IF2B_YEAST
ID IF2B_YEAST Reviewed; 285 AA.
AC P09064; D6W3D3; Q6B200;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Eukaryotic translation initiation factor 2 subunit beta;
DE Short=eIF-2-beta;
GN Name=SUI3; Synonyms=TIF212; OrderedLocusNames=YPL237W;
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=3136928; DOI=10.1016/s0092-8674(88)80006-0;
RA Donahue T.F., Cigan A.M., Pabich E.K., Valavicius B.C.;
RT "Mutations at a Zn(II) finger motif in the yeast eIF-2 beta gene alter
RT ribosomal start-site selection during the scanning process.";
RL Cell 54:621-632(1988).
RN [2]
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 [3]
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 [4]
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 [5]
RP INTERACTION WITH GCD6 AND TIF5, AND MUTAGENESIS OF 16-LYS--LYS-23;
RP 49-LYS--LYS-56 AND 82-LYS--LYS-89.
RX PubMed=10075937; DOI=10.1093/emboj/18.6.1673;
RA Asano K., Krishnamoorthy T., Phan L., Pavitt G.D., Hinnebusch A.G.;
RT "Conserved bipartite motifs in yeast eIF5 and eIF2Bepsilon, GTPase-
RT activating and GDP-GTP exchange factors in translation initiation, mediate
RT binding to their common substrate eIF2.";
RL EMBO J. 18:1673-1688(1999).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40 AND SER-112, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40; THR-69; SER-80 AND
RP SER-112, AND 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-40; SER-80; SER-92; SER-112;
RP THR-116 AND SER-118, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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: eIF-2 functions in the early steps of protein synthesis by
CC forming a ternary complex with GTP and initiator tRNA. This complex
CC binds to a 40S ribosomal subunit, followed by mRNA binding to form a
CC 43S preinitiation complex. Junction of the 60S ribosomal subunit to
CC form the 80S initiation complex is preceded by hydrolysis of the GTP
CC bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for
CC eIF-2 to recycle and catalyze another round of initiation, the GDP
CC bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by
CC eIF-2B.
CC -!- SUBUNIT: Eukaryotic translation initiation factor 2 (eIF-2) is a
CC heterotrimer composed of an alpha, a beta and a gamma subunit. The
CC factors eIF-1, eIF-2, eIF-3, TIF5/eIF-5 and methionyl-tRNAi form a
CC multifactor complex (MFC) that may bind to the 40S ribosome. SUI3
CC interacts with GCD6 and TIF5/eIF-5. {ECO:0000269|PubMed:10075937}.
CC -!- INTERACTION:
CC P09064; P32481: GCD11; NbExp=5; IntAct=EBI-8920, EBI-8924;
CC -!- SIMILARITY: Belongs to the eIF-2-beta/eIF-5 family. {ECO:0000305}.
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DR EMBL; M21813; AAA34589.1; -; Genomic_DNA.
DR EMBL; Z67751; CAA91607.1; -; Genomic_DNA.
DR EMBL; Z73594; CAA97959.1; -; Genomic_DNA.
DR EMBL; AY692930; AAT92949.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11199.1; -; Genomic_DNA.
DR PIR; S29368; S29368.
DR RefSeq; NP_015087.1; NM_001184051.1.
DR PDB; 3J81; EM; 4.00 A; l=1-285.
DR PDB; 3JAP; EM; 4.90 A; l=1-285.
DR PDB; 3JAQ; EM; 6.00 A; l=1-285.
DR PDB; 6FYX; EM; 3.05 A; l=1-285.
DR PDB; 6FYY; EM; 3.05 A; l=1-285.
DR PDB; 6GSM; EM; 5.15 A; l=127-270.
DR PDB; 6GSN; EM; 5.75 A; l=127-270.
DR PDB; 6I3M; EM; 3.93 A; M/N=1-285.
DR PDB; 6I7T; EM; 4.61 A; M/N=1-285.
DR PDB; 6QG0; EM; 4.20 A; O/P=1-285.
DR PDB; 6QG1; EM; 4.20 A; O/P=1-285.
DR PDB; 6QG2; EM; 4.60 A; O/P=1-285.
DR PDB; 6QG3; EM; 9.40 A; O/P=1-285.
DR PDB; 6QG5; EM; 10.10 A; O/P=1-285.
DR PDB; 6QG6; EM; 4.65 A; O/P=1-285.
DR PDBsum; 3J81; -.
DR PDBsum; 3JAP; -.
DR PDBsum; 3JAQ; -.
DR PDBsum; 6FYX; -.
DR PDBsum; 6FYY; -.
DR PDBsum; 6GSM; -.
DR PDBsum; 6GSN; -.
DR PDBsum; 6I3M; -.
