EAP1_YEAST
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 03-AUG-2022, entry version 155.
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; 485.
DR DIP; DIP-1778N; -.
DR IntAct; P36041; 13.
DR MINT; P36041; -.
DR STRING; 4932.YKL204W; -.
DR iPTMnet; P36041; -.
DR MaxQB; P36041; -.
DR PaxDb; P36041; -.
DR PRIDE; P36041; -.
DR EnsemblFungi; YKL204W_mRNA; YKL204W; YKL204W.
DR GeneID; 853631; -.
DR KEGG; sce:YKL204W; -.
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 BioCyc; YEAST:G3O-31963-MON; -.
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:0005844; C:polysome; 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 GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
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
