ID EF1B_YEAST Reviewed; 206 AA. AC P32471; D6VPL3; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 02-SEP-2026, entry version 215. DE RecName: Full=Elongation factor 1-beta; DE Short=EF-1-beta; DE AltName: Full=Eukaryotic elongation factor 1Balpha; DE Short=eEF1Balpha; DE AltName: Full=Translation elongation factor 1B alpha; GN Name=EFB1; Synonyms=TEF5; OrderedLocusNames=YAL003W; 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=8420802; DOI=10.1016/0014-5793(93)81208-h; RA Hiraga K., Suzuki K., Tsuchiya E., Miyakawa T.; RT "Cloning and characterization of the elongation factor EF-1 beta homologue RT of Saccharomyces cerevisiae. EF-1 beta is essential for growth."; RL FEBS Lett. 316:165-169(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204511 / S288c / AB972; RX PubMed=7941740; DOI=10.1002/yea.320100413; RA Clark M.W., Keng T., Storms R.K., Zhong W.-W., Fortin N., Zeng B., RA Delaney S., Ouellette B.F.F., Barton A.B., Kaback D.B., Bussey H.; RT "Sequencing of chromosome I of Saccharomyces cerevisiae: analysis of the 42 RT kbp SPO7-CENI-CDC15 region."; RL Yeast 10:535-541(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809; RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N., RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J., RA Storms R.K.; RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae."; RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995). 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 PROTEIN SEQUENCE OF 14-22 AND 51-56. RC STRAIN=ATCC 38531 / Y41; RX PubMed=8935650; DOI=10.1111/j.1574-6968.1996.tb08073.x; RA Norbeck J., Blomberg A.; RT "Protein expression during exponential growth in 0.7 M NaCl medium of RT Saccharomyces cerevisiae."; RL FEMS Microbiol. Lett. 137:1-8(1996). RN [6] RP PROTEIN SEQUENCE OF 168-178. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7895733; DOI=10.1002/elps.11501501210; RA Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B., RA Volpe T., Warner J.R., McLaughlin C.S.; RT "Protein identifications for a Saccharomyces cerevisiae protein database."; RL Electrophoresis 15:1466-1486(1994). RN [7] RP ACETYLATION AT ALA-2. RX PubMed=9298649; DOI=10.1002/elps.1150180810; RA Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I., RA Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R., RA Payne W.E.; RT "Proteome studies of Saccharomyces cerevisiae: identification and RT characterization of abundant proteins."; RL Electrophoresis 18:1347-1360(1997). RN [8] RP FUNCTION, AND MUTAGENESIS OF SER-121. RX PubMed=10409717; DOI=10.1128/mcb.19.8.5257; RA Carr-Schmid A., Valente L., Loik V.I., Williams T., Starita L.M., RA Kinzy T.G.; RT "Mutations in elongation factor 1beta, a guanine nucleotide exchange RT factor, enhance translational fidelity."; RL Mol. Cell. Biol. 19:5257-5266(1999). RN [9] RP PHOSPHORYLATION. RX PubMed=10523624; DOI=10.1128/mcb.19.11.7357; RA Futcher B., Latter G.I., Monardo P., McLaughlin C.S., Garrels J.I.; RT "A sampling of the yeast proteome."; RL Mol. Cell. Biol. 19:7357-7368(1999). RN [10] RP S-THIOLATION. RX PubMed=12755685; DOI=10.1042/bj20030414; RA Shenton D., Grant C.M.; RT "Protein S-thiolation targets glycolysis and protein synthesis in response RT to oxidative stress in the yeast Saccharomyces cerevisiae."; RL Biochem. J. 374:513-519(2003). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=YAL6B; RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200; RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., RA Jensen O.N.; RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling RT pathway."; RL Mol. Cell. Proteomics 4:310-327(2005). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, AND IDENTIFICATION BY RP 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31 AND SER-86, 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, 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 [15] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-13, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22106047; DOI=10.1002/pmic.201100166; RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.; RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae."; RL Proteomics 12:236-240(2012). RN [16] RP X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 113-206 IN COMPLEX WITH EEF1A, RP AND MUTAGENESIS OF PHE-163. RX PubMed=11106763; DOI=10.1016/s1097-2765(00)00122-2; RA Andersen G.R., Pedersen L., Valente L., Chatterjee I., Kinzy T.G., RA Kjeldgaard M., Nyborg J.; RT "Structural basis for nucleotide exchange and competition with tRNA in the RT yeast elongation factor complex eEF1A:eEF1Balpha."; RL Mol. Cell 6:1261-1266(2000). RN [17] RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 113-206 IN COMPLEX WITH EEF1A, RP AND MUTAGENESIS OF LYS-205. RX PubMed=11373622; DOI=10.1038/88598; RA Andersen G.R., Valente L., Pedersen L., Kinzy T.G., Nyborg J.; RT "Crystal structures of nucleotide exchange intermediates in the eEF1A- RT eEF1Balpha complex."; RL Nat. Struct. Biol. 8:531-534(2001). CC -!- FUNCTION: Catalytic subunit of the guanine nucleotide exchange factor CC (GEF) (eEF1B subcomplex) of the eukaryotic elongation factor 1 complex CC (eEF1). Stimulates the exchange of GDP for GTP on elongation factor 1A CC (eEF1A), probably by displacing GDP from the nucleotide binding pocket CC in eEF1A. The 30-fold higher concentration of GTP compared to GDP in CC cells favors the formation of eEF1A-GTP, which rapidly forms a ternary CC complex with aminoacyl-tRNA that in turn displaces eEF1B from the CC complex. {ECO:0000269|PubMed:10409717}. CC -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation. CC -!- SUBUNIT: The eukaryotic elongation factor 1 complex (eEF1) is probably CC a heterohexamer. Two trimeric complexes, each composed of eEF1A (TEF1 CC or TEF2), eEF1Balpha (EFB1) and eEF1Bgamma (CAM1 or TEF4), are probably CC dimerized via the eF1Bgamma subunits. eEF1Balpha interacts directly CC with eEF1A. eEF1Balpha and eEF1Bgamma form the eEF1B subcomplex with CC the GEF activity. {ECO:0000269|PubMed:11106763, CC ECO:0000269|PubMed:11373622}. CC -!- INTERACTION: CC P32471; P02994: TEF2; NbExp=4; IntAct=EBI-6319, EBI-6314; CC -!- DOMAIN: The C-terminus (pos. 119-205) exhibits guanine nucleotide CC exchange activity. CC -!- PTM: S-thiolated in response to oxidative stress, probably inhibiting CC the protein and causing a reduction in protein synthesis. CC {ECO:0000269|PubMed:12755685}. CC -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family. {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; D14080; BAA03165.1; -; Genomic_DNA. DR EMBL; L22015; AAC04954.1; -; Genomic_DNA. DR EMBL; BK006935; DAA06983.1; -; Genomic_DNA. DR PIR; S43445; S43445. DR RefSeq; NP_009398.1; NM_001178150.1. DR PDB; 1F60; X-ray; 1.67 A; B=113-206. DR PDB; 1G7C; X-ray; 2.05 A; B=113-206. DR PDB; 1IJE; X-ray; 2.40 A; B=117-206. DR PDB; 1IJF; X-ray; 3.00 A; B=117-206. DR PDB; 2B7B; X-ray; 2.60 A; B=113-206. DR PDB; 2B7C; X-ray; 1.80 A; B=113-206. DR PDB; 5O8W; X-ray; 1.67 A; B=113-206. DR AlphaFoldDB; P32471; -. DR MDposit; P32471; -. DR SMR; P32471; -. DR BioGRID; 31787; 114. DR ComplexPortal; CPX-2854; Elongation Factor eEF1 complex, variant CAM1. DR ComplexPortal; CPX-425; Elongation Factor eEF1 complex, variant TEF4. DR DIP; DIP-6445N; -. DR FunCoup; P32471; 991. DR IntAct; P32471; 25. DR MINT; P32471; -. DR STRING; 4932.YAL003W; -. DR iPTMnet; P32471; -. DR PaxDb; 4932-YAL003W; -. DR PeptideAtlas; P32471; -. DR TopDownProteomics; P32471; -. DR EnsemblFungi; YAL003W_mRNA; YAL003W; YAL003W. DR GeneID; 851260; -. DR KEGG; sce:YAL003W; -. DR AGR; SGD:S000000003; -. DR SGD; S000000003; EFB1. DR VEuPathDB; FungiDB:YAL003W; -. DR eggNOG; KOG1668; Eukaryota. DR HOGENOM; CLU_050172_0_2_1; -. DR InParanoid; P32471; -. DR OMA; YRWYKHI; -. DR OrthoDB; 331763at2759; -. DR BioCyc; YEAST:G3O-28818-MONOMER; -. DR Reactome; R-SCE-156842; Eukaryotic Translation Elongation. DR UniPathway; UPA00345; -. DR BioGRID-ORCS; 851260; 7 hits in 10 CRISPR screens. DR CD-CODE; E03F929F; Stress granule. DR EvolutionaryTrace; P32471; -. DR