ID IF4F1_YEAST Reviewed; 952 AA. AC P39935; D6VUU6; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 2. DT 27-MAR-2024, entry version 216. DE RecName: Full=Eukaryotic initiation factor 4F subunit p150; DE Short=eIF-4F p150 {ECO:0000303|PubMed:8336723}; DE Short=eIF4F p150; DE AltName: Full=Translation initiation factor 4(4)-F(6) subunit gamma(3) protein 1 {ECO:0000303|PubMed:8336723}; DE AltName: Full=eIF4G1; DE AltName: Full=mRNA cap-binding protein complex subunit p150; GN Name=TIF4631 {ECO:0000303|PubMed:8336723}; OrderedLocusNames=YGR162W; 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 [GENOMIC DNA]. RX PubMed=8336723; DOI=10.1128/mcb.13.8.4860-4874.1993; RA Goyer C., Altmann M., Lee H.S., Blanc A., Deshmukh M., Woolford J.L. Jr., RA Trachsel H., Sonenberg N.; RT "TIF4631 and TIF4632: two yeast genes encoding the high-molecular-weight RT subunits of the cap-binding protein complex (eukaryotic initiation factor RT 4F) contain an RNA recognition motif-like sequence and carry out an RT essential function."; RL Mol. Cell. Biol. 13:4860-4874(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9290212; RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y; RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.; RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae RT chromosome VII."; RL Yeast 13:1077-1090(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169869; RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H., RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."; RL Nature 387:81-84(1997). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [6] RP FUNCTION, INTERACTION WITH PAB1, AND MUTAGENESIS OF 214-LYS--LYS-217. RX PubMed=9256432; DOI=10.1073/pnas.94.17.9046; RA Tarun S.Z. Jr., Wells S.E., Deardorff J.A., Sachs A.B.; RT "Translation initiation factor eIF4G mediates in vitro poly(A) tail- RT dependent translation."; RL Proc. Natl. Acad. Sci. U.S.A. 94:9046-9051(1997). RN [7] RP INTERACTION WITH PAB1, AND ATOMIC FORCE MICROSCOPY OF CIRCULAR MRNP RP STRUCTURE. RX PubMed=9702200; DOI=10.1016/s1097-2765(00)80122-7; RA Wells S.E., Hillner P.E., Vale R.D., Sachs A.B.; RT "Circularization of mRNA by eukaryotic translation initiation factors."; RL Mol. Cell 2:135-140(1998). RN [8] RP FUNCTION, AND INTERACTION WITH PAB1. RX PubMed=10357826; DOI=10.1093/emboj/18.11.3153; RA Otero L.J., Ashe M.P., Sachs A.B.; RT "The yeast poly(A)-binding protein Pab1p stimulates in vitro poly(A)- RT dependent and cap-dependent translation by distinct mechanisms."; RL EMBO J. 18:3153-3163(1999). RN [9] RP INTERACTION WITH PAB1. RX PubMed=10944120; DOI=10.1093/emboj/19.16.4372; RA Vilela C., Velasco C., Ptushkina M., McCarthy J.E.G.; RT "The eukaryotic mRNA decapping protein Dcp1 interacts physically and RT functionally with the eIF4F translation initiation complex."; RL EMBO J. 19:4372-4382(2000). RN [10] RP INTERACTION WITH PAT1. RX PubMed=11741542; DOI=10.1016/s1097-2765(01)00395-1; RA Tharun S., Parker R.; RT "Targeting an mRNA for decapping: displacement of translation factors and RT association of the Lsm1p-7p complex on deadenylated yeast mRNAs."; RL Mol. Cell 8:1075-1083(2001). RN [11] 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 [12] 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-181 AND SER-948, AND 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-883 AND THR-888, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17287358; DOI=10.1073/pnas.0607084104; RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; RT "Analysis of phosphorylation sites on proteins from Saccharomyces RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry."; RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-908 AND SER-948, AND RP IDENTIFICATION BY MASS SPECTROMETRY [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 [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-948, AND IDENTIFICATION BY RP 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). RN [17] RP SUBCELLULAR LOCATION. RX PubMed=23222640; DOI=10.1038/nsmb.2468; RA Mitchell S.F., Jain S., She M., Parker R.; RT "Global analysis of yeast mRNPs."; RL Nat. Struct. Mol. Biol. 20:127-133(2013). RN [18] RP PHOSPHORYLATION AT SER-163; SER-195; SER-503; SER-892; SER-896; SER-908 AND RP SER-948. RX PubMed=33856219; DOI=10.1021/acs.jproteome.0c00927; RA Hamey J.J., Nguyen A., Wilkins M.R.; RT "Discovery of arginine methylation, phosphorylation, and their co- RT occurrence in condensate-associated proteins in Saccharomyces cerevisiae."; RL J. Proteome Res. 20:2420-2434(2021). RN [19] {ECO:0007744|PDB:1RF8} RP STRUCTURE BY NMR OF 389-488. RX PubMed=14675538; DOI=10.1016/s0092-8674(03)00975-9; RA Gross J.D., Moerke N.J., von der Haar T., Lugovskoy A.A., Sachs A.B., RA McCarthy J.E.G., Wagner G.; RT "Ribosome loading onto the mRNA cap is driven by conformational coupling RT between eIF4G and eIF4E."; RL Cell 115:739-750(2003). RN [20] {ECO:0007744|PDB:2VSO, ECO:0007744|PDB:2VSX} RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 572-854. RX PubMed=18606994; DOI=10.1073/pnas.0800418105; RA Schuetz P., Bumann M., Oberholzer A.E., Bieniossek C., Trachsel H., RA Altmann M., Baumann U.; RT "Crystal structure of the yeast eIF4A-eIF4G complex: an RNA-helicase RT controlled by protein-protein interactions."; RL Proc. Natl. Acad. Sci. U.S.A. 105:9564-9569(2008). CC -!- FUNCTION: Component of the eIF4F complex, which interacts with the mRNA CC cap structure and serves as an initial point of assembly for the CC translation apparatus. Stimulates translation by interaction with CC polyadenylate-binding protein PAB1, bringing the 5'- and 3'-ends of the CC mRNA in proximity. The formation of this circular mRNP structure CC appears to be critical for the synergistic effects of the cap and the CC poly(A) tail in facilitating translation initiation, recycling of CC ribosomes, and mRNA stability. TIF4631 is probably essential when CC TIF4632 is missing. {ECO:0000269|PubMed:10357826, CC ECO:0000269|PubMed:9256432}. CC -!- SUBUNIT: Component of the eIF4F complex, which composition varies with CC external and internal environmental conditions. It is composed of at CC least eIF4A (TIF1/TIF2), eIF4E (TIF45) and eIF4G (TIF4631 or TIF4632) CC (By similarity). Interacts with PAT1 in a RNA-dependent manner. CC {ECO:0000250, ECO:0000269|PubMed:10357826, ECO:0000269|PubMed:10944120, CC ECO:0000269|PubMed:11741542, ECO:0000269|PubMed:9256432, CC ECO:0000269|PubMed:9702200}. CC -!- INTERACTION: CC P39935; P07260: CDC33; NbExp=14; IntAct=EBI-9002, EBI-150; CC P39935; P04147: PAB1; NbExp=16; IntAct=EBI-9002, EBI-12823; CC P39935; P10081: TIF2; NbExp=10; IntAct=EBI-9002, EBI-9017; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095, CC ECO:0000269|PubMed:23222640}. Cytoplasm, P-body CC {ECO:0000269|PubMed:23222640}. Cytoplasm, Stress granule CC {ECO:0000269|PubMed:23222640}. CC -!- MISCELLANEOUS: Present with 9760 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4G family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L16923; AAA02757.1; -; Genomic_DNA. DR EMBL; Z72947; CAA97184.1; -; Genomic_DNA. DR EMBL; AY692973; AAT92992.1; -; Genomic_DNA. DR EMBL; BK006941; DAA08257.1; -; Genomic_DNA. DR PIR; S64473; S64473. DR RefSeq; NP_011678.3; NM_001181291.3. DR PDB; 1RF8; NMR; -; B=391-488. DR PDB; 2VSO; X-ray; 2.60 A; E/F=572-854. DR PDB; 2VSX; X-ray; 2.80 A; E/F=572-854. DR PDB; 6Z29; NMR; -; A=35-49. DR PDBsum; 1RF8; -. DR PDBsum; 2VSO; -. DR PDBsum; 2VSX; -. DR PDBsum; 6Z29; -. DR AlphaFoldDB; P39935; -. DR SASBDB; P39935; -. DR SMR; P39935; -. DR BioGRID; 33414; 425. DR ComplexPortal; CPX-430; Eukaryotic translation initiation factor 4F complex, variant TIF4631. DR DIP; DIP-985N; -. DR ELM; P39935; -. DR IntAct; P39935; 74. DR MINT; P39935; -. DR STRING; 4932.YGR162W; -. DR GlyGen; P39935; 18 sites, 1 O-linked glycan (18 sites). DR iPTMnet; P39935; -. DR