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P23301 (IF5A1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Eukaryotic translation initiation factor 5A-1

Short name=eIF-5A-1
Alternative name(s):
Hypusine-containing protein HP2
eIF-4D
Gene names
Name:HYP2
Synonyms:TIF51A
Ordered Locus Names:YEL034W
ORF Names:SYGP-ORF21
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length157 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.7 Ref.11 Ref.12 Ref.13 Ref.15 Ref.17 Ref.19 Ref.23 Ref.25

Subunit structure

Homodimer. Interacts with DYS1 and LIA1. Ref.14 Ref.18 Ref.24

Subcellular location

Cytoplasm. Note: Concentrates in the perinuclear region. Ref.13

Induction

Expressed in aerobic conditions. Ref.9

Post-translational modification

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.

Sequence similarities

Belongs to the eIF-5A family.

Caution

Was originally thought (Ref.7) to be a translation initiation factor but further analysis (Ref.25 and Ref.23) clearly suggests that it is involved in translation elongation and not translation initiation. subclass.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DYS1P387914EBI-9033,EBI-5871
LIA1P471202EBI-9033,EBI-25526

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 157156Eukaryotic translation initiation factor 5A-1
PRO_0000142488

Amino acid modifications

Modified residue21N-acetylserine Ref.6 Ref.27
Modified residue21Phosphoserine Ref.6 Ref.10 Ref.16 Ref.20 Ref.22 Ref.26
Modified residue71Phosphothreonine By similarity
Modified residue101Phosphothreonine Ref.26
Modified residue511Hypusine
Modified residue741Phosphoserine Ref.20 Ref.22

Experimental info

Mutagenesis221Q → H: Temperature-sensitive growth phenotype; when associated with F-93. Ref.21
Mutagenesis241S → P: Temperature-sensitive growth phenotype. Ref.21
Mutagenesis391C → 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. Ref.13 Ref.21
Mutagenesis501G → A or P: Lethal. Ref.21
Mutagenesis511K → R: Impairs association to the ribosome and cell growth. Ref.17 Ref.18 Ref.21 Ref.24 Ref.25
Mutagenesis521H → A or D: Lethal. Ref.21
Mutagenesis531G → A or D: Lethal. Ref.21
Mutagenesis541H → D: Lethal. Ref.21
Mutagenesis561K → A: Temperature-sensitive growth phenotype. Ref.21
Mutagenesis561K → D: Lethal. Ref.21
Mutagenesis571V → D: Temperature-sensitive growth phenotype. Ref.21
Mutagenesis631D → V: Impairs programmed ribosomal frameshifting. Ref.25
Mutagenesis661T → I: Temperature-sensitive growth phenotype. Lethal; when associated with Y-39 and D-118. Ref.21
Mutagenesis831P → S or L: Temperature-sensitive growth phenotype. Lethal; when associated with Y-39 and D-118. Ref.13 Ref.21
Mutagenesis931L → F: Lethal. Ref.21
Mutagenesis1021L → A: Temperature-sensitive growth phenotype. Ref.19
Mutagenesis1161P → L: Temperature-sensitive growth phenotype; when associated with D-118. Lethal; when associated with Y-39 and D-118. Ref.21
Mutagenesis1181G → 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. Ref.13 Ref.21
Mutagenesis1181G → V: Temperature-sensitive growth phenotype; when associated with W-122. Ref.21
Mutagenesis1201L → N: Lethal; when associated with D-118 and D-124. Ref.21
Mutagenesis1221D → W: Temperature-sensitive growth phenotype; when associated with V-118. Ref.21
Mutagenesis1241L → D: Lethal; when associated with D-118 and N-120. Ref.21
Mutagenesis1401S → F: Temperature-sensitive growth phenotype; when associated with D-118. Lethal; when associated with Y-39 and D-118. Ref.21
Mutagenesis1421M → I: Temperature-sensitive growth phenotype; when associated with D-118. Lethal; when associated with Y-39 and D-118. Ref.21
Mutagenesis1491S → P in ts1159; temperature-sensitive growth phenotype and impairs programmed ribosomal frameshifting. Ref.12 Ref.21 Ref.25

