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Protein

Eukaryotic translation initiation factor 1A

Gene

TIF11

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Seems to be required for maximal rate of protein biosynthesis. Enhances ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal subunits.

GO - Molecular functioni

  • double-stranded RNA binding Source: SGD
  • ribosomal small subunit binding Source: SGD
  • translation initiation factor activity Source: SGD
  • translation initiation factor binding Source: SGD

GO - Biological processi

  • formation of cytoplasmic translation initiation complex Source: SGD
  • formation of translation preinitiation complex Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

BioCyciYEAST:G3O-32935-MONOMER.
ReactomeiR-SCE-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-SCE-72689. Formation of a pool of free 40S subunits.
R-SCE-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-SCE-72702. Ribosomal scanning and start codon recognition.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 1A
Short name:
eIF-1A
Alternative name(s):
Eukaryotic translation initiation factor 4C
Short name:
eIF-4C
Gene namesi
Name:TIF11
Ordered Locus Names:YMR260C
ORF Names:YM8156.02C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YMR260C.
SGDiS000004873. TIF11.

Subcellular locationi

GO - Cellular componenti

  • eukaryotic 43S preinitiation complex Source: SGD
  • eukaryotic 48S preinitiation complex Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 153153Eukaryotic translation initiation factor 1APRO_0000145113Add
BLAST

Proteomic databases

MaxQBiP38912.

PTM databases

iPTMnetiP38912.

Interactioni

GO - Molecular functioni

  • translation initiation factor binding Source: SGD

Protein-protein interaction databases

BioGridi35438. 28 interactions.
DIPiDIP-4401N.
IntActiP38912. 3 interactions.
MINTiMINT-562037.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J80electron microscopy3.75i1-153[»]
3J81electron microscopy4.00i1-153[»]
3JAMelectron microscopy3.46i1-153[»]
3JAPelectron microscopy4.90i1-153[»]
3JAQelectron microscopy6.00i1-153[»]
3WBKX-ray3.30C27-153[»]
ProteinModelPortaliP38912.
SMRiP38912. Positions 5-115.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 9675S1-likeAdd
BLAST

Sequence similaritiesi

Belongs to the eIF-1A family.Curated
Contains 1 S1-like domain.Curated

Phylogenomic databases

GeneTreeiENSGT00390000008256.
HOGENOMiHOG000223675.
InParanoidiP38912.
KOiK03236.
OMAiNETAVDM.
OrthoDBiEOG092C5KXX.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
HAMAPiMF_00216. aIF_1A. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR006196. RNA-binding_domain_S1_IF1.
IPR001253. TIF_eIF-1A.
IPR018104. TIF_eIF-1A_CS.
[Graphical view]
PANTHERiPTHR21668. PTHR21668. 1 hit.
PfamiPF01176. eIF-1a. 1 hit.
[Graphical view]
ProDomiPD005579. TIF_eIF-1A. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00652. eIF1a. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00523. eIF-1A. 1 hit.
PROSITEiPS01262. IF1A. 1 hit.
PS50832. S1_IF1_TYPE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P38912-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKKNTKGGK KGRRGKNDSD GPKRELIYKE EGQEYAQITK MLGNGRVEAS
60 70 80 90 100
CFDGNKRMAH IRGKLRKKVW MGQGDIILVS LRDFQDDQCD VVHKYNLDEA
110 120 130 140 150
RTLKNQGELP ENAKINETDN FGFESDEDVN FEFGNADEDD EEGEDEELDI

DDI
Length:153
Mass (Da):17,435
Last modified:February 1, 1995 - v1
Checksum:iAEF000104BBA3041
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U11585 Genomic DNA. Translation: AAA82039.1.
Z49260 Genomic DNA. Translation: CAA89243.1.
AY557964 Genomic DNA. Translation: AAS56290.1.
BK006946 Genomic DNA. Translation: DAA10160.1.
PIRiS47943.
RefSeqiNP_013987.1. NM_001182767.1.

Genome annotation databases

EnsemblFungiiYMR260C; YMR260C; YMR260C.
GeneIDi855302.
KEGGisce:YMR260C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U11585 Genomic DNA. Translation: AAA82039.1.
Z49260 Genomic DNA. Translation: CAA89243.1.
AY557964 Genomic DNA. Translation: AAS56290.1.
BK006946 Genomic DNA. Translation: DAA10160.1.
PIRiS47943.
RefSeqiNP_013987.1. NM_001182767.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J80electron microscopy3.75i1-153[»]
3J81electron microscopy4.00i1-153[»]
3JAMelectron microscopy3.46i1-153[»]
3JAPelectron microscopy4.90i1-153[»]
3JAQelectron microscopy6.00i1-153[»]
3WBKX-ray3.30C27-153[»]
ProteinModelPortaliP38912.
SMRiP38912. Positions 5-115.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35438. 28 interactions.
DIPiDIP-4401N.
IntActiP38912. 3 interactions.
MINTiMINT-562037.

PTM databases

iPTMnetiP38912.

Proteomic databases

MaxQBiP38912.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYMR260C; YMR260C; YMR260C.
GeneIDi855302.
KEGGisce:YMR260C.

Organism-specific databases

EuPathDBiFungiDB:YMR260C.
SGDiS000004873. TIF11.

Phylogenomic databases

GeneTreeiENSGT00390000008256.
HOGENOMiHOG000223675.
InParanoidiP38912.
KOiK03236.
OMAiNETAVDM.
OrthoDBiEOG092C5KXX.

Enzyme and pathway databases

BioCyciYEAST:G3O-32935-MONOMER.
ReactomeiR-SCE-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-SCE-72689. Formation of a pool of free 40S subunits.
R-SCE-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-SCE-72702. Ribosomal scanning and start codon recognition.

Miscellaneous databases

PROiP38912.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
HAMAPiMF_00216. aIF_1A. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR006196. RNA-binding_domain_S1_IF1.
IPR001253. TIF_eIF-1A.
IPR018104. TIF_eIF-1A_CS.
[Graphical view]
PANTHERiPTHR21668. PTHR21668. 1 hit.
PfamiPF01176. eIF-1a. 1 hit.
[Graphical view]
ProDomiPD005579. TIF_eIF-1A. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00652. eIF1a. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00523. eIF-1A. 1 hit.
PROSITEiPS01262. IF1A. 1 hit.
PS50832. S1_IF1_TYPE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiIF1A_YEAST
AccessioniPrimary (citable) accession number: P38912
Secondary accession number(s): D6W086
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: September 7, 2016
This is version 133 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 35100 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, 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 XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: 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.