ID IF5A1_YEAST Reviewed; 157 AA. AC P23301; D3DLL5; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 216. DE RecName: Full=Eukaryotic translation initiation factor 5A-1; DE Short=eIF-5A-1; DE AltName: Full=Hypusine-containing protein HP2; DE AltName: Full=eIF-4D; GN Name=HYP2; Synonyms=TIF51A; OrderedLocusNames=YEL034W; GN ORFNames=SYGP-ORF21; 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=1903841; DOI=10.1128/mcb.11.6.3105-3114.1991; RA Schnier J., Schwelberger H.G., Smit-Mcbride Z., Kang H.A., Hershey J.W.B.; RT "Translation initiation factor 5A and its hypusine modification are RT essential for cell viability in the yeast Saccharomyces cerevisiae."; RL Mol. Cell. Biol. 11:3105-3114(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=DBY874; RA Sandholzer U.R.; RL Submitted (DEC-1990) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2135872; RA Kitaoka Y., Miyazaki M.; RT "Sequence determination of cDNA encoding yeast cycloheximide sensitivity RT factor (CH-SF) and its plausible role at a first peptide bond formation RT step in the initiation process of protein synthesis."; RL Nucleic Acids Symp. Ser. 22:69-70(1990). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169868; RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., RA Botstein D., Davis R.W.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V."; RL Nature 387:78-81(1997). RN [5] 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 [6] RP PARTIAL PROTEIN SEQUENCE, ACETYLATION AT SER-2, AND PHOSPHORYLATION AT RP SER-2. RX PubMed=8243648; DOI=10.1016/0014-5793(93)80712-4; RA Klier H., Woehl T., Eckerskorn C., Magdolen V., Lottspeich F.; RT "Determination and mutational analysis of the phosphorylation site in the RT hypusine-containing protein Hyp2p."; RL FEBS Lett. 334:360-364(1993). RN [7] RP FUNCTION. RX PubMed=641056; DOI=10.1016/s0021-9258(17)40805-2; RA Benne R., Hershey J.W.B.; RT "The mechanism of action of protein synthesis initiation factors from RT rabbit reticulocytes."; RL J. Biol. Chem. 253:3078-3087(1978). RN [8] RP HYPUSINE. RX PubMed=3119589; DOI=10.1016/s0021-9258(18)49297-6; RA Gordon E.D., Mora R., Meredith S.C., Lindquist S.L.; RT "Hypusine formation in eukaryotic initiation factor 4D is not reversed when RT rates or specificity of protein synthesis is altered."; RL J. Biol. Chem. 262:16590-16595(1987). RN [9] RP INDUCTION. RX PubMed=8314769; DOI=10.1016/s0021-9258(19)85203-1; RA Schwelberger H.G., Kang H.A., Hershey J.W.B.; RT "Translation initiation factor eIF-5A expressed from either of two yeast RT genes or from human cDNA. Functional identity under aerobic and anaerobic RT conditions."; RL J. Biol. Chem. 268:14018-14025(1993). RN [10] RP PHOSPHORYLATION AT SER-2. RX PubMed=8325852; DOI=10.1016/s0021-9258(18)82396-1; RA Kang H.A., Schwelberger H.G., Hershey J.W.B.; RT "Translation initiation factor eIF-5A, the hypusine-containing protein, is RT phosphorylated on serine in Saccharomyces cerevisiae."; RL J. Biol. Chem. 268:14750-14756(1993). RN [11] RP FUNCTION. RX PubMed=8307948; DOI=10.1016/s0021-9258(17)41723-6; RA Kang H.A., Hershey J.W.B.; RT "Effect of initiation factor eIF-5A depletion on protein synthesis and RT proliferation of Saccharomyces cerevisiae."; RL J. Biol. Chem. 269:3934-3940(1994). RN [12] RP MUTAGENESIS OF SER-149, AND FUNCTION. RX PubMed=9582285; DOI=10.1093/emboj/17.10.2914; RA Zuk D., Jacobson A.; RT "A single amino acid substitution in yeast eIF-5A results in mRNA RT stabilization."; RL EMBO J. 17:2914-2925(1998). RN [13] RP SUBCELLULAR LOCATION, FUNCTION, AND MUTAGENESIS OF CYS-39 AND PRO-83. RX PubMed=10229683; DOI=10.1042/bj3400273; RA Lee Y.B., Joe Y.A., Wolff E.C., Dimitriadis E.K., Park M.H.; RT "Complex formation between deoxyhypusine synthase and its protein RT substrate, the eukaryotic translation initiation factor 5A (eIF5A) RT precursor."; RL Biochem. J. 340:273-281(1999). RN [14] RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-39; PRO-83 AND GLY-118. RX PubMed=11861547; DOI=10.1093/genetics/160.2.393; RA Valentini S.R., Casolari J.M., Oliveira C.C., Silver P.A., McBride A.E.; RT "Genetic interactions of yeast eukaryotic translation initiation factor 5A RT (eIF5A) reveal connections to poly(A)-binding protein and protein kinase C RT signaling."; RL Genetics 160:393-405(2002). RN [15] RP INTERACTION WITH DYS1 AND LIA1. RX PubMed=14675757; DOI=10.1016/s0014-5793(03)01305-x; RA Thompson G.M., Cano V.S.P., Valentini S.R.; RT "Mapping eIF5A binding sites for Dys1 and Lia1: in vivo evidence for RT regulation of eIF5A hypusination."; RL FEBS Lett. 555:464-468(2003). RN [16] RP FUNCTION. RX PubMed=16157662; DOI=10.1534/genetics.105.048082; RA Zanelli C.F., Valentini S.R.; RT "Pkc1 acts through Zds1 and Gic1 to suppress growth and cell polarity RT defects of a yeast eIF5A mutant."; RL Genetics 171:1571-1581(2005). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY MASS RP 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 [18] RP FUNCTION, ASSOCIATION WITH THE 80S RIBOSOME, AND MUTAGENESIS OF LYS-51. RX PubMed=16914118; DOI=10.1016/j.bbrc.2006.07.195; RA Zanelli C.F., Maragno A.L.C., Gregio A.P.B., Komili S., Pandolfi J.R., RA Mestriner C.A., Lustri W.R., Valentini S.R.; RT "eIF5A binds to translational machinery components and affects translation RT in yeast."; RL Biochem. Biophys. Res. Commun. 348:1358-1366(2006). RN [19] RP INTERACTION WITH DYS1, RIBOSOME-BINDING, AND MUTAGENESIS OF LYS-51. RX PubMed=16215987; DOI=10.1002/jcb.20658; RA Jao D.L., Chen K.Y.; RT "Tandem affinity purification revealed the hypusine-dependent binding of RT eukaryotic initiation factor 5A to the translating 80S ribosomal complex."; RL J. Cell. Biochem. 97:583-598(2006). RN [20] RP MUTAGENESIS OF LEU-102, AND FUNCTION. RX PubMed=16408210; DOI=10.1007/s00438-005-0086-4; RA Chatterjee I., Gross S.R., Kinzy T.G., Chen K.Y.; RT "Rapid depletion of mutant eukaryotic initiation factor 5A at restrictive RT temperature reveals connections to actin cytoskeleton and cell cycle RT progression."; RL Mol. Genet. Genomics 275:264-276(2006). