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Protein

Eukaryotic translation initiation factor 5

Gene

TIF5

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of GTP bound to the 40S ribosomal initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) with the subsequent joining of a 60S ribosomal subunit resulting in the release of eIF-2 and the guanine nucleotide. The subsequent joining of a 60S ribosomal subunit results in the formation of a functional 80S initiation complex (80S.mRNA.Met-tRNA[F]). eIF-5 is essential for cell viability.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi27 – 348GTPSequence analysis

GO - Molecular functioni

  • GDP-dissociation inhibitor activity Source: SGD
  • GTPase activator activity Source: SGD
  • GTP binding Source: UniProtKB-KW
  • translation initiation factor activity Source: SGD
  • translation initiation factor binding Source: SGD

GO - Biological processi

  • formation of cytoplasmic translation initiation complex Source: SGD
  • mature ribosome assembly Source: SGD
  • negative regulation of translational initiation Source: SGD
  • positive regulation of GTPase activity Source: GOC
  • regulation of catalytic activity Source: GOC
  • regulation of translational initiation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-34197-MONOMER.
ReactomeiR-SCE-72702. Ribosomal scanning and start codon recognition.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 5
Short name:
eIF-5
Gene namesi
Name:TIF5
Ordered Locus Names:YPR041W
ORF Names:YP3085.05
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPR041W.
SGDiS000006245. TIF5.

Subcellular locationi

GO - Cellular componenti

  • cytosolic small ribosomal subunit Source: SGD
  • eukaryotic 48S preinitiation complex Source: SGD
  • multi-eIF complex Source: SGD
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi343 – 36422LPKIL…EIMRF → APKAAVQAANNDAASAAEAA RA in TIF5-12A; Abolishes binding to SUI3 and NIP1. Add
BLAST
Mutagenesisi388 – 39811FITWLETAESD → AATAAETAAAA in TIF5-7A; Abolishes binding to SUI3 and NIP1. 1 PublicationAdd
BLAST

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 405405Eukaryotic translation initiation factor 5PRO_0000007791Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei170 – 1701PhosphoserineCombined sources
Modified residuei172 – 1721PhosphoserineCombined sources
Modified residuei191 – 1911PhosphothreonineCombined sources
Modified residuei228 – 2281PhosphoserineCombined sources
Modified residuei317 – 3171PhosphothreonineCombined sources
Modified residuei397 – 3971PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP38431.
PeptideAtlasiP38431.

PTM databases

iPTMnetiP38431.

Interactioni

Subunit structurei

Monomer. Interacts with NIP1 and SUI3. The factors eIF-1, eIF-2, eIF-3, TIF5/eIF-5 and methionyl-tRNAi form a multifactor complex (MFC) that may bind to the 40S ribosome. TIF32, NIP1 and TIF5/eIF-5 comprise a minimal 40S-ribosome-binding unit.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NIP1P324975EBI-9038,EBI-8965

GO - Molecular functioni

  • translation initiation factor binding Source: SGD

Protein-protein interaction databases

BioGridi36218. 90 interactions.
DIPiDIP-2303N.
IntActiP38431. 40 interactions.
MINTiMINT-564473.

Structurei

Secondary structure

1
405
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi244 – 25916Combined sources
Helixi269 – 27810Combined sources
Helixi287 – 2948Combined sources
Helixi300 – 3034Combined sources
Helixi308 – 3147Combined sources
Helixi318 – 33316Combined sources
Helixi337 – 3426Combined sources
Helixi343 – 35210Combined sources
Helixi358 – 3669Combined sources
Beta strandi370 – 3734Combined sources
Helixi375 – 3839Combined sources
Helixi386 – 3949Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FULX-ray1.50A/B/C/D/E/F241-405[»]
ProteinModelPortaliP38431.
SMRiP38431. Positions 1-154, 241-396.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38431.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini241 – 402162W2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi152 – 1565Poly-Lys
Compositional biasi396 – 40510Asp/Glu-rich (acidic)

Sequence similaritiesi

Belongs to the eIF-2-beta/eIF-5 family.Curated
Contains 1 W2 domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00390000016478.
HOGENOMiHOG000214327.
InParanoidiP38431.
KOiK03262.
OMAiTWLENAE.
OrthoDBiEOG7B05QM.

Family and domain databases

Gene3Di1.25.40.180. 1 hit.
3.30.30.50. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR016021. MIF4-like.
IPR002735. Transl_init_fac_IF2/IF5.
IPR016189. Transl_init_fac_IF2/IF5_N.
IPR016190. Transl_init_fac_IF2/IF5_Zn-bd.
IPR003307. W2_domain.
[Graphical view]
PfamiPF01873. eIF-5_eIF-2B. 1 hit.
PF02020. W2. 1 hit.
[Graphical view]
SMARTiSM00653. eIF2B_5. 1 hit.
SM00515. eIF5C. 1 hit.
[Graphical view]
SUPFAMiSSF100966. SSF100966. 1 hit.
SSF48371. SSF48371. 1 hit.
SSF75689. SSF75689. 1 hit.
PROSITEiPS51363. W2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform Long (identifier: P38431-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSINICRDNH DPFYRYKMPP IQAKVEGRGN GIKTAVLNVA DISHALNRPA
60 70 80 90 100
PYIVKYFGFE LGAQTSISVD KDRYLVNGVH EPAKLQDVLD GFINKFVLCG
110 120 130 140 150
SCKNPETEII ITKDNDLVRD CKACGKRTPM DLRHKLSSFI LKNPPDSVSG
160 170 180 190 200
SKKKKKAATA SANVRGGGLS ISDIAQGKSQ NAPSDGTGSS TPQHHDEDED
210 220 230 240 250
ELSRQIKAAA STLEDIEVKD DEWAVDMSEE AIRARAKELE VNSELTQLDE
260 270 280 290 300
YGEWILEQAG EDKENLPSDV ELYKKAAELD VLNDPKIGCV LAQCLFDEDI
310 320 330 340 350
VNEIAEHNAF FTKILVTPEY EKNFMGGIER FLGLEHKDLI PLLPKILVQL
360 370 380 390 400
YNNDIISEEE IMRFGTKSSK KFVPKEVSKK VRRAAKPFIT WLETAESDDD

EEDDE
Length:405
Mass (Da):45,261
Last modified:October 1, 1994 - v1
Checksum:i1A1DA563B4ED1B1F
GO
Isoform Short (identifier: P38431-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-17: Missing.

Note: Produced by alternative initiation at Met-18 of isoform Long.
Show »
Length:388
Mass (Da):43,107
Checksum:iD988447BA354E2AD
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1717Missing in isoform Short. CuratedVSP_018724Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L10840 Genomic DNA. No translation available.
Z71255 Genomic DNA. Translation: CAA94989.1.
Z68111 Genomic DNA. Translation: CAA92145.1.
Z73616 Genomic DNA. Translation: CAA97991.1.
BK006949 Genomic DNA. Translation: DAA11466.1.
PIRiA46699.
RefSeqiNP_015366.1. NM_001184138.1. [P38431-1]

Genome annotation databases

EnsemblFungiiYPR041W; YPR041W; YPR041W. [P38431-1]
GeneIDi856154.
KEGGisce:YPR041W.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L10840 Genomic DNA. No translation available.
Z71255 Genomic DNA. Translation: CAA94989.1.
Z68111 Genomic DNA. Translation: CAA92145.1.
Z73616 Genomic DNA. Translation: CAA97991.1.
BK006949 Genomic DNA. Translation: DAA11466.1.
PIRiA46699.
RefSeqiNP_015366.1. NM_001184138.1. [P38431-1]

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FULX-ray1.50A/B/C/D/E/F241-405[»]
ProteinModelPortaliP38431.
SMRiP38431. Positions 1-154, 241-396.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36218. 90 interactions.
DIPiDIP-2303N.
IntActiP38431. 40 interactions.
MINTiMINT-564473.

