Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Eukaryotic translation initiation factor 2 subunit gamma

Gene

GCD11

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
Nucleotide bindingi107 – 1148GTPBy similarity
Nucleotide bindingi193 – 1975GTPBy similarity
Nucleotide bindingi249 – 2524GTPBy similarity

GO - Molecular functioni

  • GTPase activity Source: GO_Central
  • GTP binding Source: UniProtKB-KW
  • translation initiation factor activity Source: SGD
  • translation initiation factor binding Source: SGD

GO - Biological processi

  • formation of translation preinitiation complex Source: SGD
  • positive regulation of translational fidelity Source: SGD
  • translational initiation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30207-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 gamma
Short name:
eIF-2-gamma
Gene namesi
Name:GCD11
Synonyms:TIF213
Ordered Locus Names:YER025W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome V

Organism-specific databases

EuPathDBiFungiDB:YER025W.
SGDiS000000827. GCD11.

Subcellular locationi

GO - Cellular componenti

  • eukaryotic 43S preinitiation complex Source: SGD
  • eukaryotic 48S preinitiation complex Source: SGD
  • eukaryotic translation initiation factor 2 complex Source: SGD
  • multi-eIF complex Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 527527Eukaryotic translation initiation factor 2 subunit gammaPRO_0000137448Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei60 – 601PhosphothreonineCombined sources
Modified residuei258 – 2581PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP32481.
PRIDEiP32481.

PTM databases

iPTMnetiP32481.

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.

GO - Molecular functioni

  • translation initiation factor binding Source: SGD

Protein-protein interaction databases

BioGridi36759. 147 interactions.
DIPiDIP-2561N.
IntActiP32481. 60 interactions.
MINTiMINT-423090.

Structurei

Secondary structure

1
527
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi425 – 43612Combined sources
Beta strandi460 – 4667Combined sources
Beta strandi469 – 47810Combined sources
Beta strandi480 – 49314Combined sources
Beta strandi498 – 5047Combined sources
Beta strandi506 – 52318Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J81electron microscopy4.00k1-527[»]
3JAPelectron microscopy4.90k1-527[»]
3JAQelectron microscopy6.00k1-527[»]
4ZGNX-ray2.90B410-527[»]
4ZGQX-ray3.00B410-527[»]
ProteinModelPortaliP32481.
SMRiP32481. Positions 69-525.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini98 – 307210tr-type GPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni107 – 1148G1PROSITE-ProRule annotation
Regioni135 – 1395G2PROSITE-ProRule annotation
Regioni193 – 1964G3PROSITE-ProRule annotation
Regioni249 – 2524G4PROSITE-ProRule annotation
Regioni284 – 2863G5PROSITE-ProRule annotation

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi155 – 17925Cys-richAdd
BLAST

Sequence similaritiesi

Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EIF2G subfamily.PROSITE-ProRule annotation
Contains 1 tr-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00550000074801.
HOGENOMiHOG000229292.
InParanoidiP32481.
KOiK03242.
OMAiRCTNESC.
OrthoDBiEOG7W15CW.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR004161. EFTu-like_2.
IPR027417. P-loop_NTPase.
IPR000795. TF_GTP-bd_dom.
IPR015256. TIF2_gsu_C.
IPR009000. Transl_B-barrel.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
[Graphical view]
PfamiPF09173. eIF2_C. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEiPS51722. G_TR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32481-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDLQDQEPS IIINGNLEPV GEPDIVEETE VVAQETQETQ DADKPKKKVA
60 70 80 90 100
FTGLEEDGET EEEKRKREFE EGGGLPEQPL NPDFSKLNPL SAEIINRQAT
110 120 130 140 150
INIGTIGHVA HGKSTVVRAI SGVQTVRFKD ELERNITIKL GYANAKIYKC
160 170 180 190 200
QEPTCPEPDC YRSFKSDKEI SPKCQRPGCP GRYKLVRHVS FVDCPGHDIL
210 220 230 240 250
MSTMLSGAAV MDAALLLIAG NESCPQPQTS EHLAAIEIMK LKHVIILQNK
260 270 280 290 300
VDLMREESAL EHQKSILKFI RGTIADGAPI VPISAQLKYN IDAVNEFIVK
310 320 330 340 350
TIPVPPRDFM ISPRLIVIRS FDVNKPGAEI EDLKGGVAGG SILNGVFKLG
360 370 380 390 400
DEIEIRPGIV TKDDKGKIQC KPIFSNIVSL FAEQNDLKFA VPGGLIGVGT
410 420 430 440 450
KVDPTLCRAD RLVGQVVGAK GHLPNIYTDI EINYFLLRRL LGVKTDGQKQ
460 470 480 490 500
AKVRKLEPNE VLMVNIGSTA TGARVVAVKA DMARLQLTSP ACTEINEKIA
510 520
LSRRIEKHWR LIGWATIKKG TTLEPIA
Length:527
Mass (Da):57,866
Last modified:October 1, 1993 - v1
Checksum:iD498AE62BC3E81CD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04268 Genomic DNA. Translation: AAA34633.1.
U18778 Genomic DNA. Translation: AAB64558.1.
BK006939 Genomic DNA. Translation: DAA07678.1.
PIRiA48117.
RefSeqiNP_010942.1. NM_001178916.1.

Genome annotation databases

EnsemblFungiiYER025W; YER025W; YER025W.
GeneIDi856746.
KEGGisce:YER025W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04268 Genomic DNA. Translation: AAA34633.1.
U18778 Genomic DNA. Translation: AAB64558.1.
BK006939 Genomic DNA. Translation: DAA07678.1.
PIRiA48117.
RefSeqiNP_010942.1. NM_001178916.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J81electron microscopy4.00k1-527[»]
3JAPelectron microscopy4.90k1-527[»]
3JAQelectron microscopy6.00k1-527[»]
4ZGNX-ray2.90B410-527[»]
4ZGQX-ray3.00B410-527[»]
ProteinModelPortaliP32481.
SMRiP32481. Positions 69-525.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36759. 147 interactions.
DIPiDIP-2561N.
IntActiP32481. 60 interactions.
MINTiMINT-423090.

PTM databases

iPTMnetiP32481.

Proteomic databases

MaxQBiP32481.
PRIDEiP32481.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYER025W; YER025W; YER025W.
GeneIDi856746.
KEGGisce:YER025W.

Organism-specific databases

EuPathDBiFungiDB:YER025W.
SGDiS000000827. GCD11.

Phylogenomic databases

GeneTreeiENSGT00550000074801.
HOGENOMiHOG000229292.
InParanoidiP32481.
KOiK03242.
OMAiRCTNESC.
OrthoDBiEOG7W15CW.

Enzyme and pathway databases

BioCyciYEAST:G3O-30207-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

PROiP32481.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR004161. EFTu-like_2.
IPR027417. P-loop_NTPase.
IPR000795. TF_GTP-bd_dom.
IPR015256. TIF2_gsu_C.
IPR009000. Transl_B-barrel.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
[Graphical view]
PfamiPF09173. eIF2_C. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEiPS51722. G_TR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "GCD11, a negative regulator of GCN4 expression, encodes the gamma subunit of eIF-2 in Saccharomyces cerevisiae."
    Hannig E.M., Cigan A.M., Freeman B.A., Kinzy T.G.
    Mol. Cell. Biol. 13:506-520(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  5. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-60 AND SER-258, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiIF2G_YEAST
AccessioniPrimary (citable) accession number: P32481
Secondary accession number(s): D3DLS4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: July 6, 2016
This is version 153 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 20800 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 V
    Yeast (Saccharomyces cerevisiae) chromosome V: 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.