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-74, 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 [22] RP MUTAGENESIS OF GLN-22; SER-24; CYS-39; GLY-50; LYS-51; HIS-52; GLY-53; RP HIS-54; LYS-56; VAL-57; THR-66; PRO-83; LEU-93; PRO-116; GLY-118; LEU-120; RP ASP-122; LEU-124; SER-140; MET-142; SER-149 AND 116-PRO--ASP-157. RX PubMed=18341589; DOI=10.1111/j.1742-4658.2008.06345.x; RA Dias C.A.O., Cano V.S.P., Rangel S.M., Apponi L.H., Frigieri M.C., RA Muniz J.R.C., Garcia W., Park M.H., Garratt R.C., Zanelli C.F., RA Valentini S.R.; RT "Structural modeling and mutational analysis of yeast eukaryotic RT translation initiation factor 5A reveal new critical residues and reinforce RT its involvement in protein synthesis."; RL FEBS J. 275:1874-1888(2008). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-74, 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 [24] RP FUNCTION. RX PubMed=19338753; DOI=10.1016/j.bbrc.2009.01.148; RA Gregio A.P.B., Cano V.P.S., Avaca J.S., Valentini S.R., Zanelli C.F.; RT "eIF5A has a function in the elongation step of translation in yeast."; RL Biochem. Biophys. Res. Commun. 380:785-790(2009). RN [25] RP SUBUNIT, HYPUSINE AT LYS-51, AND MUTAGENESIS OF LYS-51. RX PubMed=19120453; DOI=10.1111/j.1742-4658.2008.06817.x; RA Gentz P.M., Blatch G.L., Dorrington R.A.; RT "Dimerization of the yeast eukaryotic translation initiation factor 5A RT requires hypusine and is RNA dependent."; RL FEBS J. 276:695-706(2009). RN [26] RP FUNCTION, AND MUTAGENESIS OF LYS-51; ASP-63 AND SER-149. RX PubMed=19424157; DOI=10.1038/nature08034; RA Saini P., Eyler D.E., Green R., Dever T.E.; RT "Hypusine-containing protein eIF5A promotes translation elongation."; RL Nature 459:118-121(2009). RN [27] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND THR-10, 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). RN [28] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [29] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-86, 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 [30] RP FUNCTION, AND MUTAGENESIS OF SER-149. RX PubMed=23727016; DOI=10.1016/j.molcel.2013.04.021; RA Gutierrez E., Shin B.S., Woolstenhulme C.J., Kim J.R., Saini P., RA Buskirk A.R., Dever T.E.; RT "eIF5A promotes translation of polyproline motifs."; RL Mol. Cell 51:35-45(2013). RN [31] RP FUNCTION. RX PubMed=24923804; DOI=10.1534/genetics.114.166926; RA Li T., Belda-Palazon B., Ferrando A., Alepuz P.; RT "Fertility and polarized cell growth depends on eIF5A for translation of RT polyproline-rich formins in Saccharomyces cerevisiae."; RL Genetics 197:1191-1200(2014). RN [32] RP RIBOSOME-BINDING, AND MUTAGENESIS OF GLN-22; LYS-56 AND LEU-93. RX PubMed=27115996; DOI=10.1371/journal.pone.0154205; RA Rossi D., Barbosa N.M., Galvao F.C., Boldrin P.E., Hershey J.W., RA Zanelli C.F., Fraser C.S., Valentini S.R.; RT "Evidence for a negative cooperativity between eIF5A and eEF2 on binding to RT the ribosome."; RL PLoS ONE 11:e0154205-e0154205(2016). RN [33] RP FUNCTION. RX PubMed=28392174; DOI=10.1016/j.molcel.2017.03.003; RA Schuller A.P., Wu C.C., Dever T.E., Buskirk A.R., Green R.; RT "eIF5A functions globally in translation elongation and termination."; RL