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Protein

Eukaryotic translation initiation factor 4B

Gene

TIF3

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

Involved in translation initiation. May be the homolog of mammalian eIF4B and be part of an RNA helicase. STM1/TIF3 is a non-essential gene.

GO - Molecular functioni

  1. nucleotide binding Source: InterPro
  2. ribosomal small subunit binding Source: SGD
  3. RNA binding Source: SGD
  4. RNA strand annealing activity Source: SGD
  5. RNA strand-exchange activity Source: SGD
  6. single-stranded RNA binding Source: SGD
  7. translation initiation factor activity Source: UniProtKB-KW

GO - Biological processi

  1. cytoplasmic translation Source: SGD
  2. eukaryotic translation initiation factor 4F complex assembly Source: SGD
  3. formation of translation preinitiation complex Source: SGD
  4. translational initiation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-34292-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 4B
Short name:
eIF-4B
Gene namesi
Name:TIF3
Synonyms:STM1, TIF42
Ordered Locus Names:YPR163C
ORF Names:P9325.6
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XVI

Organism-specific databases

CYGDiYPR163c.
SGDiS000006367. TIF3.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi106 – 1061N → G, V or Y: Retention of function. 1 Publication
Mutagenesisi106 – 1061N → S or P: Loss of function. 1 Publication
Mutagenesisi150 – 1501A → S or C: Retention of function. 1 Publication
Mutagenesisi150 – 1501A → Y, F, N or L: Loss of function. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 436436Eukaryotic translation initiation factor 4BPRO_0000081618Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei65 – 651Phosphoserine2 Publications
Modified residuei71 – 711Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP34167.
PaxDbiP34167.
PeptideAtlasiP34167.

Expressioni

Gene expression databases

GenevestigatoriP34167.

Interactioni

Protein-protein interaction databases

BioGridi36336. 42 interactions.
DIPiDIP-3806N.
IntActiP34167. 5 interactions.
MINTiMINT-406545.
STRINGi4932.YPR163C.

Structurei

3D structure databases

ProteinModelPortaliP34167.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini101 – 18383RRMPROSITE-ProRule annotationAdd
BLAST
Repeati190 – 210211; approximateAdd
BLAST
Repeati211 – 232222Add
BLAST
Repeati233 – 258263Add
BLAST
Repeati259 – 284264Add
BLAST
Repeati285 – 310265Add
BLAST
Repeati311 – 340306Add
BLAST
Repeati341 – 350107; truncated

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni190 – 3501617 X approximate tandem repeatsAdd
BLAST

Sequence similaritiesi

Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG238591.
HOGENOMiHOG000248309.
InParanoidiP34167.
KOiK03258.
OMAiDWSSARG.
OrthoDBiEOG7D59Z7.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P34167-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAPPKKTVKK MDLTSFLNDD TFGSSWAEED VDLNKITIPI ETANANTIPL
60 70 80 90 100
SELAHAKNNS NNTRSGGFGG SFGGRSRLDP ALGGGSSDRR EEYPVPDAPP
110 120 130 140 150
YRAVINNIPW DITPEGVQAW VEDGLVKPEA VEEVVLPKNL RDPTRLKGNA
160 170 180 190 200
FVTLKERADL VAVLKFNGTK LNERTVYVSV AAPRRGGGAD VDWSSARGSN
210 220 230 240 250
FQGDGREDAP DLDWGAARGS NFRGPRRERE EVDIDWTAAR GSNFQGSSRP
260 270 280 290 300
PRREREEVDI DWSAARGSNF QGSSRPPRRE REEPDIDWSA ARGSNFQSSS
310 320 330 340 350
RPPRREREEP DIDWSAARGS NFQSSSRPPR REREKEEPAL DWGAARGAQF
360 370 380 390 400
GKPQQTKNTY KDRSLTNKKT TDEQPKIQKS VYDVLRTEDD DEDEEAEKQN
410 420 430
GDAKENKVDA AVEKLQDKTA QLTVEDGDNW EVVGKK
Length:436
Mass (Da):48,522
Last modified:February 1, 1994 - v1
Checksum:i1DFE89D90BF7D677
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X71996 Genomic DNA. Translation: CAA50870.1.
U25840 Genomic DNA. Translation: AAB68150.1.
AY693114 Genomic DNA. Translation: AAT93133.1.
BK006949 Genomic DNA. Translation: DAA11580.1.
PIRiS37302.
RefSeqiNP_015489.1. NM_001184260.1.

Genome annotation databases

EnsemblFungiiYPR163C; YPR163C; YPR163C.
GeneIDi856292.
KEGGisce:YPR163C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X71996 Genomic DNA. Translation: CAA50870.1.
U25840 Genomic DNA. Translation: AAB68150.1.
AY693114 Genomic DNA. Translation: AAT93133.1.
BK006949 Genomic DNA. Translation: DAA11580.1.
PIRiS37302.
RefSeqiNP_015489.1. NM_001184260.1.

3D structure databases

ProteinModelPortaliP34167.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36336. 42 interactions.
DIPiDIP-3806N.
IntActiP34167. 5 interactions.
MINTiMINT-406545.
STRINGi4932.YPR163C.

Proteomic databases

MaxQBiP34167.
PaxDbiP34167.
PeptideAtlasiP34167.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPR163C; YPR163C; YPR163C.
GeneIDi856292.
KEGGisce:YPR163C.

Organism-specific databases

CYGDiYPR163c.
SGDiS000006367. TIF3.

Phylogenomic databases

eggNOGiNOG238591.
HOGENOMiHOG000248309.
InParanoidiP34167.
KOiK03258.
OMAiDWSSARG.
OrthoDBiEOG7D59Z7.

Enzyme and pathway databases

BioCyciYEAST:G3O-34292-MONOMER.

Miscellaneous databases

NextBioi981635.

Gene expression databases

GenevestigatoriP34167.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A Saccharomyces cerevisiae homologue of mammalian translation initiation factor 4B contributes to RNA helicase activity."
    Altmann M., Mueller P.P., Wittmer B., Ruchti F., Lanker S., Trachsel H.
    EMBO J. 12:3997-4003(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "A new yeast translation initiation factor suppresses a mutation in the eIF-4A RNA helicase."
    Coppolecchia R., Buser P., Stotz A., Linder P.
    EMBO J. 12:4005-4011(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS.
  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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "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-65 AND SER-71, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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-65 AND SER-71, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiIF4B_YEAST
AccessioniPrimary (citable) accession number: P34167
Secondary accession number(s): D6W4G4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: January 7, 2015
This is version 127 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 24000 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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 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.