MaxQB; P39935; -. DR PaxDb; 4932-YGR162W; -. DR PeptideAtlas; P39935; -. DR EnsemblFungi; YGR162W_mRNA; YGR162W; YGR162W. DR GeneID; 853071; -. DR KEGG; sce:YGR162W; -. DR AGR; SGD:S000003394; -. DR SGD; S000003394; TIF4631. DR VEuPathDB; FungiDB:YGR162W; -. DR eggNOG; KOG0401; Eukaryota. DR GeneTree; ENSGT00940000154675; -. DR HOGENOM; CLU_006715_1_0_1; -. DR InParanoid; P39935; -. DR OMA; QFYSVIT; -. DR OrthoDB; 92033at2759; -. DR BioCyc; YEAST:G3O-30861-MONOMER; -. DR Reactome; R-SCE-156827; L13a-mediated translational silencing of Ceruloplasmin expression. DR Reactome; R-SCE-166208; mTORC1-mediated signalling. DR Reactome; R-SCE-72649; Translation initiation complex formation. DR Reactome; R-SCE-72662; Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S. DR Reactome; R-SCE-72702; Ribosomal scanning and start codon recognition. DR Reactome; R-SCE-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC). DR Reactome; R-SCE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC). DR BioGRID-ORCS; 853071; 10 hits in 10 CRISPR screens. DR EvolutionaryTrace; P39935; -. DR PRO; PR:P39935; -. DR Proteomes; UP000002311; Chromosome VII. DR RNAct; P39935; Protein. DR GO; GO:0005737; C:cytoplasm; IDA:SGD. DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD. DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IMP:SGD. DR GO; GO:0005739; C:mitochondrion; HDA:SGD. DR GO; GO:0000932; C:P-body; IDA:SGD. DR GO; GO:0005840; C:ribosome; NAS:ComplexPortal. DR GO; GO:0001671; F:ATPase activator activity; IDA:SGD. DR GO; GO:0140693; F:molecular condensate scaffold activity; IDA:DisProt. DR GO; GO:0003729; F:mRNA binding; HDA:SGD. DR GO; GO:0043621; F:protein self-association; EXP:DisProt. DR GO; GO:0003723; F:RNA binding; IDA:SGD. DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central. DR GO; GO:1900103; P:positive regulation of endoplasmic reticulum unfolded protein response; IGI:ParkinsonsUK-UCL. DR GO; GO:1901195; P:positive regulation of formation of translation preinitiation complex; IDA:SGD. DR GO; GO:0051246; P:regulation of protein metabolic process; IGI:ParkinsonsUK-UCL. DR GO; GO:0006446; P:regulation of translational initiation; NAS:ComplexPortal. DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IMP:SGD. DR GO; GO:0034063; P:stress granule assembly; IMP:SGD. DR GO; GO:0006413; P:translational initiation; IMP:SGD. DR DisProt; DP00082; -. DR Gene3D; 1.25.40.180; -; 1. DR Gene3D; 1.20.970.30; eIF4G, eIF4E-binding domain; 1. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR022745; eIF4G1_eIF4E-bd. DR InterPro; IPR036211; eIF4G_eIF4E-bd_sf. DR InterPro; IPR045208; IF4G. DR InterPro; IPR003890; MIF4G-like_typ-3. DR PANTHER; PTHR23253; EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA; 1. DR PANTHER; PTHR23253:SF9; EUKARYOTIC TRANSLATION INITIATION FACTOR 4G1, ISOFORM B-RELATED; 1. DR Pfam; PF12152; eIF_4G1; 1. DR Pfam; PF02854; MIF4G; 1. DR SMART; SM00543; MIF4G; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR SUPFAM; SSF101489; Eukaryotic initiation factor 4f subunit eIF4g, eIF4e-binding domain; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Initiation factor; Phosphoprotein; KW Protein biosynthesis; Reference proteome; RNA-binding; KW Translation regulation. FT CHAIN 1..952 FT /note="Eukaryotic initiation factor 4F subunit p150" FT /id="PRO_0000213331" FT DOMAIN 607..850 FT /note="MIF4G" FT REGION 1..77 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 115..389 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 188..299 FT /note="Interaction with PAB1" FT REGION 481..575 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 870..952 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..60 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 138..155 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 156..195 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 196..229 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 