Mol. Cell 66:194-205(2017). RN [34] {ECO:0007744|PDB:5DC3} RP X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) IN COMPLEX WITH RIBOSOME, AND RP HYPUSINE AT LYS-51. RX PubMed=27196944; DOI=10.1016/j.jmb.2016.05.011; RA Melnikov S., Mailliot J., Shin B.S., Rigger L., Yusupova G., Micura R., RA Dever T.E., Yusupov M.; RT "Crystal structure of Hypusine-containing translation factor eIF5A bound to RT a rotated eukaryotic ribosome."; RL J. Mol. Biol. 428:3570-3576(2016). RN [35] {ECO:0007744|PDB:5GAK} RP STRUCTURE BY ELECTRON MICROSCOPY (3.88 ANGSTROMS) IN COMPLEX WITH RIBOSOME, RP AND HYPUSINE AT LYS-51. RX PubMed=26715760; DOI=10.1093/nar/gkv1517; RA Schmidt C., Becker T., Heuer A., Braunger K., Shanmuganathan V., Pech M., RA Berninghausen O., Wilson D.N., Beckmann R.; RT "Structure of the hypusinylated eukaryotic translation factor eIF-5A bound RT to the ribosome."; RL Nucleic Acids Res. 44:1944-1951(2016). RN [36] RP STRUCTURE BY ELECTRON MICROSCOPY (2.7 ANGSTROMS) IN COMPLEX WITH RQC2; RP RKK1; TIF6 AND 60S RIBOSOMAL SUBUNIT, FUNCTION, AND MUTAGENESIS OF LYS-51; RP LYS-69 AND LEU-102. RX PubMed=36804914; DOI=10.1016/j.molcel.2023.01.020; RA Tesina P., Ebine S., Buschauer R., Thoms M., Matsuo Y., Inada T., RA Beckmann R.; RT "Molecular basis of eIF5A-dependent CAT tailing in eukaryotic ribosome- RT associated quality control."; RL Mol. Cell 83:607-621(2023). CC -!- FUNCTION: Translation factor that promotes translation elongation and CC termination, particularly upon ribosome stalling at specific amino acid CC sequence contexts (PubMed:10229683, PubMed:16157662, PubMed:16914118, CC PubMed:19338753, PubMed:19424157, PubMed:641056, PubMed:8307948, CC PubMed:9582285, PubMed:23727016, PubMed:24923804, PubMed:28392174, CC PubMed:36804914). Binds between the exit (E) and peptidyl (P) site of CC the ribosome and promotes rescue of stalled ribosome: specifically CC required for efficient translation of polyproline-containing peptides CC as well as other motifs that stall the ribosome (PubMed:23727016, CC PubMed:24923804, PubMed:28392174). Acts as a ribosome quality control CC (RQC) cofactor by joining the RQC complex to facilitate peptidyl CC transfer during CAT tailing step (PubMed:36804914). Involved in actin CC dynamics and cell cycle progression, mRNA decay and probably in a CC pathway involved in stress response and maintenance of cell wall CC integrity (PubMed:16408210). {ECO:0000269|PubMed:10229683, CC ECO:0000269|PubMed:16157662, ECO:0000269|PubMed:16408210, CC ECO:0000269|PubMed:16914118, ECO:0000269|PubMed:19338753, CC ECO:0000269|PubMed:19424157, ECO:0000269|PubMed:23727016, CC ECO:0000269|PubMed:24923804, ECO:0000269|PubMed:28392174, CC ECO:0000269|PubMed:36804914, ECO:0000269|PubMed:641056, CC ECO:0000269|PubMed:8307948, ECO:0000269|PubMed:9582285}. CC -!- SUBUNIT: Homodimer (PubMed:19120453). Binds to 80S ribosomes CC (PubMed:16215987, PubMed:27115996). Actively translating ribosomes show CC mutually exclusive binding of eIF5a (HYP2 or ANB1) and EFT1/eEF2 CC (PubMed:27115996). Interacts with DYS1 and LIA1 (PubMed:14675757, CC PubMed:16215987). {ECO:0000269|PubMed:14675757, CC ECO:0000269|PubMed:16215987, ECO:0000269|PubMed:19120453, CC ECO:0000269|PubMed:27115996}. CC -!