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Reviewed, UniProtKB/Swiss-Prot P32502 (EI2BB_YEAST)

Last modified June 16, 2009. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Translation initiation factor eIF-2B subunit beta
Alternative name(s):
    eIF-2B GDP-GTP exchange factor subunit beta
    Guanine nucleotide exchange factor subunit GCD7
    GCD complex subunit GCD7
Gene names
Name: GCD7
Synonyms: TIF222
Ordered Locus Names: YLR291C
ORF Names: L8003.17
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length381 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Acts as a regulatory component of the translation initiation factor 2B (eIF2-B or GCD complex), which catalyzes the exchange of eukaryotic initiation factor 2 (eIF-2)-bound GDP for GTP and is regulated by phosphorylated eIF-2. It activates the synthesis of GCN4 in yeast under amino acid starvation conditions by suppressing the inhibitory effects of multiple AUG codons present in the leader of GCN4 mRNA. It may promote either repression or activation of GCN4 expression depending on amino acid availability. GCD6 and GCD7 repress GCN4 expression at the translational level by ensuring that ribosomes which have translated UORF1 will reinitiate at UORF2, -3, or -4 and thus fail to reach the GCN4 start site. Ref.3 Ref.4

Subunit structure

Translation initiation factor 2B (eIF2-B) is composed of five different subunits; alpha (GCN3), beta (GCD7), gamma (GCD1), delta (GCD2) and epsilon (GCD6). A regulatory subcomplex comprising GCN3, GCD7 and GCD2 interacts preferentially with phosphorylated eIF-2 and has no exchange activity in vitro.

Miscellaneous

Present with 6650 molecules/cell in log phase SD medium. Ref.5

Sequence similarities

Belongs to the EIF-2B alpha/beta/delta subunits family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 381381Translation initiation factor eIF-2B subunit beta
PRO_0000156066

Sequences

Sequence LengthMass (Da)Tools
P32502-1 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: A5409FAF1594854C

FASTA38142,570
        10         20         30         40         50         60 
MSSQAFTSVH PNAATSDVNV TIDTFVAKLK RRQVQGSYAI ALETLQLLMR FISAARWNHV 

        70         80         90        100        110        120 
NDLIEQIRDL GNSLEKAHPT AFSCGNVIRR ILAVLRDEVE EDTMSTTVTS TSVAEPLISS 

       130        140        150        160        170        180 
MFNLLQKPEQ PHQNRKNSSG SSSMKTKTDY RQVAIQGIKD LIDEIKNIDE GIQQIAIDLI 

       190        200        210        220        230        240 
HDHEILLTPT PDSKTVLKFL ITARERSNRT FTVLVTEGFP NNTKNAHEFA KKLAQHNIET 

       250        260        270        280        290        300 
LVVPDSAVFA LMSRVGKVII GTKAVFVNGG TISSNSGVSS VCECAREFRT PVFAVAGLYK 

       310        320        330        340        350        360 
LSPLYPFDVE KFVEFGGSQR ILPRMDPRKR LDTVNQITDY VPPENIDIYI TNVGGFNPSF 

       370        380 
IYRIAWDNYK QIDVHLDKNK A 

« Hide

References

« Hide 'large scale' references
[1]"Evidence that GCD6 and GCD7, translational regulators of GCN4, are subunits of the guanine nucleotide exchange factor for eIF-2 in Saccharomyces cerevisiae."
Bushman J.L., Asuru A.I., Matts R.L., Hinnebusch A.G.
Mol. Cell. Biol. 13:1920-1932(1993) [PubMed: 8441423] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. expand/collapse author list , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
Nature 387:87-90(1997) [PubMed: 9169871] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[3]"A protein complex of translational regulators of GCN4 mRNA is the guanine nucleotide-exchange factor for translation initiation factor 2 in yeast."
Cigan A.M., Bushman J.L., Boal T.R., Hinnebusch A.G.
Proc. Natl. Acad. Sci. U.S.A. 90:5350-5354(1993) [PubMed: 8506384] [Abstract]
Cited for: IDENTIFICATION IN THE EIF2-B COMPLEX, FUNCTION OF THE EIF2-B COMPLEX.
[4]"eIF2 independently binds two distinct eIF2B subcomplexes that catalyze and regulate guanine-nucleotide exchange."
Pavitt G.D., Ramaiah K.V., Kimball S.R., Hinnebusch A.G.
Genes Dev. 12:514-526(1998) [PubMed: 9472020] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN A EIF2-B SUBCOMPLEX.
[5]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

L07116 Genomic DNA. Translation: AAA34634.1.
U17243 Genomic DNA. Translation: AAB67337.1.
PIRB48156.
RefSeqNP_013394.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP:1185N.
IntActP32502. 70 interactions.

Proteomic databases

PeptideAtlasP32502.

Genome annotation databases

EnsemblYLR291C. Saccharomyces cerevisiae. [Contig view]
GeneID850998.
GenomeReviewsGene locus YLR291C in contig Y13138_GR.
KEGGsce:YLR291C.
NMPDRfig|4932.3.peg.4411.

Organism-specific databases

CYGDYLR291c.
SGDS000004282. GCD7.
Yeast-GFPSearch...

Phylogenomic databases

HOGENOMP32502.
OMAP32502. IITDHRW.

Gene expression databases

GermOnlineYLR291C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR000649. IF-2B_related.
[Graphical view]
PANTHERPTHR10233. IF-2B_related. 1 hit.
PfamPF01008. IF-2B. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio967537.

Entry information

Entry nameEI2BB_YEAST
AccessionPrimary (citable) accession number: P32502
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: June 16, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents