Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Eukaryotic translation initiation factor 5A-1 (eIF-5A-1) (Hypusine-containing protein HP2) (eIF-4D)

 IF5A1_YEAST             Reviewed;         157 AA.
P23301; D3DLL5;
01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
18-JUL-2018, entry version 184.
RecName: Full=Eukaryotic translation initiation factor 5A-1;
Short=eIF-5A-1;
AltName: Full=Hypusine-containing protein HP2;
AltName: Full=eIF-4D;
Name=HYP2; Synonyms=TIF51A; OrderedLocusNames=YEL034W;
ORFNames=SYGP-ORF21;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1903841; DOI=10.1128/MCB.11.6.3105;
Schnier J., Schwelberger H.G., Smit-Mcbride Z., Kang H.A.,
Hershey J.W.B.;
"Translation initiation factor 5A and its hypusine modification are
essential for cell viability in the yeast Saccharomyces cerevisiae.";
Mol. Cell. Biol. 11:3105-3114(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=DBY874;
Sandholzer U.R.;
Submitted (DEC-1990) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2135872;
Kitaoka Y., Miyazaki M.;
"Sequence determination of cDNA encoding yeast cycloheximide
sensitivity factor (CH-SF) and its plausible role at a first peptide
bond formation step in the initiation process of protein synthesis.";
Nucleic Acids Symp. Ser. 22:69-70(1990).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169868;
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G.,
Hunicke-Smith S., Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H.,
Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P.,
Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T.,
Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
Nature 387:78-81(1997).
[5]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[6]
PARTIAL PROTEIN SEQUENCE, ACETYLATION AT SER-2, AND PHOSPHORYLATION AT
SER-2.
PubMed=8243648; DOI=10.1016/0014-5793(93)80712-4;
Klier H., Woehl T., Eckerskorn C., Magdolen V., Lottspeich F.;
"Determination and mutational analysis of the phosphorylation site in
the hypusine-containing protein Hyp2p.";
FEBS Lett. 334:360-364(1993).
[7]
FUNCTION.
PubMed=641056;
Benne R., Hershey J.W.B.;
"The mechanism of action of protein synthesis initiation factors from
rabbit reticulocytes.";
J. Biol. Chem. 253:3078-3087(1978).
[8]
HYPUSINE.
PubMed=3119589;
Gordon E.D., Mora R., Meredith S.C., Lindquist S.L.;
"Hypusine formation in eukaryotic initiation factor 4D is not reversed
when rates or specificity of protein synthesis is altered.";
J. Biol. Chem. 262:16590-16595(1987).
[9]
INDUCTION.
PubMed=8314769;
Schwelberger H.G., Kang H.A., Hershey J.W.B.;
"Translation initiation factor eIF-5A expressed from either of two
yeast genes or from human cDNA. Functional identity under aerobic and
anaerobic conditions.";
J. Biol. Chem. 268:14018-14025(1993).
[10]
PHOSPHORYLATION AT SER-2.
PubMed=8325852;
Kang H.A., Schwelberger H.G., Hershey J.W.B.;
"Translation initiation factor eIF-5A, the hypusine-containing
protein, is phosphorylated on serine in Saccharomyces cerevisiae.";
J. Biol. Chem. 268:14750-14756(1993).
[11]
FUNCTION.
PubMed=8307948;
Kang H.A., Hershey J.W.B.;
"Effect of initiation factor eIF-5A depletion on protein synthesis and
proliferation of Saccharomyces cerevisiae.";
J. Biol. Chem. 269:3934-3940(1994).
[12]
MUTAGENESIS OF SER-149, AND FUNCTION.
PubMed=9582285; DOI=10.1093/emboj/17.10.2914;
Zuk D., Jacobson A.;
"A single amino acid substitution in yeast eIF-5A results in mRNA
stabilization.";
EMBO J. 17:2914-2925(1998).
[13]
SUBCELLULAR LOCATION, FUNCTION, AND MUTAGENESIS OF CYS-39 AND PRO-83.