- INTERACTION: CC P23301; P38791: DYS1; NbExp=4; IntAct=EBI-9033, EBI-5871; CC P23301; P47120: LIA1; NbExp=2; IntAct=EBI-9033, EBI-25526; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10229683, CC ECO:0000269|PubMed:11861547}. Note=Concentrates in the perinuclear CC region. {ECO:0000269|PubMed:11861547}. CC -!- INDUCTION: Expressed in aerobic conditions. CC {ECO:0000269|PubMed:8314769}. CC -!- PTM: Lys-51 undergoes hypusination, a unique post-translational CC modification that consists in the addition of a butylamino group from CC spermidine to lysine side chain, leading to the formation of the CC unusual amino acid hypusine. eIF-5As are the only known proteins to CC undergo this modification, which is essential for their function. CC {ECO:0000269|PubMed:19120453, ECO:0000269|PubMed:26715760, CC ECO:0000269|PubMed:27196944, ECO:0000269|PubMed:3119589}. CC -!- MISCELLANEOUS: There are two genes for eIF-5A in yeast. CC -!- SIMILARITY: Belongs to the eIF-5A family. {ECO:0000305}. CC -!- CAUTION: Was originally thought (PubMed:641056) to be a translation CC initiation factor but further analysis (PubMed:19424157, CC PubMed:19338753) clearly suggests that it is involved in translation CC elongation and not translation initiation. subclass. CC {ECO:0000305|PubMed:641056}. 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; M63541; AAA35155.1; -; Genomic_DNA. DR EMBL; X56236; CAA39693.1; -; Genomic_DNA. DR EMBL; D83166; BAA11826.1; -; mRNA. DR EMBL; U18779; AAB65008.1; -; Genomic_DNA. DR EMBL; BK006939; DAA07619.1; -; Genomic_DNA. DR PIR; A40259; FIBYA1. DR RefSeq; NP_010880.3; NM_001178849.3. DR PDB; 3ER0; X-ray; 3.35 A; A/B=1-157. DR PDB; 5DAT; X-ray; 3.15 A; f=1-157. DR PDB; 5DC3; X-ray; 3.25 A; f=1-157. DR PDB; 5DGE; X-ray; 3.45 A; f=1-157. DR PDB; 5DGF; X-ray; 3.30 A; f=1-157. DR PDB; 5GAK; EM; 3.88 A; q=1-157. DR PDB; 5MC6; EM; 3.80 A; BT=1-157. DR PDB; 6Q84; X-ray; 3.70 A; C/F=16-157. DR PDB; 6TNU; EM; 3.10 A; eI=4-157. DR PDB; 7NRC; EM; 3.90 A; Ls=4-157. DR PDB; 8AAF; EM; 2.50 A; v=1-157. DR PDB; 8AGT; EM; 2.60 A; v=1-157. DR PDB; 8AGU; EM; 2.70 A; v=1-157. DR PDB; 8AGV; EM; 2.60 A; v=1-157. DR PDB; 8AGX; EM; 2.40 A; v=1-157. DR PDB; 8AGZ; EM; 2.60 A; v=1-157. DR PDBsum; 3ER0; -. DR PDBsum; 5DAT; -. DR PDBsum; 5DC3; -. DR PDBsum; 5DGE; -. DR PDBsum; 5DGF; -. DR PDBsum; 5GAK; -. DR PDBsum; 5MC6; -. DR PDBsum; 6Q84; -. DR PDBsum; 6TNU; -. DR PDBsum; 7NRC; -. DR PDBsum; 8AAF; -. DR PDBsum; 8AGT; -. DR PDBsum; 8AGU; -. DR PDBsum; 8AGV; -. DR PDBsum; 8AGX; -. DR PDBsum; 8AGZ; -. DR AlphaFoldDB; P23301; -. DR EMDB; EMD-10537; -. DR EMDB; EMD-12534; -. DR EMDB; EMD-3227; -. DR EMDB; EMD-3461; -. DR SMR; P23301; -. DR BioGRID; 36695; 1079. DR DIP; DIP-4230N; -. DR IntAct; P23301; 66. DR MINT; P23301; -. DR STRING; 4932.YEL034W; -. DR CarbonylDB; P23301; -. DR iPTMnet; P23301; -. DR MaxQB; P23301; -. DR PaxDb; 4932-YEL034W; -. DR PeptideAtlas; P23301; -. DR TopDownProteomics; P23301; -. DR