ID   EAP1_YEAST              Reviewed;         632 AA.
AC   P36041; D6VWZ9;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   27-MAR-2024, entry version 163.
DE   RecName: Full=Protein EAP1;
DE   AltName: Full=eIF4E-associated protein 1;
GN   Name=EAP1; OrderedLocusNames=YKL204W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA   Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA   von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA   Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(1994).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   FUNCTION.
RX   PubMed=11114520; DOI=10.1016/s0960-9822(00)00829-0;
RA   Chial H.J., Stemm-Wolf A.J., McBratney S., Winey M.;
RT   "Yeast Eap1p, an eIF4E-associated protein, has a separate function
RT   involving genetic stability.";
RL   Curr. Biol. 10:1519-1522(2000).
RN   [4]
RP   FUNCTION, INTERACTION WITH EIF4E, AND MUTAGENESIS OF TYR-109.
RX   PubMed=10848587; DOI=10.1128/mcb.20.13.4604-4613.2000;
RA   Cosentino G.P., Schmelzle T., Haghighat A., Helliwell S.B., Hall M.N.,
RA   Sonenberg N.;
RT   "Eap1p, a novel eukaryotic translation initiation factor 4E-associated
RT   protein in Saccharomyces cerevisiae.";
RL   Mol. Cell. Biol. 20:4604-4613(2000).
RN   [5]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   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 [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   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, AND MUTAGENESIS OF TYR-109 AND LEU-114.
RX   PubMed=15848184; DOI=10.1016/j.febslet.2005.03.043;
RA   Matsuo R., Kubota H., Obata T., Kito K., Ota K., Kitazono T., Ibayashi S.,
RA   Sasaki T., Iida M., Ito T.;
RT   "The yeast eIF4E-associated protein Eap1p attenuates GCN4 translation upon
RT   TOR-inactivation.";
RL   FEBS Lett. 579:2433-2438(2005).
RN   [8]
RP   INTERACTION WITH SMY2 AND SYH1.
RX   PubMed=16120600; DOI=10.1074/mcp.m500129-mcp200;
RA   Kofler M., Motzny K., Freund C.;
RT   "GYF domain proteomics reveals interaction sites in known and novel target
RT   proteins.";
RL   Mol. Cell. Proteomics 4:1797-1811(2005).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-281; SER-282;
RP   SER-327; SER-344 AND SER-387, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282 AND SER-327, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: Can regulate translation through binding to eIF4E. Competes
CC       with eIF4G and p20 for binding to eIF4E in vivo and inhibits cap-
CC       dependent translation in vitro. Plays a role in cell growth and is
CC       implicated in the TOR signaling cascade. Functions independently of
CC       eIF4E to maintain genetic stability and to attenuate GCN4 translation
CC       upon TOR inactivation. {ECO:0000269|PubMed:10848587,
CC       ECO:0000269|PubMed:11114520, ECO:0000269|PubMed:15848184}.
CC   -!- SUBUNIT: Interacts with SMY2, SYH1 and eIF4E.
CC       {ECO:0000269|PubMed:10848587, ECO:0000269|PubMed:16120600}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 3240 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; Z28204; CAA82049.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA08965.1; -; Genomic_DNA.
DR   PIR; S38042; S38042.
DR   RefSeq; NP_012718.1; NM_001179769.1.
DR   PDB; 6FC1; X-ray; 1.35 A; B/D=91-150.
DR   PDB; 6FC2; X-ray; 1.92 A; B/D=91-150.
DR   PDBsum; 6FC1; -.
DR   PDBsum; 6FC2; -.
DR   AlphaFoldDB; P36041; -.
DR   SMR; P36041; -.
DR   BioGRID; 33919; 506.
DR   DIP; DIP-1778N; -.
DR   IntAct; P36041; 13.
DR   MINT; P36041; -.
DR   STRING; 4932.YKL204W; -.
DR   GlyGen; P36041; 20 sites, 1 O-linked glycan (20 sites).
DR   iPTMnet; P36041; -.
DR   MaxQB; P36041; -.
DR   PaxDb; 4932-YKL204W; -.
DR   PeptideAtlas; P36041; -.
DR   EnsemblFungi; YKL204W_mRNA; YKL204W; YKL204W.
DR   GeneID; 853631; -.
DR   KEGG; sce:YKL204W; -.
