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Protein

Eukaryotic translation initiation factor 2 subunit alpha

Gene

SUI2

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

eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S preinitiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B.

GO - Molecular functioni

  • ribosome binding Source: GO_Central
  • translation initiation factor activity Source: SGD

GO - Biological processi

  • formation of translation preinitiation complex Source: SGD
  • 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-31653-MONOMER.
ReactomeiR-SCE-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-SCE-381042. PERK regulates gene expression.
R-SCE-382556. ABC-family proteins mediated transport.
R-SCE-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-SCE-72702. Ribosomal scanning and start codon recognition.
R-SCE-72731. Recycling of eIF2:GDP.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 2 subunit alpha
Short name:
eIF-2-alpha
Gene namesi
Name:SUI2
Synonyms:TIF211
Ordered Locus Names:YJR007W
ORF Names:J1429
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJR007W.
SGDiS000003767. SUI2.

Subcellular locationi

GO - Cellular componenti

  • eukaryotic 48S preinitiation complex Source: SGD
  • eukaryotic translation initiation factor 2B complex Source: GO_Central
  • eukaryotic translation initiation factor 2 complex Source: SGD
  • multi-eIF complex Source: SGD
  • ribosome Source: SGD
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi52 – 521S → A: Strongly impairs derepression of GCN4 expression in amino acid-starved cells. 1 Publication
Mutagenesisi52 – 521S → D: Weakly impairs derepression of GCN4 expression in amino acid-starved cells. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 304304Eukaryotic translation initiation factor 2 subunit alphaPRO_0000137389Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei52 – 521Phosphoserine; by GCN21 Publication
Modified residuei292 – 2921PhosphoserineCombined sources
Modified residuei294 – 2941PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated; phosphorylation on Ser-52 by the GCN2 protein kinase occurs in response to amino acid starvation (PubMed:1739968).1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP20459.
PRIDEiP20459.

PTM databases

iPTMnetiP20459.

Interactioni

Subunit structurei

Eukaryotic translation initiation factor 2 (eIF-2) is a heterotrimer composed of an alpha, a beta and a gamma subunit. 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.

Protein-protein interaction databases

BioGridi33763. 99 interactions.
DIPiDIP-2327N.
IntActiP20459. 16 interactions.
MINTiMINT-519024.

Structurei

Secondary structure

1
304
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 136Combined sources
Beta strandi19 – 2810Combined sources
Beta strandi31 – 366Combined sources
Turni37 – 415Combined sources
Beta strandi43 – 475Combined sources
Helixi48 – 503Combined sources
Helixi59 – 613Combined sources
Beta strandi67 – 7711Combined sources
Turni78 – 814Combined sources
Beta strandi82 – 876Combined sources
Helixi92 – 11827Combined sources
Helixi123 – 1297Combined sources
Helixi131 – 1388Combined sources
Helixi141 – 15010Combined sources
Helixi152 – 1554Combined sources
Helixi163 – 17311Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q46X-ray2.86A2-176[»]
2A19X-ray2.50A4-176[»]
2A1AX-ray2.80A4-176[»]
3J81electron microscopy4.00j1-300[»]
3JAPelectron microscopy4.90j1-304[»]
3JAQelectron microscopy6.00j1-304[»]
ProteinModelPortaliP20459.
SMRiP20459. Positions 3-265.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20459.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 8872S1 motifPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the eIF-2-alpha family.Curated
Contains 1 S1 motif domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00390000007015.
HOGENOMiHOG000199476.
InParanoidiP20459.
KOiK03237.
OMAiKDVNEHQ.
OrthoDBiEOG7BW0VK.

Family and domain databases

Gene3Di1.10.150.190. 1 hit.
2.40.50.140. 1 hit.
3.30.70.1130. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR022967. S1_dom.
IPR003029. S1_domain.
IPR024055. TIF2_asu_C.
IPR024054. TIF2_asu_middle.
IPR011488. TIF_2_asu.
[Graphical view]
PfamiPF07541. EIF_2_alpha. 1 hit.
PF00575. S1. 1 hit.
[Graphical view]
SMARTiSM00316. S1. 1 hit.
[Graphical view]
SUPFAMiSSF110993. SSF110993. 1 hit.
SSF116742. SSF116742. 1 hit.
SSF50249. SSF50249. 1 hit.
PROSITEiPS50126. S1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P20459-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTSHCRFYE NKYPEIDDIV MVNVQQIAEM GAYVKLLEYD NIEGMILLSE
60 70 80 90 100
LSRRRIRSIQ KLIRVGKNDV AVVLRVDKEK GYIDLSKRRV SSEDIIKCEE
110 120 130 140 150
KYQKSKTVHS ILRYCAEKFQ IPLEELYKTI AWPLSRKFGH AYEAFKLSII
160 170 180 190 200
DETVWEGIEP PSKDVLDELK NYISKRLTPQ AVKIRADVEV SCFSYEGIDA
210 220 230 240 250
IKDALKSAED MSTEQMQVKV KLVAAPLYVL TTQALDKQKG IEQLESAIEK
260 270 280 290 300
ITEVITKYGG VCNITMPPKA VTATEDAELQ ALLESKELDN RSDSEDDEDE

SDDE
Length:304
Mass (Da):34,718
Last modified:February 1, 1991 - v1
Checksum:iAF4F1C80303A4E98
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti258 – 2581Y → H in AAS56202 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25552 Genomic DNA. Translation: AAA70332.1.
X87611 Genomic DNA. Translation: CAA60929.1.
Z49507 Genomic DNA. Translation: CAA89529.1.
AY557876 Genomic DNA. Translation: AAS56202.1.
BK006943 Genomic DNA. Translation: DAA08798.1.
PIRiA32108.
RefSeqiNP_012540.3. NM_001181664.3.

Genome annotation databases

EnsemblFungiiYJR007W; YJR007W; YJR007W.
GeneIDi853463.
KEGGisce:YJR007W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25552 Genomic DNA. Translation: AAA70332.1.
X87611 Genomic DNA. Translation: CAA60929.1.
Z49507 Genomic DNA. Translation: CAA89529.1.
AY557876 Genomic DNA. Translation: AAS56202.1.
BK006943 Genomic DNA. Translation: DAA08798.1.
PIRiA32108.
RefSeqiNP_012540.3. NM_001181664.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q46X-ray2.86A2-176[»]
2A19X-ray2.50A4-176[»]
2A1AX-ray2.80A4-176[»]
3J81electron microscopy4.00j1-300[»]
3JAPelectron microscopy4.90j1-304[»]
3JAQelectron microscopy6.00j1-304[»]
ProteinModelPortaliP20459.
SMRiP20459. Positions 3-265.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33763. 99 interactions.
DIPiDIP-2327N.
IntActiP20459. 16 interactions.
MINTiMINT-519024.

PTM databases

iPTMnetiP20459.

Proteomic databases

MaxQBiP20459.
PRIDEiP20459.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJR007W; YJR007W; YJR007W.
GeneIDi853463.
KEGGisce:YJR007W.

Organism-specific databases

EuPathDBiFungiDB:YJR007W.
SGDiS000003767. SUI2.

Phylogenomic databases

GeneTreeiENSGT00390000007015.
HOGENOMiHOG000199476.
InParanoidiP20459.
KOiK03237.
OMAiKDVNEHQ.
OrthoDBiEOG7BW0VK.

Enzyme and pathway databases

BioCyciYEAST:G3O-31653-MONOMER.
ReactomeiR-SCE-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-SCE-381042. PERK regulates gene expression.
R-SCE-382556. ABC-family proteins mediated transport.
R-SCE-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-SCE-72702. Ribosomal scanning and start codon recognition.
R-SCE-72731. Recycling of eIF2:GDP.

Miscellaneous databases

EvolutionaryTraceiP20459.
PROiP20459.

Family and domain databases

Gene3Di1.10.150.190. 1 hit.
2.40.50.140. 1 hit.
3.30.70.1130. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR022967. S1_dom.
IPR003029. S1_domain.
IPR024055. TIF2_asu_C.
IPR024054. TIF2_asu_middle.
IPR011488. TIF_2_asu.
[Graphical view]
PfamiPF07541. EIF_2_alpha. 1 hit.
PF00575. S1. 1 hit.
[Graphical view]
SMARTiSM00316. S1. 1 hit.
[Graphical view]
SUPFAMiSSF110993. SSF110993. 1 hit.
SSF116742. SSF116742. 1 hit.
SSF50249. SSF50249. 1 hit.
PROSITEiPS50126. S1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Yeast translation initiation suppressor sui2 encodes the alpha subunit of eukaryotic initiation factor 2 and shares sequence identity with the human alpha subunit."
    Cigan A.M., Pabich E.K., Feng L., Donahue T.F.
    Proc. Natl. Acad. Sci. U.S.A. 86:2784-2788(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
    Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K.
    , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
    EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "Phosphorylation of initiation factor 2 alpha by protein kinase GCN2 mediates gene-specific translational control of GCN4 in yeast."
    Dever T.E., Feng L., Wek R.C., Cigan A.M., Donahue T.F., Hinnebusch A.G.
    Cell 68:585-596(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-52 BY GCN2, MUTAGENESIS OF SER-52.
  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-292 AND SER-294, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "The crystal structure of the N-terminal region of the alpha subunit of translation initiation factor 2 (eIF2alpha) from Saccharomyces cerevisiae provides a view of the loop containing serine 51, the target of the eIF2alpha-specific kinases."
    Dhaliwal S., Hoffman D.W.
    J. Mol. Biol. 334:187-195(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.86 ANGSTROMS) OF 2-176.
  9. "Higher-order substrate recognition of eIF2alpha by the RNA-dependent protein kinase PKR."
    Dar A.C., Dever T.E., Sicheri F.
    Cell 122:887-900(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 4-176.

Entry informationi

Entry nameiIF2A_YEAST
AccessioniPrimary (citable) accession number: P20459
Secondary accession number(s): D6VWI2, E9P8T6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: July 6, 2016
This is version 158 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 17100 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 X
    Yeast (Saccharomyces cerevisiae) chromosome X: 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.