Secondary structure

.......................... 157
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P23301 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 738F29CCC7820C47

FASTA15717,114
        10         20         30         40         50         60 
MSDEEHTFET ADAGSSATYP MQCSALRKNG FVVIKSRPCK IVDMSTSKTG KHGHAKVHLV 

        70         80         90        100        110        120 
AIDIFTGKKL EDLSPSTHNM EVPVVKRNEY QLLDIDDGFL SLMNMDGDTK DDVKAPEGEL 

       130        140        150 
GDSLQTAFDE GKDLMVTIIS AMGEEAAISF KEAARTD 

« Hide

References

« Hide 'large scale' references
[1]"Translation initiation factor 5A and its hypusine modification are essential for cell viability in the yeast Saccharomyces cerevisiae."
Schnier J., Schwelberger H.G., Smit-Mcbride Z., Kang H.A., Hershey J.W.B.
Mol. Cell. Biol. 11:3105-3114(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Sandholzer U.R.
Submitted (DEC-1990) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: DBY874.
[3]"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."
Kitaoka Y., Miyazaki M.
Nucleic Acids Symp. Ser. 22:69-70(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"The nucleotide sequence of Saccharomyces cerevisiae chromosome V."
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. expand/collapse author list , 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.
Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[6]"Determination and mutational analysis of the phosphorylation site in the hypusine-containing protein Hyp2p."
Klier H., Woehl T., Eckerskorn C., Magdolen V., Lottspeich F.
FEBS Lett. 334:360-364(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, ACETYLATION AT SER-2, PHOSPHORYLATION AT SER-2.
[7]"The mechanism of action of protein synthesis initiation factors from rabbit reticulocytes."
Benne R., Hershey J.W.B.
J. Biol. Chem. 253:3078-3087(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Hypusine formation in eukaryotic initiation factor 4D is not reversed when rates or specificity of protein synthesis is altered."
Gordon E.D., Mora R., Meredith S.C., Lindquist S.L.
J. Biol. Chem. 262:16590-16595(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: HYPUSINE FORMATION.
[9]"Translation initiation factor eIF-5A expressed from either of two yeast genes or from human cDNA. Functional identity under aerobic and anaerobic conditions."
Schwelberger H.G., Kang H.A., Hershey J.W.B.
J. Biol. Chem. 268:14018-14025(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[10]"Translation initiation factor eIF-5A, the hypusine-containing protein, is phosphorylated on serine in Saccharomyces cerevisiae."
Kang H.A., Schwelberger H.G., Hershey J.W.B.
J. Biol. Chem. 268:14750-14756(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-2.
[11]"Effect of initiation factor eIF-5A depletion on protein synthesis and proliferation of Saccharomyces cerevisiae."
Kang H.A., Hershey J.W.B.
J. Biol. Chem. 269:3934-3940(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"A single amino acid substitution in yeast eIF-5A results in mRNA stabilization."
Zuk D., Jacobson A.
EMBO J. 17:2914-2925(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF SER-149, FUNCTION.
[13]"Complex formation between deoxyhypusine synthase and its protein substrate, the eukaryotic translation initiation factor 5A (eIF5A) precursor."
Lee Y.B., Joe Y.A., Wolff E.C., Dimitriadis E.K., Park M.H.
Biochem. J. 340:273-281(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF CYS-39 AND PRO-83.
[14]"Mapping eIF5A binding sites for Dys1 and Lia1: in vivo evidence for regulation of eIF5A hypusination."
Thompson G.M., Cano V.S.P., Valentini S.R.
FEBS Lett. 555:464-468(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DYS1 AND LIA1.
[15]"Pkc1 acts through Zds1 and Gic1 to suppress growth and cell polarity defects of a yeast eIF5A mutant."
Zanelli C.F., Valentini S.R.
Genetics 171:1571-1581(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: YAL6B.
[17]"eIF5A binds to translational machinery components and affects translation in yeast."
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.
Biochem. Biophys. Res. Commun. 348:1358-1366(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ASSOCIATION WITH THE 80S RIBOSOME, MUTAGENESIS OF LYS-51.
[18]"Tandem affinity purification revealed the hypusine-dependent binding of eukaryotic initiation factor 5A to the translating 80S ribosomal complex."
Jao D.L., Chen K.Y.
J. Cell. Biochem. 97:583-598(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DYS1, ASSOCIATION WITH THE 80S RIBOSOME, MUTAGENESIS OF LYS-51.
[19]"Rapid depletion of mutant eukaryotic initiation factor 5A at restrictive temperature reveals connections to actin cytoskeleton and cell cycle progression."
Chatterjee I., Gross S.R., Kinzy T.G., Chen K.Y.
Mol. Genet. Genomics 275:264-276(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF LEU-102, FUNCTION.
[20]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-74, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[21]"Structural modeling and mutational analysis of yeast eukaryotic translation initiation factor 5A reveal new critical residues and reinforce its involvement in protein synthesis."
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.
FEBS J. 275:1874-1888(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: 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.
[22]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-74, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"eIF5A has a function in the elongation step of translation in yeast."
Gregio A.P.B., Cano V.P.S., Avaca J.S., Valentini S.R., Zanelli C.F.
Biochem. Biophys. Res. Commun. 380:785-790(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[24]"Dimerization of the yeast eukaryotic translation initiation factor 5A requires hypusine and is RNA dependent."
Gentz P.M., Blatch G.L., Dorrington R.A.
FEBS J. 276:695-706(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, MUTAGENESIS OF LYS-51.
[25]"Hypusine-containing protein eIF5A promotes translation elongation."
Saini P., Eyler D.E., Green R., Dever T.E.
Nature 459:118-121(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF LYS-51; ASP-63 AND SER-149.
[26]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND THR-10, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"Sites of ubiquitin attachment in Saccharomyces cerevisiae."
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M63541 Genomic DNA. Translation: AAA35155.1.
X56236 Genomic DNA. Translation: CAA39693.1.
D83166 mRNA. Translation: BAA11826.1.
U18779 Genomic DNA. Translation: AAB65008.1.
BK006939 Genomic DNA. Translation: DAA07619.1.
PIRFIBYA1. A40259.
RefSeqNP_010880.3. NM_001178849.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3ER0X-ray3.35A/B1-157[»]
ProteinModelPortalP23301.
SMRP23301. Positions 12-157.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36695. 155 interactions.
DIPDIP-4230N.
IntActP23301. 8 interactions.
MINTMINT-545311.
STRING4932.YEL034W.

2D gel databases

SWISS-2DPAGEP23301.

Proteomic databases

PaxDbP23301.
PeptideAtlasP23301.
PRIDEP23301.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYEL034W; YEL034W; YEL034W.
GeneID856677.
KEGGsce:YEL034W.

Organism-specific databases

SGDS000000760. HYP2.

Phylogenomic databases

eggNOGCOG0231.
GeneTreeENSGT00390000003738.
HOGENOMHOG000106270.
KOK03263.
OrthoDBEOG7WMCWW.

Enzyme and pathway databases

BioCycYEAST:G3O-30156-MONOMER.

Gene expression databases

GenevestigatorP23301.

Family and domain databases

Gene3D2.30.30.30. 1 hit.
2.40.50.140. 1 hit.
InterProIPR012340. NA-bd_OB-fold.
IPR014722. Rib_L2_dom2.
IPR019769. Trans_elong_IF5A_hypusine_site.
IPR001884. Transl_elong_IF5A.
IPR020189. Transl_elong_IF5A_C.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERPTHR11673. PTHR11673. 1 hit.
PfamPF01287. eIF-5a. 1 hit.
[Graphical view]
PIRSFPIRSF003025. eIF5A. 1 hit.
SUPFAMSSF50104. SSF50104. 1 hit.
SSF50249. SSF50249. 1 hit.
TIGRFAMsTIGR00037. eIF_5A. 1 hit.
PROSITEPS00302. IF5A_HYPUSINE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP23301.
NextBio982702.

Entry information

Entry nameIF5A1_YEAST
AccessionPrimary (citable) accession number: P23301
Secondary accession number(s): D3DLL5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 140 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome V

Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Translation initiation factors

List of translation initiation factor entries