EnsemblFungi; YEL034W_mRNA; YEL034W; YEL034W. DR GeneID; 856677; -. DR KEGG; sce:YEL034W; -. DR AGR; SGD:S000000760; -. DR SGD; S000000760; HYP2. DR VEuPathDB; FungiDB:YEL034W; -. DR eggNOG; KOG3271; Eukaryota. DR GeneTree; ENSGT00390000003738; -. DR HOGENOM; CLU_102600_0_0_1; -. DR InParanoid; P23301; -. DR OrthoDB; 5472148at2759; -. DR BioCyc; YEAST:G3O-30156-MONOMER; -. DR Reactome; R-SCE-204626; Hypusine synthesis from eIF5A-lysine. DR BioGRID-ORCS; 856677; 4 hits in 10 CRISPR screens. DR ChiTaRS; HYP2; yeast. DR EvolutionaryTrace; P23301; -. DR PRO; PR:P23301; -. DR Proteomes; UP000002311; Chromosome V. DR RNAct; P23301; Protein. DR GO; GO:0005737; C:cytoplasm; HDA:SGD. DR GO; GO:0005739; C:mitochondrion; HDA:SGD. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:SGD. DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; IDA:SGD. DR GO; GO:0003746; F:translation elongation factor activity; IDA:SGD. DR GO; GO:0003743; F:translation initiation factor activity; IDA:SGD. DR GO; GO:0140708; P:CAT tailing; IDA:UniProtKB. DR GO; GO:1903272; P:positive regulation of cytoplasmic translational elongation through polyproline stretches; IDA:UniProtKB. DR GO; GO:0045901; P:positive regulation of translational elongation; IDA:UniProtKB. DR GO; GO:0045948; P:positive regulation of translational initiation; IDA:SGD. DR GO; GO:0045905; P:positive regulation of translational termination; IDA:UniProtKB. DR GO; GO:0072344; P:rescue of stalled ribosome; IDA:UniProtKB. DR GO; GO:0006414; P:translational elongation; IBA:GO_Central. DR GO; GO:0006452; P:translational frameshifting; IGI:SGD. DR CDD; cd04468; S1_eIF5A; 1. DR Gene3D; 2.30.30.30; -; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1. DR InterPro; IPR001884; IF5A-like. DR InterPro; IPR048670; IF5A-like_N. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR014722; Rib_uL2_dom2. DR InterPro; IPR019769; Trans_elong_IF5A_hypusine_site. DR InterPro; IPR020189; Transl_elong_IF5A_C. DR InterPro; IPR008991; Translation_prot_SH3-like_sf. DR NCBIfam; TIGR00037; eIF_5A; 1. DR PANTHER; PTHR11673:SF6; EUKARYOTIC TRANSLATION INITIATION FACTOR 5A; 1. DR PANTHER; PTHR11673; TRANSLATION INITIATION FACTOR 5A FAMILY MEMBER; 1. DR Pfam; PF01287; eIF-5a; 1. DR Pfam; PF21485; IF5A-like_N; 1. DR PIRSF; PIRSF003025; eIF5A; 1. DR SMART; SM01376; eIF-5a; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1. DR SUPFAM; SSF50104; Translation proteins SH3-like domain; 1. DR PROSITE; PS00302; IF5A_HYPUSINE; 1. DR SWISS-2DPAGE; P23301; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; KW Elongation factor; Hypusine; Isopeptide bond; Phosphoprotein; KW Protein biosynthesis; Reference proteome; RNA-binding; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:8243648, FT ECO:0007744|PubMed:22814378" FT CHAIN 2..157 FT /note="Eukaryotic translation initiation factor 5A-1" FT /id="PRO_0000142488" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000269|PubMed:8243648, FT ECO:0007744|PubMed:22814378" FT MOD_RES 2 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:8243648, FT