PubMed=10229683; DOI=10.1042/bj3400273;
Lee Y.B., Joe Y.A., Wolff E.C., Dimitriadis E.K., Park M.H.;
"Complex formation between deoxyhypusine synthase and its protein
substrate, the eukaryotic translation initiation factor 5A (eIF5A)
precursor.";
Biochem. J. 340:273-281(1999).
[14]
INTERACTION WITH DYS1 AND LIA1.
PubMed=14675757; DOI=10.1016/S0014-5793(03)01305-X;
Thompson G.M., Cano V.S.P., Valentini S.R.;
"Mapping eIF5A binding sites for Dys1 and Lia1: in vivo evidence for
regulation of eIF5A hypusination.";
FEBS Lett. 555:464-468(2003).
[15]
FUNCTION.
PubMed=16157662; DOI=10.1534/genetics.105.048082;
Zanelli C.F., Valentini S.R.;
"Pkc1 acts through Zds1 and Gic1 to suppress growth and cell polarity
defects of a yeast eIF5A mutant.";
Genetics 171:1571-1581(2005).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=YAL6B;
PubMed=15665377; DOI=10.1074/mcp.M400219-MCP200;
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,
Mann M., Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone
signaling pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[17]
FUNCTION, ASSOCIATION WITH THE 80S RIBOSOME, AND MUTAGENESIS OF
LYS-51.
PubMed=16914118; DOI=10.1016/j.bbrc.2006.07.195;
Zanelli C.F., Maragno A.L.C., Gregio A.P.B., Komili S., Pandolfi J.R.,
Mestriner C.A., Lustri W.R., Valentini S.R.;
"eIF5A binds to translational machinery components and affects
translation in yeast.";
Biochem. Biophys. Res. Commun. 348:1358-1366(2006).
[18]
INTERACTION WITH DYS1, ASSOCIATION WITH THE 80S RIBOSOME, AND
MUTAGENESIS OF LYS-51.
PubMed=16215987; DOI=10.1002/jcb.20658;
Jao D.L., Chen K.Y.;
"Tandem affinity purification revealed the hypusine-dependent binding
of eukaryotic initiation factor 5A to the translating 80S ribosomal
complex.";
J. Cell. Biochem. 97:583-598(2006).
[19]
MUTAGENESIS OF LEU-102, AND FUNCTION.
PubMed=16408210; DOI=10.1007/s00438-005-0086-4;
Chatterjee I., Gross S.R., Kinzy T.G., Chen K.Y.;
"Rapid depletion of mutant eukaryotic initiation factor 5A at
restrictive temperature reveals connections to actin cytoskeleton and
cell cycle progression.";
Mol. Genet. Genomics 275:264-276(2006).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-74, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[21]
MUTAGENESIS OF GLN-22; SER-24; CYS-39; GLY-50; LYS-51; HIS-52; GLY-53;
HIS-54; LYS-56; VAL-57; THR-66; PRO-83; LEU-93; PRO-116; GLY-118;
LEU-120; ASP-122; LEU-124; SER-140; MET-142; SER-149 AND
116-PRO--ASP-157.
PubMed=18341589; DOI=10.1111/j.1742-4658.2008.06345.x;
Dias C.A.O., Cano V.S.P., Rangel S.M., Apponi L.H., Frigieri M.C.,
Muniz J.R.C., Garcia W., Park M.H., Garratt R.C., Zanelli C.F.,
Valentini S.R.;
"Structural modeling and mutational analysis of yeast eukaryotic
translation initiation factor 5A reveal new critical residues and
reinforce its involvement in protein synthesis.";
FEBS J. 275:1874-1888(2008).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-74, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[23]
FUNCTION.
PubMed=19338753; DOI=10.1016/j.bbrc.2009.01.148;
Gregio A.P.B., Cano V.P.S., Avaca J.S., Valentini S.R., Zanelli C.F.;
"eIF5A has a function in the elongation step of translation in
yeast.";
Biochem. Biophys. Res. Commun. 380:785-790(2009).
[24]
SUBUNIT, HYPUSINE AT LYS-51, AND MUTAGENESIS OF LYS-51.
