IF4B_YEAST
ID IF4B_YEAST Reviewed; 436 AA.
AC P34167; D6W4G4;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Eukaryotic translation initiation factor 4B;
DE Short=eIF-4B;
GN Name=TIF3; Synonyms=STM1, TIF42; OrderedLocusNames=YPR163C;
GN ORFNames=P9325.6;
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=8404865; DOI=10.1002/j.1460-2075.1993.tb06077.x;
RA Altmann M., Mueller P.P., Wittmer B., Ruchti F., Lanker S., Trachsel H.;
RT "A Saccharomyces cerevisiae homologue of mammalian translation initiation
RT factor 4B contributes to RNA helicase activity.";
RL EMBO J. 12:3997-4003(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS.
RX PubMed=8404866; DOI=10.1002/j.1460-2075.1993.tb06078.x;
RA Coppolecchia R., Buser P., Stotz A., Linder P.;
RT "A new yeast translation initiation factor suppresses a mutation in the
RT eIF-4A RNA helicase.";
RL EMBO J. 12:4005-4011(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65 AND SER-71, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65 AND SER-71, 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: Involved in translation initiation. May be the homolog of
CC mammalian eIF4B and be part of an RNA helicase. STM1/TIF3 is a non-
CC essential gene.
CC -!- MISCELLANEOUS: Present with 24000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
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DR EMBL; X71996; CAA50870.1; -; Genomic_DNA.
DR EMBL; U25840; AAB68150.1; -; Genomic_DNA.
DR EMBL; AY693114; AAT93133.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11580.1; -; Genomic_DNA.
DR PIR; S37302; S37302.
DR RefSeq; NP_015489.1; NM_001184260.1.
DR AlphaFoldDB; P34167; -.
DR SMR; P34167; -.
DR BioGRID; 36336; 73.
DR DIP; DIP-3806N; -.
DR IntAct; P34167; 5.
DR MINT; P34167; -.
DR STRING; 4932.YPR163C; -.
DR iPTMnet; P34167; -.
DR MaxQB; P34167; -.
DR PaxDb; P34167; -.
DR PRIDE; P34167; -.
DR TopDownProteomics; P34167; -.
DR EnsemblFungi; YPR163C_mRNA; YPR163C; YPR163C.
DR GeneID; 856292; -.
DR KEGG; sce:YPR163C; -.
DR SGD; S000006367; TIF3.
DR VEuPathDB; FungiDB:YPR163C; -.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_045870_0_0_1; -.
DR InParanoid; P34167; -.
DR OMA; VARGSNF; -.
DR BioCyc; YEAST:G3O-34292-MON; -.
DR PRO; PR:P34167; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P34167; protein.
DR GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0043024; F:ribosomal small subunit binding; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0033592; F:RNA strand annealing activity; IDA:SGD.
DR GO; GO:0034057; F:RNA strand-exchange activity; IDA:SGD.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:SGD.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0002181; P:cytoplasmic translation; IMP:SGD.
DR GO; GO:0097010; P:eukaryotic translation initiation factor 4F complex assembly; IMP:SGD.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IMP:SGD.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; IDA:SGD.
DR GO; GO:1902280; P:regulation of RNA helicase activity; IDA:SGD.
DR GO; GO:0006413; P:translational initiation; IDA:SGD.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Initiation factor; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..436
FT /note="Eukaryotic translation initiation factor 4B"
FT /id="PRO_0000081618"
FT DOMAIN 101..183
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REPEAT 190..210
FT /note="1; approximate"
FT REPEAT 211..232
FT /note="2"
FT REPEAT 233..258
FT /note="3"
FT REPEAT 259..284
FT /note="4"
FT REPEAT 285..310
FT /note="5"
FT REPEAT 311..340
FT /note="6"
FT REPEAT 341..350
FT /note="7; truncated"
FT REGION 56..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..350
FT /note="7 X approximate tandem repeats"
FT COMPBIAS 222..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 106
FT /note="N->G,V,Y: Retention of function."
FT /evidence="ECO:0000269|PubMed:8404866"
FT MUTAGEN 106
FT /note="N->S,P: Loss of function."
FT /evidence="ECO:0000269|PubMed:8404866"
FT MUTAGEN 150
FT /note="A->S,C: Retention of function."
FT /evidence="ECO:0000269|PubMed:8404866"
FT MUTAGEN 150
FT /note="A->Y,F,N,L: Loss of function."
FT /evidence="ECO:0000269|PubMed:8404866"
SQ SEQUENCE 436 AA; 48522 MW; 1DFE89D90BF7D677 CRC64;
MAPPKKTVKK MDLTSFLNDD TFGSSWAEED VDLNKITIPI ETANANTIPL SELAHAKNNS
NNTRSGGFGG SFGGRSRLDP ALGGGSSDRR EEYPVPDAPP YRAVINNIPW DITPEGVQAW
VEDGLVKPEA VEEVVLPKNL RDPTRLKGNA FVTLKERADL VAVLKFNGTK LNERTVYVSV
AAPRRGGGAD VDWSSARGSN FQGDGREDAP DLDWGAARGS NFRGPRRERE EVDIDWTAAR
GSNFQGSSRP PRREREEVDI DWSAARGSNF QGSSRPPRRE REEPDIDWSA ARGSNFQSSS
RPPRREREEP DIDWSAARGS NFQSSSRPPR REREKEEPAL DWGAARGAQF GKPQQTKNTY
KDRSLTNKKT TDEQPKIQKS VYDVLRTEDD DEDEEAEKQN GDAKENKVDA AVEKLQDKTA
QLTVEDGDNW EVVGKK