PRO; PR:P32471; -. DR Proteomes; UP000002311; Chromosome I. DR RNAct; P32471; protein. DR GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; IMP:SGD. DR GO; GO:0005840; C:ribosome; IDA:ComplexPortal. DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:SGD. DR GO; GO:0003746; F:translation elongation factor activity; IEA:InterPro. DR GO; GO:1990145; P:maintenance of translational fidelity; IMP:SGD. DR GO; GO:0032232; P:negative regulation of actin filament bundle assembly; IDA:SGD. DR GO; GO:0006449; P:regulation of translational termination; IGI:SGD. DR GO; GO:0006414; P:translational elongation; IDA:ComplexPortal. DR CDD; cd00292; EF1B; 1. DR FunFam; 1.20.1050.130:FF:000009; Elongation factor 1-beta; 1. DR FunFam; 3.30.70.60:FF:000001; Elongation factor 1-beta 1 like; 1. DR Gene3D; 1.20.1050.130; -; 1. DR Gene3D; 3.30.70.60; -; 1. DR InterPro; IPR053836; Arc1-like_N. DR InterPro; IPR036219; eEF-1beta-like_sf. DR InterPro; IPR018940; EF-1_beta_acid_region_euk. DR InterPro; IPR049720; EF1B_bsu/dsu. DR InterPro; IPR014038; EF1B_bsu/dsu_GNE. DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf. DR InterPro; IPR014717; Transl_elong_EF1B/ribsomal_bS6. DR InterPro; IPR001326; Transl_elong_EF1B_B/D_CS. DR PANTHER; PTHR11595; EF-HAND AND COILED-COIL DOMAIN-CONTAINING FAMILY MEMBER; 1. DR PANTHER; PTHR11595:SF21; ELONGATION FACTOR 1-BETA; 1. DR Pfam; PF21972; Arc1p_N_like; 1. DR Pfam; PF10587; EF-1_beta_acid; 1. DR Pfam; PF00736; EF1_GNE; 1. DR SMART; SM01182; EF-1_beta_acid; 1. DR SMART; SM00888; EF1_GNE; 1. DR SUPFAM; SSF54984; eEF-1beta-like; 1. DR SUPFAM; SSF47616; GST C-terminal domain-like; 1. DR PROSITE; PS00824; EF1BD_1; 1. DR PROSITE; PS00825; EF1BD_2; 1. DR PDBsum; 1F60; -. DR PDBsum; 1G7C; -. DR PDBsum; 1IJE; -. DR PDBsum; 1IJF; -. DR PDBsum; 2B7B; -. DR PDBsum; 2B7C; -. DR PDBsum; 5O8W; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Direct protein sequencing; Elongation factor; KW Isopeptide bond; Phosphoprotein; Protein biosynthesis; Reference proteome; KW Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:9298649" FT CHAIN 2..206 FT /note="Elongation factor 1-beta" FT /id="PRO_0000155042" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|PubMed:9298649" FT MOD_RES 31 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 86 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198" FT CROSSLNK 13 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0007744|PubMed:22106047" FT MUTAGEN 120..122 FT /note="KSI->R: In TEF5-7; reduces translation efficiency FT and enhances translation fidelity." FT MUTAGEN 121 FT /note="S->I,L,N: Reduces translation efficiency and FT enhances translation fidelity." FT /evidence="ECO:0000269|PubMed:10409717" FT MUTAGEN 163 FT /note="F->A: Temperature-sensitive." FT /evidence="ECO:0000269|PubMed:11106763" FT MUTAGEN 205 FT /note="K->A: Loss of catalytic activity, but still binds to FT eEF1A." FT /evidence="ECO:0000269|PubMed:11373622" FT CONFLICT 49 FT /note="S -> F (in Ref. 1; BAA03165)" FT /evidence="ECO:0000305" FT CONFLICT 57 FT /note="S -> F (in Ref. 1; BAA03165)" FT /evidence="ECO:0000305" FT CONFLICT 98 FT /note="L -> W (in Ref. 1; BAA03165)" FT /evidence="ECO:0000305" FT CONFLICT 168 FT /note="L -> E (in Ref. 6; AA sequence)" FT /evidence="ECO:0000305" FT HELIX 117..119 FT /evidence="ECO:0007829|PDB:5O8W" FT STRAND 120..131 FT /evidence="ECO:0007829|PDB:1F60" FT HELIX 136..144 FT /evidence="ECO:0007829|PDB:1F60" FT STRAND 151..162 FT /evidence="ECO:0007829|PDB:1F60" FT STRAND 165..175 FT /evidence="ECO:0007829|PDB:1F60" FT TURN 176..178 FT /evidence="ECO:0007829|PDB:1F60" FT HELIX 181..189 FT /evidence="ECO:0007829|PDB:1F60" FT TURN 192..194 FT /evidence="ECO:0007829|PDB:1F60" FT STRAND 195..205 FT /evidence="ECO:0007829|PDB:1F60" SQ SEQUENCE 206 AA; 22627 MW; BEA764852CE125F7 CRC64; MASTDFSKIE TLKQLNASLA DKSYIEGTAV SQADVTVFKA FQSAYPEFSR WFNHIASKAD EFDSFPAASA AAAEEEEDDD VDLFGSDDEE ADAEAEKLKA ERIAAYNAKK AAKPAKPAAK SIVTLDVKPW DDETNLEEMV ANVKAIEMEG LTWGAHQFIP IGFGIKKLQI NCVVEDDKVS LDDLQQSIEE DEDHVQSTDI AAMQKL //