IF5A1_YEAST
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 03-AUG-2022, entry version 208.
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; 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 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 [15]
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 [16]
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 [17]
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 [18]
RP INTERACTION WITH DYS1, ASSOCIATION WITH THE 80S RIBOSOME, AND MUTAGENESIS
RP 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 [19]
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 [20]
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 [21]
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 [22]
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 [23]
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 [24]
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 [25]
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 [26]
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 [27]
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 [28]
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).
CC -!- FUNCTION: mRNA-binding protein involved in translation elongation. Has
CC an important function at the level of mRNA turnover, probably acting
CC downstream of decapping. Critical for the efficient synthesis of
CC peptide bonds between consecutive proline residues. Can resolve
CC ribosomal stalling caused by consecutive prolines during translation
CC (By similarity). Involved in actin dynamics and cell cycle progression,
CC mRNA decay and probably in a pathway involved in stress response and
CC maintenance of cell wall integrity. Essential for polarized growth, a
CC process necessary for G1/S transition. May mediate large range of
CC effects of the polyamine spermidine in the cell.
CC {ECO:0000250|UniProtKB:P63241, 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:641056,
CC ECO:0000269|PubMed:8307948, ECO:0000269|PubMed:9582285}.
CC -!- SUBUNIT: Homodimer. Interacts with DYS1 and LIA1.
CC {ECO:0000269|PubMed:14675757, ECO:0000269|PubMed:16215987,
CC ECO:0000269|PubMed:19120453}.
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 Note=Concentrates in the perinuclear region.
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: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 and
CC PubMed:19338753) clearly suggests that it is involved in translation
CC elongation and not translation initiation. subclass.
CC {ECO:0000305|PubMed:641056}.
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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 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 AlphaFoldDB; P23301; -.
DR SMR; P23301; -.
DR BioGRID; 36695; 1061.
DR DIP; DIP-4230N; -.
DR IntAct; P23301; 66.
DR MINT; P23301; -.
DR STRING; 4932.YEL034W; -.
DR CarbonylDB; P23301; -.
DR iPTMnet; P23301; -.
DR SWISS-2DPAGE; P23301; -.
DR MaxQB; P23301; -.
DR PaxDb; P23301; -.
DR PRIDE; P23301; -.
DR TopDownProteomics; P23301; -.
DR EnsemblFungi; YEL034W_mRNA; YEL034W; YEL034W.
DR GeneID; 856677; -.
DR KEGG; sce:YEL034W; -.
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 BioCyc; YEAST:G3O-30156-MON; -.
DR Reactome; R-SCE-204626; Hypusine synthesis from eIF5A-lysine.
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:SGD.
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:1903272; P:positive regulation of cytoplasmic translational elongation through polyproline stretches; IMP:SGD.
DR GO; GO:0045901; P:positive regulation of translational elongation; IDA:SGD.
DR GO; GO:0045948; P:positive regulation of translational initiation; IDA:SGD.
DR GO; GO:0045905; P:positive regulation of translational termination; IDA:SGD.
DR GO; GO:0006452; P:translational frameshifting; IGI:SGD.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR001884; IF5A-like.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR014722; Rib_L2_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 PANTHER; PTHR11673; PTHR11673; 1.
DR Pfam; PF01287; eIF-5a; 1.
DR PIRSF; PIRSF003025; eIF5A; 1.
DR SMART; SM01376; eIF-5a; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00037; eIF_5A; 1.
DR PROSITE; PS00302; IF5A_HYPUSINE; 1.
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 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."
FT /evidence="ECO:0000269|PubMed:18341589"
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: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."
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 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 /evidence="ECO:0000269|PubMed:18341589"
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 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:18341589"
FT MUTAGEN 93
FT /note="L->F: Lethal."
FT /evidence="ECO:0000269|PubMed:18341589"
FT MUTAGEN 102
FT /note="L->A: Temperature-sensitive growth phenotype."
FT /evidence="ECO:0000269|PubMed:16408210"
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: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 /evidence="ECO:0000269|PubMed:18341589,
FT ECO:0000269|PubMed:19424157, 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