PubMed=19120453; DOI=10.1111/j.1742-4658.2008.06817.x;
Gentz P.M., Blatch G.L., Dorrington R.A.;
"Dimerization of the yeast eukaryotic translation initiation factor 5A
requires hypusine and is RNA dependent.";
FEBS J. 276:695-706(2009).
[25]
FUNCTION, AND MUTAGENESIS OF LYS-51; ASP-63 AND SER-149.
PubMed=19424157; DOI=10.1038/nature08034;
Saini P., Eyler D.E., Green R., Dever T.E.;
"Hypusine-containing protein eIF5A promotes translation elongation.";
Nature 459:118-121(2009).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND THR-10, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[27]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[28]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-86, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
-!- FUNCTION: mRNA-binding protein involved in translation elongation.
Has an important function at the level of mRNA turnover, probably
acting downstream of decapping. Involved in actin dynamics and
cell cycle progression, mRNA decay and probably in a pathway
involved in stress response and maintenance of cell wall
integrity. Essential for polarized growth, a process necessary for
G1/S transition. May mediate large range of effects of the
polyamine spermidine in the cell. {ECO:0000269|PubMed:10229683,
ECO:0000269|PubMed:16157662, ECO:0000269|PubMed:16408210,
ECO:0000269|PubMed:16914118, ECO:0000269|PubMed:19338753,
ECO:0000269|PubMed:19424157, ECO:0000269|PubMed:641056,
ECO:0000269|PubMed:8307948, ECO:0000269|PubMed:9582285}.
-!- SUBUNIT: Homodimer. Interacts with DYS1 and LIA1.
{ECO:0000269|PubMed:14675757, ECO:0000269|PubMed:16215987,
ECO:0000269|PubMed:19120453}.
-!- INTERACTION:
P53741:BRE5; NbExp=2; IntAct=EBI-9033, EBI-28528;
P38791:DYS1; NbExp=4; IntAct=EBI-9033, EBI-5871;
P47120:LIA1; NbExp=2; IntAct=EBI-9033, EBI-25526;
P0CG63:UBI4; NbExp=2; IntAct=EBI-9033, EBI-7000452;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10229683}.
Note=Concentrates in the perinuclear region.
-!- INDUCTION: Expressed in aerobic conditions.
{ECO:0000269|PubMed:8314769}.
-!- PTM: eIF-5A seems to be the only eukaryotic protein to have a
hypusine residue which is a post-translational modification of a
lysine by the addition of a butylamino group (from spermidine).
-!- MISCELLANEOUS: There are two genes for eIF-5A in yeast.
-!- SIMILARITY: Belongs to the eIF-5A family. {ECO:0000305}.
-!- CAUTION: Was originally thought (PubMed:641056) to be a
translation initiation factor but further analysis
(PubMed:19424157 and PubMed:19338753) clearly suggests that it is
involved in translation elongation and not translation initiation.
subclass. {ECO:0000305|PubMed:641056}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M63541; AAA35155.1; -; Genomic_DNA.
EMBL; X56236; CAA39693.1; -; Genomic_DNA.
EMBL; D83166; BAA11826.1; -; mRNA.
EMBL; U18779; AAB65008.1; -; Genomic_DNA.
EMBL; BK006939; DAA07619.1; -; Genomic_DNA.
PIR; A40259; FIBYA1.
RefSeq; NP_010880.3; NM_001178849.3.
PDB; 3ER0; X-ray; 3.35 A; A/B=1-157.
PDB; 5DAT; X-ray; 3.15 A; f=1-157.
PDB; 5DC3; X-ray; 3.25 A; f=1-157.
PDB; 5DGE; X-ray; 3.45 A; f=1-157.
PDB; 5DGF; X-ray; 3.30 A; f=1-157.
PDB; 5GAK; EM; 3.88 A; q=1-157.
PDB; 5MC6; EM; 3.80 A; BT=1-157.
PDBsum; 3ER0; -.
PDBsum; 5DAT; -.
PDBsum; 5DC3; -.