DR   AGR; SGD:S000001687; -.
DR   SGD; S000001687; EAP1.
DR   VEuPathDB; FungiDB:YKL204W; -.
DR   eggNOG; ENOG502S0PT; Eukaryota.
DR   HOGENOM; CLU_418607_0_0_1; -.
DR   InParanoid; P36041; -.
DR   OMA; HANNHHF; -.
DR   OrthoDB; 2014218at2759; -.
DR   BioCyc; YEAST:G3O-31963-MONOMER; -.
DR   BioGRID-ORCS; 853631; 2 hits in 10 CRISPR screens.
DR   PRO; PR:P36041; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P36041; Protein.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008190; F:eukaryotic initiation factor 4E binding; IDA:SGD.
DR   GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR   GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IMP:SGD.
DR   GO; GO:0006402; P:mRNA catabolic process; IMP:SGD.
DR   GO; GO:0017148; P:negative regulation of translation; IDA:SGD.
DR   InterPro; IPR046784; Eap1.
DR   Pfam; PF20566; Eap1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cytoplasm; Growth regulation;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Translation regulation.
FT   CHAIN           1..632
FT                   /note="Protein EAP1"
FT                   /id="PRO_0000203133"
FT   REGION          1..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          149..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          248..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          347..378
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          429..541
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          587..632
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..72
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..204
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..263
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..313
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..448
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        470..484
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        493..508
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        509..530
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         440..447
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         30
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         281
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         282
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         327
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         344
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         387
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MUTAGEN         109
FT                   /note="Y->A: Abolishes interaction with eIF4E; when
FT                   associated with A-114."
FT                   /evidence="ECO:0000269|PubMed:10848587,
FT                   ECO:0000269|PubMed:15848184"
FT   MUTAGEN         114
FT                   /note="L->A: Abolishes interaction with eIF4E; when
FT                   associated with A-109."
FT                   /evidence="ECO:0000269|PubMed:15848184"
FT   HELIX           93..96
FT                   /evidence="ECO:0007829|PDB:6FC1"
FT   HELIX           111..116
FT                   /evidence="ECO:0007829|PDB:6FC1"
FT   HELIX           122..124
FT                   /evidence="ECO:0007829|PDB:6FC1"
FT   TURN            125..127
FT                   /evidence="ECO:0007829|PDB:6FC1"
FT   HELIX           130..137
FT                   /evidence="ECO:0007829|PDB:6FC1"
FT   HELIX           142..145
FT                   /evidence="ECO:0007829|PDB:6FC1"
FT   HELIX           147..149
FT                   /evidence="ECO:0007829|PDB:6FC2"
SQ   SEQUENCE   632 AA;  69762 MW;  775F73F57BB0EF2B CRC64;
     MELNDPSIIS SSQFSGELSD SDTAAATHKS QQAISNLFQK LAKKGREEKP IGSVESSTDS
     SNISVATSGN NKESNKKKNK KTAMLNFSSL TDPITNYKPM DLQYKTYAYS MNELYHLKPS
     LASASYEEDP LISELVRSLP KRKFWRLRMG PPDQKHANNH HFNGNNGGGS WKAGYKNGKN
     DERRMSRTKN MQGGKRRSQQ DDEEKKIDQE MLEMDKNLQL GGDVGHSIAD FEDWKAKMKE
     LELKKLSKSK GISNSTAIAP RESASHETPT DLRPVIPRGP SSITDFLNLK RQDKKEESSQ
     QTPGIPVGQP SLSKTSIEQV NELETNSDLG KSSSSRFSSF FNKSATSLPS LDNNNQVPSS
     NVSVVNNDGN STPHQSGSRL MSFFKESRSS TPNAESQLLS ASDKDNGKMQ TLPQFQQQPQ
     QMQPMAFTQH PPNNNAFFNG LLNKGKSETS TPPPPPPGLI AHQGPQFPVM GVPPNFPQRM
     MPPPPGLVQF QKDSKDVNKK EDRQLRQNKN PNGTRNSKGK QEETATPDLP QQQYMPPPPP
     PGFFPMHPNF PNGPMPPLPQ GFPIPPNGML PVTGQQPQPP YPNMMLQGNF PPNFQQGFGS
     NSPMPIPSII NANGKNVTNQ LPPGLNSKKN IK
//