserine Ref.11 Ref.12
	Modified residue	315	1	Phosphothreonine Ref.12
	Modified residue	325	1	Phosphothreonine Ref.12
	Modified residue	327	1	Phosphoserine Ref.12
	Modified residue	338	1	Phosphoserine Ref.10
	Modified residue	344	1	Phosphoserine Ref.11 Ref.12
	Modified residue	346	1	Phosphothreonine Ref.11
	Modified residue	387	1	Phosphoserine Ref.12
	Modified residue	390	1	Phosphoserine Ref.11
	Modified residue	391	1	Phosphothreonine Ref.12
Experimental info
	Mutagenesis	109	1	Y → A: Abolishes interaction with eIF4E; when associated with A-114. Ref.4 Ref.7
	Mutagenesis	114	1	L → A: Abolishes interaction with eIF4E; when associated with A-109. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	P36041 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 775F73F57BB0EF2B	FASTA	632	69,762
	10 20 30 40 50 60 MELNDPSIIS SSQFSGELSD SDTAAATHKS QQAISNLFQK LAKKGREEKP IGSVESSTDS 70 80 90 100 110 120 SNISVATSGN NKESNKKKNK KTAMLNFSSL TDPITNYKPM DLQYKTYAYS MNELYHLKPS 130 140 150 160 170 180 LASASYEEDP LISELVRSLP KRKFWRLRMG PPDQKHANNH HFNGNNGGGS WKAGYKNGKN 190 200 210 220 230 240 DERRMSRTKN MQGGKRRSQQ DDEEKKIDQE MLEMDKNLQL GGDVGHSIAD FEDWKAKMKE 250 260 270 280 290 300 LELKKLSKSK GISNSTAIAP RESASHETPT DLRPVIPRGP SSITDFLNLK RQDKKEESSQ 310 320 330 340 350 360 QTPGIPVGQP SLSKTSIEQV NELETNSDLG KSSSSRFSSF FNKSATSLPS LDNNNQVPSS 370 380 390 400 410 420 NVSVVNNDGN STPHQSGSRL MSFFKESRSS TPNAESQLLS ASDKDNGKMQ TLPQFQQQPQ 430 440 450 460 470 480 QMQPMAFTQH PPNNNAFFNG LLNKGKSETS TPPPPPPGLI AHQGPQFPVM GVPPNFPQRM 490 500 510 520 530 540 MPPPPGLVQF QKDSKDVNKK EDRQLRQNKN PNGTRNSKGK QEETATPDLP QQQYMPPPPP 550 560 570 580 590 600 PGFFPMHPNF PNGPMPPLPQ GFPIPPNGML PVTGQQPQPP YPNMMLQGNF PPNFQQGFGS 610 620 630 NSPMPIPSII NANGKNVTNQ LPPGLNSKKN IK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8196765] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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: 11114520] [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: 10848587] [Abstract] Cited for: FUNCTION, INTERACTION WITH EIF4E, MUTAGENESIS OF TYR-109.
[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]	"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: 15848184] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF TYR-109 AND LEU-114.
[8]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281, MASS SPECTROMETRY. Strain: YAL6B.
[9]	"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: 16120600] [Abstract] Cited for: INTERACTION WITH SMY2 AND SYH1.
[10]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338, 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-281; SER-282; SER-344; THR-346 AND SER-390, MASS SPECTROMETRY.
[12]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-281; SER-282; THR-315; THR-325; SER-327; SER-344; SER-387 AND THR-391, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z28204 Genomic DNA. Translation: CAA82049.1. BK006944 Genomic DNA. Translation: DAA08965.1.
PIR	S38042.
RefSeq	NP_012718.1. NM_001179769.1.
3D structure databases
ProteinModelPortal	P36041.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1778N.
IntAct	P36041. 12 interactions.
MINT	MINT-394822.
STRING	P36041.
Proteomic databases
PeptideAtlas	P36041.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YKL204W; YKL204W; YKL204W.
GeneID	853631.
KEGG	sce:YKL204W.
NMPDR	fig|4932.3.peg.3696.
Organism-specific databases
CYGD	YKL204w.
SGD	S000001687. EAP1.
Phylogenomic databases
eggNOG	fuNOG11951.
OMA	RESASHE.
OrthoDB	EOG415KQ6.
Gene expression databases
ArrayExpress	P36041.
Genevestigator	P36041.
GermOnline	YKL204W. Saccharomyces cerevisiae.
Family and domain databases
ProtoNet	Search...
Other
NextBio	974508.

Entry information

Entry name

EAP1_YEAST

Accession

Primary (citable) accession number: P36041
Secondary accession number(s): D6VWZ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	December 14, 2011
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program