PDBsum; 5DGE; -.
PDBsum; 5DGF; -.
PDBsum; 5GAK; -.
PDBsum; 5MC6; -.
ProteinModelPortal; P23301; -.
SMR; P23301; -.
BioGrid; 36695; 1042.
DIP; DIP-4230N; -.
IntAct; P23301; 39.
MINT; P23301; -.
STRING; 4932.YEL034W; -.
CarbonylDB; P23301; -.
iPTMnet; P23301; -.
SWISS-2DPAGE; P23301; -.
MaxQB; P23301; -.
PaxDb; P23301; -.
PRIDE; P23301; -.
TopDownProteomics; P23301; -.
EnsemblFungi; YEL034W; YEL034W; YEL034W.
GeneID; 856677; -.
KEGG; sce:YEL034W; -.
EuPathDB; FungiDB:YEL034W; -.
SGD; S000000760; HYP2.
GeneTree; ENSGT00390000003738; -.
HOGENOM; HOG000106270; -.
InParanoid; P23301; -.
KO; K03263; -.
OrthoDB; EOG092C4XQW; -.
BioCyc; YEAST:G3O-30156-MONOMER; -.
Reactome; R-SCE-204626; Hypusine synthesis from eIF5A-lysine.
EvolutionaryTrace; P23301; -.
PRO; PR:P23301; -.
Proteomes; UP000002311; Chromosome V.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:SGD.
GO; GO:0043022; F:ribosome binding; IDA:SGD.
GO; GO:0003723; F:RNA binding; IDA:SGD.
GO; GO:0003746; F:translation elongation factor activity; IDA:SGD.
GO; GO:0003743; F:translation initiation factor activity; IDA:SGD.
GO; GO:1903272; P:positive regulation of cytoplasmic translational elongation through polyproline stretches; IMP:SGD.
GO; GO:0045901; P:positive regulation of translational elongation; IDA:SGD.
GO; GO:0045948; P:positive regulation of translational initiation; IDA:SGD.
GO; GO:0045905; P:positive regulation of translational termination; IDA:SGD.
GO; GO:0006452; P:translational frameshifting; IGI:SGD.
Gene3D; 2.30.30.30; -; 1.
InterPro; IPR001884; IF5A-like.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR014722; Rib_L2_dom2.
InterPro; IPR019769; Trans_elong_IF5A_hypusine_site.
InterPro; IPR020189; Transl_elong_IF5A_C.
InterPro; IPR008991; Translation_prot_SH3-like_sf.
PANTHER; PTHR11673; PTHR11673; 1.
Pfam; PF01287; eIF-5a; 1.
PIRSF; PIRSF003025; eIF5A; 1.
SMART; SM01376; eIF-5a; 1.
SUPFAM; SSF50104; SSF50104; 1.
SUPFAM; SSF50249; SSF50249; 1.
TIGRFAMs; TIGR00037; eIF_5A; 1.
PROSITE; PS00302; IF5A_HYPUSINE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Elongation factor; Hypusine;
Isopeptide bond; Phosphoprotein; Protein biosynthesis;
Reference proteome; RNA-binding; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378,
ECO:0000269|PubMed:8243648}.
CHAIN 2 157 Eukaryotic translation initiation factor
5A-1.
/FTId=PRO_0000142488.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22814378,
ECO:0000269|PubMed:8243648}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000244|PubMed:15665377,
ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198,
ECO:0000269|PubMed:8243648,
ECO:0000269|PubMed:8325852}.
MOD_RES 7 7 Phosphothreonine.
{ECO:0000250|UniProtKB:P19211}.
MOD_RES 10 10 Phosphothreonine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 51 51 Hypusine. {ECO:0000269|PubMed:19120453}.
MOD_RES 74 74 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956}.
CROSSLNK 86 86 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
MUTAGEN 22 22 Q->H: Temperature-sensitive growth
phenotype; when associated with F-93.
{ECO:0000269|PubMed:18341589}.
MUTAGEN 24 24 S->P: Temperature-sensitive growth
phenotype. {ECO:0000269|PubMed:18341589}.
