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Protein

Eukaryotic translation initiation factor eIF-1

Gene

SUI1

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

Additional factor that functions in concert with eIF-2 and the initiator tRNA in directing the ribosome to the proper start site of translation.

GO - Molecular functioni

  • ribosomal small subunit binding Source: SGD
  • translation initiation factor activity Source: SGD
  • translation initiation factor binding Source: SGD

GO - Biological processi

  • formation of translation preinitiation complex Source: SGD
  • maintenance of translational fidelity Source: SGD
  • regulation of translation Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Protein biosynthesis, Translation regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-33241-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor eIF-1
Alternative name(s):
Protein translation factor SUI1
Gene namesi
Name:SUI1
Synonyms:RFR1
Ordered Locus Names:YNL244C
ORF Names:N0905
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL244C.
SGDiS000005188. SUI1.

Subcellular locationi

GO - Cellular componenti

  • eukaryotic 43S preinitiation complex Source: SGD
  • multi-eIF complex Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 108107Eukaryotic translation initiation factor eIF-1PRO_0000130566Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP32911.
PeptideAtlasiP32911.

PTM databases

iPTMnetiP32911.

Interactioni

Subunit structurei

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. Interacts with NIP1.1 Publication

GO - Molecular functioni

  • translation initiation factor binding Source: SGD

Protein-protein interaction databases

BioGridi35595. 64 interactions.
DIPiDIP-1471N.
IntActiP32911. 10 interactions.
MINTiMINT-391861.

Structurei

Secondary structure

1
108
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi25 – 317Combined sources
Beta strandi34 – 363Combined sources
Beta strandi39 – 435Combined sources
Helixi51 – 6212Combined sources
Beta strandi66 – 694Combined sources
Beta strandi77 – 837Combined sources
Helixi85 – 9612Combined sources
Beta strandi103 – 1053Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OGHNMR-A1-108[»]
3J80electron microscopy3.75j1-108[»]
3J81electron microscopy4.00m1-108[»]
3JAMelectron microscopy3.46j1-108[»]
3JAPelectron microscopy4.90m1-108[»]
3JAQelectron microscopy6.00m1-108[»]
ProteinModelPortaliP32911.
SMRiP32911. Positions 1-108.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32911.

Family & Domainsi

Sequence similaritiesi

Belongs to the SUI1 family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000015789.
HOGENOMiHOG000279813.
InParanoidiP32911.
KOiK03113.
OMAiVIHIRIQ.
OrthoDBiEOG7HB5NX.

Family and domain databases

Gene3Di3.30.780.10. 1 hit.
InterProiIPR005874. SUI1_euk.
IPR001950. TIF_SUI1.
[Graphical view]
PfamiPF01253. SUI1. 1 hit.
[Graphical view]
PIRSFiPIRSF004499. SUI1_euk. 1 hit.
SUPFAMiSSF55159. SSF55159. 1 hit.
TIGRFAMsiTIGR01160. SUI1_MOF2. 1 hit.
PROSITEiPS50296. SUI1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P32911-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIENLKSFD PFADTGDDET ATSNYIHIRI QQRNGRKTLT TVQGVPEEYD
60 70 80 90 100
LKRILKVLKK DFACNGNIVK DPEMGEIIQL QGDQRAKVCE FMISQLGLQK

KNIKIHGF
Length:108
Mass (Da):12,312
Last modified:October 1, 1993 - v1
Checksum:i03ECB94F3EF3A417
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77514 Genomic DNA. Translation: AAA35131.1.
X96722 Genomic DNA. Translation: CAA65499.1.
Z71520 Genomic DNA. Translation: CAA96150.1.
BK006947 Genomic DNA. Translation: DAA10315.1.
PIRiS31245.
RefSeqiNP_014155.1. NM_001183082.1.

Genome annotation databases

EnsemblFungiiYNL244C; YNL244C; YNL244C.
GeneIDi855477.
KEGGisce:YNL244C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77514 Genomic DNA. Translation: AAA35131.1.
X96722 Genomic DNA. Translation: CAA65499.1.
Z71520 Genomic DNA. Translation: CAA96150.1.
BK006947 Genomic DNA. Translation: DAA10315.1.
PIRiS31245.
RefSeqiNP_014155.1. NM_001183082.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OGHNMR-A1-108[»]
3J80electron microscopy3.75j1-108[»]
3J81electron microscopy4.00m1-108[»]
3JAMelectron microscopy3.46j1-108[»]
3JAPelectron microscopy4.90m1-108[»]
3JAQelectron microscopy6.00m1-108[»]
ProteinModelPortaliP32911.
SMRiP32911. Positions 1-108.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35595. 64 interactions.
DIPiDIP-1471N.
IntActiP32911. 10 interactions.
MINTiMINT-391861.

PTM databases

iPTMnetiP32911.

Proteomic databases

MaxQBiP32911.
PeptideAtlasiP32911.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL244C; YNL244C; YNL244C.
GeneIDi855477.
KEGGisce:YNL244C.

Organism-specific databases

EuPathDBiFungiDB:YNL244C.
SGDiS000005188. SUI1.

Phylogenomic databases

GeneTreeiENSGT00390000015789.
HOGENOMiHOG000279813.
InParanoidiP32911.
KOiK03113.
OMAiVIHIRIQ.
OrthoDBiEOG7HB5NX.

Enzyme and pathway databases

BioCyciYEAST:G3O-33241-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP32911.
PROiP32911.

Family and domain databases

Gene3Di3.30.780.10. 1 hit.
InterProiIPR005874. SUI1_euk.
IPR001950. TIF_SUI1.
[Graphical view]
PfamiPF01253. SUI1. 1 hit.
[Graphical view]
PIRSFiPIRSF004499. SUI1_euk. 1 hit.
SUPFAMiSSF55159. SSF55159. 1 hit.
TIGRFAMsiTIGR01160. SUI1_MOF2. 1 hit.
PROSITEiPS50296. SUI1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The sui1 suppressor locus in Saccharomyces cerevisiae encodes a translation factor that functions during tRNA(iMet) recognition of the start codon."
    Yoon H., Donahue T.F.
    Mol. Cell. Biol. 12:248-260(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "Sequence analysis of the 33 kb long region between ORC5 and SUI1 from the left arm of chromosome XIV from Saccharomyces cerevisiae."
    Sen-Gupta M., Gueldener U., Beinhauer J.D., Fiedler T.A., Hegemann J.H.
    Yeast 13:849-860(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
    Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
    , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
    Nature 387:93-98(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. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSUI1_YEAST
AccessioniPrimary (citable) accession number: P32911
Secondary accession number(s): D6W0U9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: June 8, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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 XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: 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.