ECO:0000269|PubMed:8325852, ECO:0007744|PubMed:15665377, FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, FT ECO:0007744|PubMed:19779198" FT MOD_RES 7 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P19211" FT MOD_RES 10 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 51 FT /note="Hypusine" FT /evidence="ECO:0000269|PubMed:19120453, FT ECO:0000269|PubMed:26715760, ECO:0000269|PubMed:27196944, FT ECO:0007744|PDB:5DC3, ECO:0007744|PDB:5GAK" FT MOD_RES 74 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:18407956" FT CROSSLNK 86 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0007744|PubMed:22106047" FT MUTAGEN 22 FT /note="Q->H: Temperature-sensitive growth phenotype; when FT associated with F-93. Reduced binding to the ribosome; when FT associated with F-93." FT /evidence="ECO:0000269|PubMed:18341589, FT ECO:0000269|PubMed:27115996" FT MUTAGEN 24 FT /note="S->P: Temperature-sensitive growth phenotype." FT /evidence="ECO:0000269|PubMed:18341589" FT MUTAGEN 39 FT /note="C->Y: Temperature-sensitive growth phenotype. FT Lethal; when associated with L-83 and D-118 or with I-66 FT and D-118 or with D-118 and I-142 or with L-116 and D-118." FT /evidence="ECO:0000269|PubMed:10229683, FT ECO:0000269|PubMed:11861547, ECO:0000269|PubMed:18341589" FT MUTAGEN 50 FT /note="G->A,P: Lethal." FT /evidence="ECO:0000269|PubMed:18341589" FT MUTAGEN 51 FT /note="K->R: Impairs association to the ribosome and cell FT growth. Reduced ability to promote CAT tailing in response FT to ribosome stalling." FT /evidence="ECO:0000269|PubMed:16215987, FT ECO:0000269|PubMed:16914118, ECO:0000269|PubMed:18341589, FT ECO:0000269|PubMed:19120453, ECO:0000269|PubMed:19424157, FT ECO:0000269|PubMed:36804914" FT MUTAGEN 52 FT /note="H->A,D: Lethal." FT /evidence="ECO:0000269|PubMed:18341589" FT MUTAGEN 53 FT /note="G->A,D: Lethal." FT /evidence="ECO:0000269|PubMed:18341589" FT MUTAGEN 54 FT /note="H->D: Lethal." FT /evidence="ECO:0000269|PubMed:18341589" FT MUTAGEN 56 FT /note="K->A: Temperature-sensitive growth phenotype. FT Reduced binding to the ribosome." FT /evidence="ECO:0000269|PubMed:18341589, FT ECO:0000269|PubMed:27115996" FT MUTAGEN 56 FT /note="K->D: Lethal." FT /evidence="ECO:0000269|PubMed:18341589" FT MUTAGEN 57 FT /note="V->D: Temperature-sensitive growth phenotype." FT /evidence="ECO:0000269|PubMed:18341589" FT MUTAGEN 63 FT /note="D->V: Impairs programmed ribosomal frameshifting." FT /evidence="ECO:0000269|PubMed:19424157" FT MUTAGEN 66 FT /note="T->I: Temperature-sensitive growth phenotype. FT Lethal; when associated with Y-39 and D-118." FT /evidence="ECO:0000269|PubMed:18341589" FT MUTAGEN 69 FT /note="K->A: Reduced ability to promote CAT tailing in FT response to ribosome stalling." FT /evidence="ECO:0000269|PubMed:36804914" FT MUTAGEN 83 FT /note="P->S,L: Temperature-sensitive growth phenotype. FT Lethal; when associated with Y-39 and D-118." FT /evidence="ECO:0000269|PubMed:10229683, FT ECO:0000269|PubMed:11861547, ECO:0000269|PubMed:18341589" FT MUTAGEN 93 FT /note="L->F: Lethal. Reduced binding to the ribosome; when FT associated with H-22." FT /evidence="ECO:0000269|PubMed:18341589, FT ECO:0000269|PubMed:27115996" FT MUTAGEN 102 FT /note="L->A: Temperature-sensitive growth phenotype. FT Impaired ability to promote CAT tailing in response to FT ribosome stalling." FT /evidence="ECO:0000269|PubMed:16408210, FT ECO:0000269|PubMed:36804914" FT MUTAGEN 116 FT /note="P->L: Temperature-sensitive growth phenotype; when FT associated with D-118. Lethal; when associated with Y-39 FT and D-118." FT /evidence="ECO:0000269|PubMed:18341589" FT MUTAGEN 118 FT /note="G->D: Temperature-sensitive growth phenotype; when FT associated with L-116 or W-122 or F-140 or I-142. Lethal; FT when associated with Y-39 and I-66 or with Y-39 and L-83 or FT with Y-39 and L-116 or with Y-39 and F-140 or with Y-39 and FT I-142 or with N-120 and D-124." FT /evidence="ECO:0000269|PubMed:11861547, FT ECO:0000269|PubMed:18341589" FT MUTAGEN 118 FT /note="G->V: Temperature-sensitive growth phenotype; when FT associated with W-122." FT /evidence="ECO:0000269|PubMed:18341589" FT MUTAGEN 120 FT /note="L->N: Lethal; when associated with D-118 and D-124." FT /evidence="ECO:0000269|PubMed:18341589" FT MUTAGEN 122 FT /note="D->W: Temperature-sensitive growth phenotype; when FT associated with V-118." FT /evidence="ECO:0000269|PubMed:18341589" FT MUTAGEN 124 FT /note="L->D: Lethal; when associated with D-118 and N-120." FT /evidence="ECO:0000269|PubMed:18341589" FT MUTAGEN 140 FT /note="S->F: Temperature-sensitive growth phenotype; when FT associated with D-118. Lethal; when associated with Y-39 FT and D-118." FT /evidence="ECO:0000269|PubMed:18341589" FT MUTAGEN 142 FT /note="M->I: Temperature-sensitive growth phenotype; when FT associated with D-118. Lethal; when associated with Y-39 FT and D-118." FT /evidence="ECO:0000269|PubMed:18341589" FT MUTAGEN 149 FT /note="S->P: In ts1159; temperature-sensitive growth FT phenotype and impairs programmed ribosomal frameshifting. FT Impaired ability to promote efficient translation of FT polyproline-containing peptides that stall ribosomes." FT /evidence="ECO:0000269|PubMed:18341589, FT ECO:0000269|PubMed:19424157, ECO:0000269|PubMed:23727016, FT ECO:0000269|PubMed:9582285" FT STRAND 19..22 FT /evidence="ECO:0007829|PDB:3ER0" FT TURN 23..25 FT /evidence="ECO:0007829|PDB:3ER0" FT STRAND 31..34 FT /evidence="ECO:0007829|PDB:3ER0" FT STRAND 37..47 FT /evidence="ECO:0007829|PDB:3ER0" FT STRAND 50..53 FT /evidence="ECO:0007829|PDB:3ER0" FT STRAND 56..66 FT /evidence="ECO:0007829|PDB:3ER0" FT STRAND 70..82 FT /evidence="ECO:0007829|PDB:3ER0" FT STRAND 87..91 FT /evidence="ECO:0007829|PDB:3ER0" FT TURN 96..99 FT /evidence="ECO:0007829|PDB:3ER0" FT STRAND 105..107 FT /evidence="ECO:0007829|PDB:3ER0" FT HELIX 120..126 FT /evidence="ECO:0007829|PDB:3ER0" FT STRAND 135..141 FT /evidence="ECO:0007829|PDB:3ER0" FT STRAND 144..150 FT /evidence="ECO:0007829|PDB:3ER0" SQ SEQUENCE 157 AA; 17114 MW; 738F29CCC7820C47 CRC64; MSDEEHTFET ADAGSSATYP MQCSALRKNG FVVIKSRPCK IVDMSTSKTG KHGHAKVHLV AIDIFTGKKL EDLSPSTHNM EVPVVKRNEY QLLDIDDGFL SLMNMDGDTK DDVKAPEGEL GDSLQTAFDE GKDLMVTIIS AMGEEAAISF KEAARTD //