MUTAGEN 39 39 C->Y: Temperature-sensitive growth
phenotype. Lethal; when associated with
L-83 and D-118 or with I-66 and D-118 or
with D-118 and I-142 or with L-116 and D-
118. {ECO:0000269|PubMed:10229683,
ECO:0000269|PubMed:18341589}.
MUTAGEN 50 50 G->A,P: Lethal.
{ECO:0000269|PubMed:18341589}.
MUTAGEN 51 51 K->R: Impairs association to the ribosome
and cell growth.
{ECO:0000269|PubMed:16215987,
ECO:0000269|PubMed:16914118,
ECO:0000269|PubMed:18341589,
ECO:0000269|PubMed:19120453,
ECO:0000269|PubMed:19424157}.
MUTAGEN 52 52 H->A,D: Lethal.
{ECO:0000269|PubMed:18341589}.
MUTAGEN 53 53 G->A,D: Lethal.
{ECO:0000269|PubMed:18341589}.
MUTAGEN 54 54 H->D: Lethal.
{ECO:0000269|PubMed:18341589}.
MUTAGEN 56 56 K->A: Temperature-sensitive growth
phenotype. {ECO:0000269|PubMed:18341589}.
MUTAGEN 56 56 K->D: Lethal.
{ECO:0000269|PubMed:18341589}.
MUTAGEN 57 57 V->D: Temperature-sensitive growth
phenotype. {ECO:0000269|PubMed:18341589}.
MUTAGEN 63 63 D->V: Impairs programmed ribosomal
frameshifting.
{ECO:0000269|PubMed:19424157}.
MUTAGEN 66 66 T->I: Temperature-sensitive growth
phenotype. Lethal; when associated with
Y-39 and D-118.
{ECO:0000269|PubMed:18341589}.
MUTAGEN 83 83 P->S,L: Temperature-sensitive growth
phenotype. Lethal; when associated with
Y-39 and D-118.
{ECO:0000269|PubMed:10229683,
ECO:0000269|PubMed:18341589}.
MUTAGEN 93 93 L->F: Lethal.
{ECO:0000269|PubMed:18341589}.
MUTAGEN 102 102 L->A: Temperature-sensitive growth
phenotype. {ECO:0000269|PubMed:16408210}.
MUTAGEN 116 116 P->L: Temperature-sensitive growth
phenotype; when associated with D-118.
Lethal; when associated with Y-39 and D-
118. {ECO:0000269|PubMed:18341589}.
MUTAGEN 118 118 G->D: Temperature-sensitive growth
phenotype; when associated with L-116 or
W-122 or F-140 or I-142. Lethal; when
associated with Y-39 and I-66 or with Y-
39 and L-83 or with Y-39 and L-116 or
with Y-39 and F-140 or with Y-39 and I-
142 or with N-120 and D-124.
{ECO:0000269|PubMed:18341589}.
MUTAGEN 118 118 G->V: Temperature-sensitive growth
phenotype; when associated with W-122.
{ECO:0000269|PubMed:18341589}.
MUTAGEN 120 120 L->N: Lethal; when associated with D-118
and D-124. {ECO:0000269|PubMed:18341589}.
MUTAGEN 122 122 D->W: Temperature-sensitive growth
phenotype; when associated with V-118.
{ECO:0000269|PubMed:18341589}.
MUTAGEN 124 124 L->D: Lethal; when associated with D-118
and N-120. {ECO:0000269|PubMed:18341589}.
MUTAGEN 140 140 S->F: Temperature-sensitive growth
phenotype; when associated with D-118.
Lethal; when associated with Y-39 and D-
118. {ECO:0000269|PubMed:18341589}.
MUTAGEN 142 142 M->I: Temperature-sensitive growth
phenotype; when associated with D-118.
Lethal; when associated with Y-39 and D-
118. {ECO:0000269|PubMed:18341589}.
MUTAGEN 149 149 S->P: In ts1159; temperature-sensitive
growth phenotype and impairs programmed
ribosomal frameshifting.