PTM databases

iPTMnetiP38431.

Proteomic databases

MaxQBiP38431.
PeptideAtlasiP38431.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPR041W; YPR041W; YPR041W. [P38431-1]
GeneIDi856154.
KEGGisce:YPR041W.

Organism-specific databases

EuPathDBiFungiDB:YPR041W.
SGDiS000006245. TIF5.

Phylogenomic databases

GeneTreeiENSGT00390000016478.
HOGENOMiHOG000214327.
InParanoidiP38431.
KOiK03262.
OMAiTWLENAE.
OrthoDBiEOG7B05QM.

Enzyme and pathway databases

BioCyciYEAST:G3O-34197-MONOMER.
ReactomeiR-SCE-72702. Ribosomal scanning and start codon recognition.

Miscellaneous databases

EvolutionaryTraceiP38431.
NextBioi981286.
PROiP38431.

Family and domain databases

Gene3Di1.25.40.180. 1 hit.
3.30.30.50. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR016021. MIF4-like.
IPR002735. Transl_init_fac_IF2/IF5.
IPR016189. Transl_init_fac_IF2/IF5_N.
IPR016190. Transl_init_fac_IF2/IF5_Zn-bd.
IPR003307. W2_domain.
[Graphical view]
PfamiPF01873. eIF-5_eIF-2B. 1 hit.
PF02020. W2. 1 hit.
[Graphical view]
SMARTiSM00653. eIF2B_5. 1 hit.
SM00515. eIF5C. 1 hit.
[Graphical view]
SUPFAMiSSF100966. SSF100966. 1 hit.
SSF48371. SSF48371. 1 hit.
SSF75689. SSF75689. 1 hit.
PROSITEiPS51363. W2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Eukaryotic translation initiation factor 5 from Saccharomyces cerevisiae. Cloning, characterization, and expression of the gene encoding the 45,346-Da protein."
    Chakravarti D., Maitra U.
    J. Biol. Chem. 268:10524-10533(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 19-30; 326-340 AND 363-377.
    Strain: ATCC 26109 / X2180.
  2. "Functional analysis of three adjacent open reading frames from the right arm of yeast chromosome XVI."
    Waskiewicz-Staniorowska B., Skala J., Jasinski M., Grenson M., Goffeau A., Ulaszewski S.
    Yeast 14:1027-1039(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 46191 / IL125-2B.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
    , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
    Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Identification of a translation initiation factor 3 (eIF3) core complex, conserved in yeast and mammals, that interacts with eIF5."
    Phan L., Zhang X., Asano K., Anderson J., Vornlocher H.-P., Greenberg J.R., Qin J., Hinnebusch A.G.
    Mol. Cell. Biol. 18:4935-4946(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NIP1.
  6. "Conserved bipartite motifs in yeast eIF5 and eIF2Bepsilon, GTPase-activating and GDP-GTP exchange factors in translation initiation, mediate binding to their common substrate eIF2."
    Asano K., Krishnamoorthy T., Phan L., Pavitt G.D., Hinnebusch A.G.
    EMBO J. 18:1673-1688(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SUI3 AND NIP1, MUTAGENESIS OF 342-LYS--PHE-364 AND 388-PHE--ASP-398.
  7. "The yeast eIF3 subunits TIF32/a, NIP1/c, and eIF5 make critical connections with the 40S ribosome in vivo."
    Valasek L., Mathew A.A., Shin B.-S., Nielsen K.H., Szamecz B., Hinnebusch A.G.
    Genes Dev. 17:786-799(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ASSOCIATION WITH THE 40S RIBOSOME.
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "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 THR-191 AND SER-397, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  10. "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-228; THR-317 AND SER-397, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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-170; SER-172; THR-191 AND SER-397, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiIF5_YEAST
AccessioniPrimary (citable) accession number: P38431
Secondary accession number(s): D6W450
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: May 11, 2016
This is version 159 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 48300 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Translation initiation factors
    List of translation initiation factor entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.