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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: -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.

Miscellaneous

Present with 17100 molecules/cell in log phase SD medium.1 Publication

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

Keywordsi

Molecular functionInitiation factor, RNA-binding
Biological processProtein biosynthesis

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi52S → A: Strongly impairs derepression of GCN4 expression in amino acid-starved cells. 1 Publication1
Mutagenesisi52S → D: Weakly impairs derepression of GCN4 expression in amino acid-starved cells. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001373891 – 304Eukaryotic translation initiation factor 2 subunit alphaAdd BLAST304

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei52Phosphoserine; by GCN21 Publication1
Modified residuei292PhosphoserineCombined sources1
Modified residuei294PhosphoserineCombined sources1

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
PaxDbiP20459
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.

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi33763, 289 interactors
DIPiDIP-2327N
IntActiP20459, 42 interactors
MINTiP20459
STRINGi4932.YJR007W

Structurei

Secondary structure

1304
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 13Combined sources6
Beta strandi19 – 28Combined sources10
Beta strandi31 – 36Combined sources6
Turni37 – 41Combined sources5
Beta strandi43 – 47Combined sources5
Helixi48 – 50Combined sources3
Helixi59 – 61Combined sources3
Beta strandi67 – 77Combined sources11
Turni78 – 81Combined sources4
Beta strandi82 – 87Combined sources6
Helixi92 – 118Combined sources27
Helixi123 – 129Combined sources7
Helixi131 – 138Combined sources8
Helixi141 – 150Combined sources10
Helixi152 – 155Combined sources4
Helixi163 – 173Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20459

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini17 – 88S1 motifPROSITE-ProRule annotationAdd BLAST72

Sequence similaritiesi

Belongs to the eIF-2-alpha family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000007015
HOGENOMiHOG000199476
InParanoidiP20459
KOiK03237
OMAiKDVNEHQ
OrthoDBiEOG092C3ENF

Family and domain databases

Gene3Di1.10.150.190, 1 hit
3.30.70.1130, 1 hit
InterProiView protein in InterPro
IPR012340 NA-bd_OB-fold
IPR022967 S1_dom
IPR003029 S1_domain
IPR024055 TIF2_asu_C
IPR024054 TIF2_asu_middle_sf
IPR011488 TIF_2_asu
PANTHERiPTHR10602 PTHR10602, 1 hit
PfamiView protein in Pfam
PF07541 EIF_2_alpha, 1 hit
PF00575 S1, 1 hit
SMARTiView protein in SMART
SM00316 S1, 1 hit
SUPFAMiSSF110993 SSF110993, 1 hit
SSF116742 SSF116742, 1 hit
SSF50249 SSF50249, 1 hit
PROSITEiView protein in PROSITE
PS50126 S1, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti258Y → H in AAS56202 (PubMed:17322287).Curated1

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

Similar proteinsi

Entry informationi

Entry nameiIF2A_YEAST
AccessioniPrimary (citable) accession number: P20459
Secondary accession number(s): D6VWI2, E9P8T6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: March 28, 2018
This is version 173 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health