{ECO:0000269|PubMed:18341589,
ECO:0000269|PubMed:19424157,
ECO:0000269|PubMed:9582285}.
STRAND 19 22 {ECO:0000244|PDB:3ER0}.
TURN 23 25 {ECO:0000244|PDB:3ER0}.
STRAND 31 34 {ECO:0000244|PDB:3ER0}.
STRAND 37 47 {ECO:0000244|PDB:3ER0}.
STRAND 50 53 {ECO:0000244|PDB:3ER0}.
STRAND 56 66 {ECO:0000244|PDB:3ER0}.
STRAND 70 82 {ECO:0000244|PDB:3ER0}.
STRAND 87 91 {ECO:0000244|PDB:3ER0}.
TURN 96 99 {ECO:0000244|PDB:3ER0}.
STRAND 105 107 {ECO:0000244|PDB:3ER0}.
HELIX 120 126 {ECO:0000244|PDB:3ER0}.
STRAND 135 141 {ECO:0000244|PDB:3ER0}.
STRAND 144 150 {ECO:0000244|PDB:3ER0}.
SEQUENCE 157 AA; 17114 MW; 738F29CCC7820C47 CRC64;
MSDEEHTFET ADAGSSATYP MQCSALRKNG FVVIKSRPCK IVDMSTSKTG KHGHAKVHLV
AIDIFTGKKL EDLSPSTHNM EVPVVKRNEY QLLDIDDGFL SLMNMDGDTK DDVKAPEGEL
GDSLQTAFDE GKDLMVTIIS AMGEEAAISF KEAARTD


Related products :

Catalog number Product name Quantity
10-288-22403F Eukaryotic translation initiation factor 4E type 3 - eIF4E type 3; eIF-4E type 3; mRNA cap-binding protein type 3; Eukaryotic translation initiation factor 4E-like 3; Eukaryotic translation initiation 0.1 mg
10-288-22403F Eukaryotic translation initiation factor 4E type 3 - eIF4E type 3; eIF-4E type 3; mRNA cap-binding protein type 3; Eukaryotic translation initiation factor 4E-like 3; Eukaryotic translation initiation 0.05 mg
15-288-22403A Eukaryotic translation initiation factor 4E type 3 - eIF4E type 3; eIF-4E type 3; mRNA cap-binding protein type 3; Eukaryotic translation initiation factor 4E-like 3; Eukaryotic translation initiation 0.05 mg
15-288-22403A Eukaryotic translation initiation factor 4E type 3 - eIF4E type 3; eIF-4E type 3; mRNA cap-binding protein type 3; Eukaryotic translation initiation factor 4E-like 3; Eukaryotic translation initiation 0.1 mg
18-003-43602 Eukaryotic translation initiation factor 4E type 2 - eIF4E type 2; eIF-4E type 2; mRNA cap-binding protein type 3; Eukaryotic translation initiation factor 4E-like 3; Eukaryotic translation initiation 0.1 mg Protein A
EIAAB12703 65 kDa eukaryotic translation initiation factor 2A,CDA02,EIF2A,eIF-2A,Eukaryotic translation initiation factor 2A,Homo sapiens,Human,MSTP004,MSTP089
EIAAB12726 eIF-3 p48,eIF3e,Eif3e,Eif3s6,Eukaryotic translation initiation factor 3 subunit 6,Eukaryotic translation initiation factor 3 subunit E,Int6,Mammary tumor-associated protein INT-6,MMTV integration site
18-003-42779 Probable ATP-dependent RNA helicase DDX48 - EC 3.6.1.-; DEAD box protein 48; Eukaryotic initiation factor 4A-like NUK-34; Nuclear matrix protein 265; hNMP 265; Eukaryotic translation initiation factor 0.1 mg Protein A
EIAAB12755 EIF3EIP,eIF3l,EIF3L,EIF3S6IP,Eukaryotic translation initiation factor 3 subunit 6-interacting protein,Eukaryotic translation initiation factor 3 subunit E-interacting protein,Eukaryotic translation in
25-604 Translation initiation is mediated by specific recognition of the cap structure by eukaryotic translation initiation factor 4F (eIF4F), which is a cap binding protein complex that consists of three su 0.05 mg