245..330 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 494..509 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 510..569 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 881..898 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 907..923 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 163 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:33856219" FT MOD_RES 181 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17330950" FT MOD_RES 195 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:33856219" FT MOD_RES 503 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:33856219" FT MOD_RES 883 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17287358" FT MOD_RES 888 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17287358" FT MOD_RES 892 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:33856219" FT MOD_RES 896 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:33856219" FT MOD_RES 908 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:33856219, FT ECO:0007744|PubMed:18407956" FT MOD_RES 948 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:33856219, FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, FT ECO:0007744|PubMed:19779198" FT MUTAGEN 214..217 FT /note="KLRK->AAAA: In TIF4631-213; abolishes interaction FT with PAB1 and inhibits poly(A)-dependent translation." FT /evidence="ECO:0000269|PubMed:9256432" FT CONFLICT 7 FT /note="H -> Q (in Ref. 1; AAA02757)" FT /evidence="ECO:0000305" FT CONFLICT 37 FT /note="T -> N (in Ref. 1; AAA02757)" FT /evidence="ECO:0000305" FT CONFLICT 110 FT /note="Q -> K (in Ref. 1; AAA02757)" FT /evidence="ECO:0000305" FT CONFLICT 207 FT /note="R -> K (in Ref. 1; AAA02757)" FT /evidence="ECO:0000305" FT CONFLICT 361 FT /note="D -> E (in Ref. 1; AAA02757)" FT /evidence="ECO:0000305" FT STRAND 43..45 FT /evidence="ECO:0007829|PDB:6Z29" FT HELIX 411..419 FT /evidence="ECO:0007829|PDB:1RF8" FT HELIX 427..429 FT /evidence="ECO:0007829|PDB:1RF8" FT HELIX 443..445 FT /evidence="ECO:0007829|PDB:1RF8" FT HELIX 454..464 FT /evidence="ECO:0007829|PDB:1RF8" FT HELIX 471..476 FT /evidence="ECO:0007829|PDB:1RF8" FT HELIX 603..615 FT /evidence="ECO:0007829|PDB:2VSO" FT STRAND 619..621 FT /evidence="ECO:0007829|PDB:2VSX" FT HELIX 622..634 FT /evidence="ECO:0007829|PDB:2VSO" FT HELIX 635..638 FT /evidence="ECO:0007829|PDB:2VSO" FT HELIX 643..658 FT /evidence="ECO:0007829|PDB:2VSO" FT HELIX 660..662 FT /evidence="ECO:0007829|PDB:2VSO" FT HELIX 663..676 FT /evidence="ECO:0007829|PDB:2VSO" FT HELIX 692..709 FT /evidence="ECO:0007829|PDB:2VSO" FT HELIX 733..755 FT /evidence="ECO:0007829|PDB:2VSO" FT HELIX 761..776 FT /evidence="ECO:0007829|PDB:2VSO" FT HELIX 781..798 FT /evidence="ECO:0007829|PDB:2VSO" FT HELIX 812..827 FT /evidence="ECO:0007829|PDB:2VSO" FT HELIX 834..848 FT /evidence="ECO:0007829|PDB:2VSO" SQ SEQUENCE 952 AA; 107101 MW; 391256802F86118E CRC64; MTDETAHPTQ SASKQESAAL KQTGDDQQES QQQRGYTNYN NGSNYTQKKP YNSNRPHQQR GGKFGPNRYN NRGNYNGGGS FRGGHMGANS SNVPWTGYYN NYPVYYQPQQ MAAAGSAPAN PIPVEEKSPV PTKIEITTKS GEHLDLKEQH KAKLQSQERS TVSPQPESKL KETSDSTSTS TPTPTPSTND SKASSEENIS EAEKTRRNFI EQVKLRKAAL EKKRKEQLEG SSGNNNIPMK TTPENVEEKG SDKPEVTEKT KPAEEKSAEP EVKQETPAEE GEQGEKGQIK EESTPKVLTF AERLKLKKQQ KEREEKTEGK ENKEVPVQEE TKSAIESAPV PPSEQVKEET EVAETEQSNI DESATTPAIP TKSDEAEAEV EAEAGDAGTK IGLEAEIETT TDETDDGTNT VSHILNVLKD ATPIEDVFSF NYPEGIEGPD IKYKKEHVKY TYGPTFLLQF KDKLNVKADA EWVQSTASKI VIPPGMGRGN RSRDSGRFGN NSSRGHDFRN TSVRNMDDRA NSRTSSKRRS KRMNDDRRSN RSYTSRRDRE RGSYRNEEKR EDDKPKEEVA PLVPSANRWV PKFKSKKTEK KLAPDGKTEL LDKDEVERKM KSLLNKLTLE MFDAISSEIL AIANISVWET NGETLKAVIE QIFLKACDEP HWSSMYAQLC GKVVKELNPD ITDETNEGKT GPKLVLHYLV ARCHAEFDKG WTDKLPTNED GTPLEPEMMS EEYYAAASAK RRGLGLVRFI GFLYRLNLLT GKMMFECFRR LMKDLTDSPS EETLESVVEL LNTVGEQFET DSFRTGQATL EGSQLLDSLF GILDNIIQTA KISSRIKFKL IDIKELRHDK NWNSDKKDNG PKTIQQIHEE EERQRQLKNN SRSNSRRTNN SSNRHSFRRD APPASKDSFI TTRTYSQRNS QRAPPPKEEP AAPTSTATNM FSALMGESDD EE //