DR PDBsum; 6I7T; -.
DR PDBsum; 6QG0; -.
DR PDBsum; 6QG1; -.
DR PDBsum; 6QG2; -.
DR PDBsum; 6QG3; -.
DR PDBsum; 6QG5; -.
DR PDBsum; 6QG6; -.
DR AlphaFoldDB; P09064; -.
DR SMR; P09064; -.
DR BioGRID; 35925; 168.
DR ComplexPortal; CPX-427; Eukaryotic translation initiation factor 2 complex.
DR DIP; DIP-2310N; -.
DR IntAct; P09064; 17.
DR MINT; P09064; -.
DR STRING; 4932.YPL237W; -.
DR iPTMnet; P09064; -.
DR MaxQB; P09064; -.
DR PaxDb; P09064; -.
DR PRIDE; P09064; -.
DR EnsemblFungi; YPL237W_mRNA; YPL237W; YPL237W.
DR GeneID; 855838; -.
DR KEGG; sce:YPL237W; -.
DR SGD; S000006158; SUI3.
DR VEuPathDB; FungiDB:YPL237W; -.
DR eggNOG; KOG2768; Eukaryota.
DR GeneTree; ENSGT00390000001804; -.
DR HOGENOM; CLU_026663_0_3_1; -.
DR InParanoid; P09064; -.
DR OMA; CMREGNK; -.
DR BioCyc; YEAST:G3O-34124-MON; -.
DR Reactome; R-SCE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-SCE-381042; PERK regulates gene expression.
DR Reactome; R-SCE-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-SCE-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-SCE-72731; Recycling of eIF2:GDP.
DR PRO; PR:P09064; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P09064; protein.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IDA:SGD.
DR GO; GO:0005850; C:eukaryotic translation initiation factor 2 complex; IDA:SGD.
DR GO; GO:0043614; C:multi-eIF complex; IDA:SGD.
DR GO; GO:0005840; C:ribosome; IDA:ComplexPortal.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR GO; GO:0003743; F:translation initiation factor activity; IMP:SGD.
DR GO; GO:0031369; F:translation initiation factor binding; IDA:SGD.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IBA:GO_Central.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IDA:SGD.
DR GO; GO:0006413; P:translational initiation; IDA:ComplexPortal.
DR InterPro; IPR045196; IF2/IF5.
DR InterPro; IPR002735; Transl_init_fac_IF2/IF5_dom.
DR InterPro; IPR016189; Transl_init_fac_IF2/IF5_N.
DR InterPro; IPR016190; Transl_init_fac_IF2/IF5_Zn-bd.
DR PANTHER; PTHR23001; PTHR23001; 1.
DR Pfam; PF01873; eIF-5_eIF-2B; 1.
DR SMART; SM00653; eIF2B_5; 1.
DR SUPFAM; SSF100966; SSF100966; 1.
DR SUPFAM; SSF75689; SSF75689; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Initiation factor; Metal-binding; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..285
FT /note="Eukaryotic translation initiation factor 2 subunit
FT beta"
FT /id="PRO_0000137415"
FT ZN_FING 236..262
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 30..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 69
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 116
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 16..23
FT /note="KKKKKTKK->AAAAATAA: Abolishes interaction with TIF5;
FT when associated with 49-K--K-56 and 82-K--K-89."
FT /evidence="ECO:0000269|PubMed:10075937"
FT MUTAGEN 49..56
FT /note="KKKKKKSK->AAAAAASA: Abolishes interaction with TIF5;
FT when associated with 16-K--K-23 and 82-K--K-89."
FT /evidence="ECO:0000269|PubMed:10075937"
FT MUTAGEN 82..89
FT /note="KKKKKKTK->AAAAAATA: Abolishes interaction with TIF5;
FT when associated with 16-K--K-23 and 49-K--K-56."
FT /evidence="ECO:0000269|PubMed:10075937"
FT CONFLICT 141
FT /note="I -> T (in Ref. 4; AAT92949)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 285 AA; 31574 MW; 34DE9323876CEE95 CRC64;
MSSDLAAELG FDPALKKKKK TKKVIPDDFD AAVNGKENGS GDDLFAGLKK KKKKSKSVSA
DAEAEKEPTD DIAEALGELS LKKKKKKTKD SSVDAFEKEL AKAGLDNVDA ESKEGTPSAN
SSIQQEVGLP YSELLSRFFN ILRTNNPELA GDRSGPKFRI PPPVCLRDGK KTIFSNIQDI
AEKLHRSPEH LIQYLFAELG TSGSVDGQKR LVIKGKFQSK QMENVLRRYI LEYVTCKTCK
SINTELKREQ SNRLFFMVCK SCGSTRSVSS IKTGFQATVG KRRRM
