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

Translation initiation factor eIF-2B subunit beta

Gene

GCD7

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

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.2 Publications

GO - Molecular functioni

  • enzyme regulator activity Source: SGD
  • translation initiation factor activity Source: SGD

GO - Biological processi

  • positive regulation of GTPase activity Source: GOC
  • regulation of catalytic activity Source: GOC
  • regulation of translational initiation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis, Translation regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-32386-MONOMER.
ReactomeiR-SCE-72731. Recycling of eIF2:GDP.

Names & Taxonomyi

Protein namesi
Recommended name:
Translation initiation factor eIF-2B subunit beta
Alternative name(s):
GCD complex subunit GCD7
Guanine nucleotide exchange factor subunit GCD7
eIF-2B GDP-GTP exchange factor subunit beta
Gene namesi
Name:GCD7
Synonyms:TIF222
Ordered Locus Names:YLR291C
ORF Names:L8003.17
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR291C.
SGDiS000004282. GCD7.

Subcellular locationi

GO - Cellular componenti

  • eukaryotic translation initiation factor 2B complex Source: SGD
  • guanyl-nucleotide exchange factor complex Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 381381Translation initiation factor eIF-2B subunit betaPRO_0000156066Add
BLAST

Proteomic databases

MaxQBiP32502.
PeptideAtlasiP32502.

Interactioni

Subunit structurei

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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GCD2P127545EBI-6260,EBI-6265
GCN3P147417EBI-6260,EBI-6253
MUK1Q028663EBI-6260,EBI-32646

Protein-protein interaction databases

BioGridi31557. 122 interactions.
DIPiDIP-1185N.
IntActiP32502. 122 interactions.
MINTiMINT-401217.

Structurei

3D structure databases

ProteinModelPortaliP32502.
SMRiP32502. Positions 28-361.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00550000074908.
HOGENOMiHOG000208487.
InParanoidiP32502.
KOiK03754.
OMAiKGAREHI.
OrthoDBiEOG70KH0H.

Family and domain databases

InterProiIPR000649. IF-2B-related.
[Graphical view]
PfamiPF01008. IF-2B. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32502-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSQAFTSVH PNAATSDVNV TIDTFVAKLK RRQVQGSYAI ALETLQLLMR
60 70 80 90 100
FISAARWNHV NDLIEQIRDL GNSLEKAHPT AFSCGNVIRR ILAVLRDEVE
110 120 130 140 150
EDTMSTTVTS TSVAEPLISS MFNLLQKPEQ PHQNRKNSSG SSSMKTKTDY
160 170 180 190 200
RQVAIQGIKD LIDEIKNIDE GIQQIAIDLI HDHEILLTPT PDSKTVLKFL
210 220 230 240 250
ITARERSNRT FTVLVTEGFP NNTKNAHEFA KKLAQHNIET LVVPDSAVFA
260 270 280 290 300
LMSRVGKVII GTKAVFVNGG TISSNSGVSS VCECAREFRT PVFAVAGLYK
310 320 330 340 350
LSPLYPFDVE KFVEFGGSQR ILPRMDPRKR LDTVNQITDY VPPENIDIYI
360 370 380
TNVGGFNPSF IYRIAWDNYK QIDVHLDKNK A
Length:381
Mass (Da):42,570
Last modified:October 1, 1993 - v1
Checksum:iA5409FAF1594854C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07116 Genomic DNA. Translation: AAA34634.1.
U17243 Genomic DNA. Translation: AAB67337.1.
BK006945 Genomic DNA. Translation: DAA09603.1.
PIRiB48156.
RefSeqiNP_013394.1. NM_001182179.1.

Genome annotation databases

EnsemblFungiiYLR291C; YLR291C; YLR291C.
GeneIDi850998.
KEGGisce:YLR291C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07116 Genomic DNA. Translation: AAA34634.1.
U17243 Genomic DNA. Translation: AAB67337.1.
BK006945 Genomic DNA. Translation: DAA09603.1.
PIRiB48156.
RefSeqiNP_013394.1. NM_001182179.1.

3D structure databases

ProteinModelPortaliP32502.
SMRiP32502. Positions 28-361.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31557. 122 interactions.
DIPiDIP-1185N.
IntActiP32502. 122 interactions.
MINTiMINT-401217.

Proteomic databases

MaxQBiP32502.
PeptideAtlasiP32502.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR291C; YLR291C; YLR291C.
GeneIDi850998.
KEGGisce:YLR291C.

Organism-specific databases

EuPathDBiFungiDB:YLR291C.
SGDiS000004282. GCD7.

Phylogenomic databases

GeneTreeiENSGT00550000074908.
HOGENOMiHOG000208487.
InParanoidiP32502.
KOiK03754.
OMAiKGAREHI.
OrthoDBiEOG70KH0H.

Enzyme and pathway databases

BioCyciYEAST:G3O-32386-MONOMER.
ReactomeiR-SCE-72731. Recycling of eIF2:GDP.

Miscellaneous databases

PROiP32502.

Family and domain databases

InterProiIPR000649. IF-2B-related.
[Graphical view]
PfamiPF01008. IF-2B. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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.
    , 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] [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. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE EIF2-B COMPLEX, FUNCTION OF THE EIF2-B COMPLEX.
  5. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A EIF2-B SUBCOMPLEX.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiEI2BB_YEAST
AccessioniPrimary (citable) accession number: P32502
Secondary accession number(s): D6VYT7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: June 8, 2016
This is version 131 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 6650 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: 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.