29-272 Translation initiation is mediated by specific recognition of the cap structure by eukaryotic translation initiation factor 4F (eIF4F), which is a cap binding protein complex that consists of three su 0.05 mg
EIAAB12723 eIF-3 p48,eIF3e,EIF3E,EIF3S6,Eukaryotic translation initiation factor 3 subunit 6,Eukaryotic translation initiation factor 3 subunit E,Homo sapiens,Human,INT6,Viral integration site protein INT-6 homo
EIAAB12753 66 kDa tyrosine-rich heat shock protein,67 kDa polymerase-associated factor,Eif3eip,eIF3l,Eif3l,Eif3s6ip,Eukaryotic translation initiation factor 3 subunit 6-interacting protein,Eukaryotic translation
EIAAB12752 Bos taurus,Bovine,EIF3EIP,eIF3l,EIF3L,EIF3S6IP,Eukaryotic translation initiation factor 3 subunit 6-interacting protein,Eukaryotic translation initiation factor 3 subunit E-interacting protein,Eukaryo
EIAAB12749 ARG134,eIF-3 p25,eIF-3 p28,eIF3k,EIF3K,EIF3S12,Eukaryotic translation initiation factor 3 subunit 12,Eukaryotic translation initiation factor 3 subunit K,Homo sapiens,HSPC029,Human,MSTP001,Muscle-spec
EIAAB12748 eIF3 p35,eIF-3-alpha,eIF3j,EIF3J,EIF3S1,Eukaryotic translation initiation factor 3 subunit 1,Eukaryotic translation initiation factor 3 subunit J,Homo sapiens,Human,PRO0391
EIAAB12729 eIF3 p47,eIF-3-epsilon,eIF3f,EIF3F,EIF3S5,Eukaryotic translation initiation factor 3 subunit 5,Eukaryotic translation initiation factor 3 subunit F,Homo sapiens,Human
EIAAB12721 eIF3 p66,eIF3d,EIF3D,EIF3S7,eIF-3-zeta,Eukaryotic translation initiation factor 3 subunit 7,Eukaryotic translation initiation factor 3 subunit D,Homo sapiens,Human
EIAAB12715 eIF3 p110,eIF3c,EIF3C,EIF3S8,Eukaryotic translation initiation factor 3 subunit 8,Eukaryotic translation initiation factor 3 subunit C,Homo sapiens,Human
EIAAB12743 eIF3 p36,eIF-3-beta,eIF3i,EIF3I,EIF3S2,Eukaryotic translation initiation factor 3 subunit 2,Eukaryotic translation initiation factor 3 subunit I,Oryctolagus cuniculus,Rabbit
EIAAB12740 Bos taurus,Bovine,eIF3 p36,eIF-3-beta,eIF3i,EIF3I,EIF3S2,Eukaryotic translation initiation factor 3 subunit 2,Eukaryotic translation initiation factor 3 subunit I
E1885r ELISA eIF3a,Eif3a,Eif3s10,eIF-3-theta,Eukaryotic translation initiation factor 3 subunit 10,Eukaryotic translation initiation factor 3 subunit A,Rat,Rattus norvegicus 96T
U1885r CLIA eIF3a,Eif3a,Eif3s10,eIF-3-theta,Eukaryotic translation initiation factor 3 subunit 10,Eukaryotic translation initiation factor 3 subunit A,Rat,Rattus norvegicus 96T
EIAAB12745 Bos taurus,Bovine,eIF3 p35,eIF-3-alpha,eIF3j,EIF3J,EIF3S1,Eukaryotic translation initiation factor 3 subunit 1,Eukaryotic translation initiation factor 3 subunit J
E1885r ELISA kit eIF3a,Eif3a,Eif3s10,eIF-3-theta,Eukaryotic translation initiation factor 3 subunit 10,Eukaryotic translation initiation factor 3 subunit A,Rat,Rattus norvegicus 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur