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Protein

Eukaryotic translation initiation factor 2 subunit beta

Gene

SUI3

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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri236 – 26227C4-typeSequence analysisAdd
BLAST

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • mRNA 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
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-34124-MONOMER.
ReactomeiR-SCE-156827. L13a-mediated translational silencing of Ceruloplasmin 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 beta
Short name:
eIF-2-beta
Gene namesi
Name:SUI3
Synonyms:TIF212
Ordered Locus Names:YPL237W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPL237W.
SGDiS000006158. SUI3.

Subcellular locationi

GO - Cellular componenti

  • eukaryotic 43S preinitiation complex Source: SGD
  • eukaryotic translation initiation factor 2 complex Source: SGD
  • multi-eIF complex Source: SGD
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi16 – 238KKKKKTKK → AAAAATAA: Abolishes interaction with TIF5; when associated with 49-K--K-56 and 82-K--K-89. 1 Publication
Mutagenesisi49 – 568KKKKKKSK → AAAAAASA: Abolishes interaction with TIF5; when associated with 16-K--K-23 and 82-K--K-89. 1 Publication
Mutagenesisi82 – 898KKKKKKTK → AAAAAATA: Abolishes interaction with TIF5; when associated with 16-K--K-23 and 49-K--K-56. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 285285Eukaryotic translation initiation factor 2 subunit betaPRO_0000137415Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei40 – 401PhosphoserineCombined sources
Modified residuei69 – 691PhosphothreonineCombined sources
Modified residuei80 – 801PhosphoserineCombined sources
Modified residuei92 – 921PhosphoserineCombined sources
Modified residuei112 – 1121PhosphoserineCombined sources
Modified residuei116 – 1161PhosphothreonineCombined sources
Modified residuei118 – 1181PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP09064.

PTM databases

iPTMnetiP09064.

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. SUI3 interacts with GCD6 and TIF5/eIF-5.1 Publication

GO - Molecular functioni

  • translation initiation factor binding Source: SGD

Protein-protein interaction databases

BioGridi35925. 56 interactions.
DIPiDIP-2310N.
IntActiP09064. 15 interactions.
MINTiMINT-637374.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J81electron microscopy4.00l1-285[»]
3JAPelectron microscopy4.90l1-285[»]
3JAQelectron microscopy6.00l1-285[»]
ProteinModelPortaliP09064.
SMRiP09064. Positions 131-264.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi16 – 238Lys-rich (basic)
Compositional biasi49 – 568Lys-rich (basic)
Compositional biasi82 – 898Lys-rich (basic)

Sequence similaritiesi

Belongs to the eIF-2-beta/eIF-5 family.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri236 – 26227C4-typeSequence analysisAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

GeneTreeiENSGT00390000001804.
HOGENOMiHOG000107197.
InParanoidiP09064.
KOiK03238.
OMAiTCKSINT.
OrthoDBiEOG092C4JA1.

Family and domain databases

Gene3Di3.30.30.50. 1 hit.
InterProiIPR002735. Transl_init_fac_IF2/IF5.
IPR016189. Transl_init_fac_IF2/IF5_N.
IPR016190. Transl_init_fac_IF2/IF5_Zn-bd.
[Graphical view]
PfamiPF01873. eIF-5_eIF-2B. 1 hit.
[Graphical view]
SMARTiSM00653. eIF2B_5. 1 hit.
[Graphical view]
SUPFAMiSSF100966. SSF100966. 1 hit.
SSF75689. SSF75689. 1 hit.

Sequencei

Sequence statusi: Complete.

P09064-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSDLAAELG FDPALKKKKK TKKVIPDDFD AAVNGKENGS GDDLFAGLKK
60 70 80 90 100
KKKKSKSVSA DAEAEKEPTD DIAEALGELS LKKKKKKTKD SSVDAFEKEL
110 120 130 140 150
AKAGLDNVDA ESKEGTPSAN SSIQQEVGLP YSELLSRFFN ILRTNNPELA
160 170 180 190 200
GDRSGPKFRI PPPVCLRDGK KTIFSNIQDI AEKLHRSPEH LIQYLFAELG
210 220 230 240 250
TSGSVDGQKR LVIKGKFQSK QMENVLRRYI LEYVTCKTCK SINTELKREQ
260 270 280
SNRLFFMVCK SCGSTRSVSS IKTGFQATVG KRRRM
Length:285
Mass (Da):31,574
Last modified:October 1, 1989 - v2
Checksum:i34DE9323876CEE95
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti141 – 1411I → T in AAT92949 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21813 Genomic DNA. Translation: AAA34589.1.
Z67751 Genomic DNA. Translation: CAA91607.1.
Z73594 Genomic DNA. Translation: CAA97959.1.
AY692930 Genomic DNA. Translation: AAT92949.1.
BK006949 Genomic DNA. Translation: DAA11199.1.
PIRiS29368.
RefSeqiNP_015087.1. NM_001184051.1.

Genome annotation databases

EnsemblFungiiYPL237W; YPL237W; YPL237W.
GeneIDi855838.
KEGGisce:YPL237W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21813 Genomic DNA. Translation: AAA34589.1.
Z67751 Genomic DNA. Translation: CAA91607.1.
Z73594 Genomic DNA. Translation: CAA97959.1.
AY692930 Genomic DNA. Translation: AAT92949.1.
BK006949 Genomic DNA. Translation: DAA11199.1.
PIRiS29368.
RefSeqiNP_015087.1. NM_001184051.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J81electron microscopy4.00l1-285[»]
3JAPelectron microscopy4.90l1-285[»]
3JAQelectron microscopy6.00l1-285[»]
ProteinModelPortaliP09064.
SMRiP09064. Positions 131-264.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35925. 56 interactions.
DIPiDIP-2310N.
IntActiP09064. 15 interactions.
MINTiMINT-637374.

PTM databases

iPTMnetiP09064.

Proteomic databases

MaxQBiP09064.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL237W; YPL237W; YPL237W.
GeneIDi855838.
KEGGisce:YPL237W.

Organism-specific databases

EuPathDBiFungiDB:YPL237W.
SGDiS000006158. SUI3.

Phylogenomic databases

GeneTreeiENSGT00390000001804.
HOGENOMiHOG000107197.
InParanoidiP09064.
KOiK03238.
OMAiTCKSINT.
OrthoDBiEOG092C4JA1.

Enzyme and pathway databases

BioCyciYEAST:G3O-34124-MONOMER.
ReactomeiR-SCE-156827. L13a-mediated translational silencing of Ceruloplasmin 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

PROiP09064.

Family and domain databases

Gene3Di3.30.30.50. 1 hit.
InterProiIPR002735. Transl_init_fac_IF2/IF5.
IPR016189. Transl_init_fac_IF2/IF5_N.
IPR016190. Transl_init_fac_IF2/IF5_Zn-bd.
[Graphical view]
PfamiPF01873. eIF-5_eIF-2B. 1 hit.
[Graphical view]
SMARTiSM00653. eIF2B_5. 1 hit.
[Graphical view]
SUPFAMiSSF100966. SSF100966. 1 hit.
SSF75689. SSF75689. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiIF2B_YEAST
AccessioniPrimary (citable) accession number: P09064
Secondary accession number(s): D6W3D3, Q6B200
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: October 1, 1989
Last modified: September 7, 2016
This is version 151 of the entry and version 2 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 XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: 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.