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Protein

Translation initiation factor eIF-2B subunit delta

Gene

GCD2

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 essential 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. GCD2 is also required for cell viability. Its function can partially be replaced by GCN3 under normal growth conditions in GCD2-defective mutants, under AA starvation conditions GCN3 is an antagonist (GCN4 translational activator).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, Repressor

Keywords - Biological processi

Protein biosynthesis, Translation regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-30795-MONOMER.
ReactomeiR-SCE-72731. Recycling of eIF2:GDP.

Names & Taxonomyi

Protein namesi
Recommended name:
Translation initiation factor eIF-2B subunit delta
Alternative name(s):
GCD complex subunit GCD2
Guanine nucleotide exchange factor subunit GCD2
eIF-2B GDP-GTP exchange factor subunit delta
Gene namesi
Name:GCD2
Synonyms:TIF224
Ordered Locus Names:YGR083C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGR083C.
SGDiS000003315. GCD2.

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
Initiator methionineiRemovedCombined sources
Chaini2 – 651650Translation initiation factor eIF-2B subunit deltaPRO_0000156072Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei106 – 1061PhosphoserineSequence analysis
Modified residuei121 – 1211PhosphothreonineSequence analysis

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP12754.
PeptideAtlasiP12754.

PTM databases

iPTMnetiP12754.

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
GCD7P325025EBI-6265,EBI-6260
GCN3P147413EBI-6265,EBI-6253

Protein-protein interaction databases

BioGridi33325. 53 interactions.
DIPiDIP-2343N.
IntActiP12754. 14 interactions.
MINTiMINT-485124.

Structurei

3D structure databases

ProteinModelPortaliP12754.
SMRiP12754. Positions 304-519.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi6 – 106101Arg/Lys-rich (basic)Add
BLAST

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00550000075009.
HOGENOMiHOG000176924.
InParanoidiP12754.
KOiK03680.
OMAiFEGRKMA.
OrthoDBiEOG7KSXK1.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P12754-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSESEAKSRS ATPPSKAKQA TPTTTAAANG EKKLTNKELK ELKKQEKAAK
60 70 80 90 100
RAAMKQANGI SIEQQQQQAQ MKKEKKQLQR EQQQKREQKQ KNANKKKQNE
110 120 130 140 150
RNVKKSTLFG HLETTEERRA TILALTSAVS SPKTSRITAA GLMVPVVASA
160 170 180 190 200
LSGSNVLTAS SLMPVGPNAS STVSASAPAS TTTTLPASSA ALSAGTSSAS
210 220 230 240 250
TNTPTAIQQE IASSNASDVA KTLASISLEA GEFNVIPGIS SVIPTVLEQS
260 270 280 290 300
FDNSSLISSV KELLLNKDLI HPSILLLTSH LAHYKIVGSI PRCIAMLEVF
310 320 330 340 350
QIVIKDYQTP KGTTLSRNLT SYLSHQIDLL KKARPLSVTM GNAIRWLKQE
360 370 380 390 400
ISLIDPSTPD KAAKKDLCEK IGQFAKEKIE LADQLIIDNA STQIEESTTI
410 420 430 440 450
VTYGSSKVLT ELLLHNAISL KKNIKVIVVD SRPLFEGRKM AETLRNAGVN
460 470 480 490 500
VMYALITSLD TIFNMDVDYV FLGAHSILSN GFLYSRAGTA MLAMSAKRRN
510 520 530 540 550
IPVLVCCESL KFSQRVQLDS VTFNELADPN DLVNIDYENP VERRGNKGAL
560 570 580 590 600
LNQFIKERKF EKKKLAMENK PKGNKIGGKK GSEGESKDAS NEEDSNSKNI
610 620 630 640 650
LDGWQELPSL NIVNILYDLT PPEYIKKVIT EFGALPPSSV PVILREYKGS

A
Length:651
Mass (Da):70,852
Last modified:October 1, 1989 - v1
Checksum:iB188457543CE1AAE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15658 Genomic DNA. Translation: CAA33693.1.
Z72868 Genomic DNA. Translation: CAA97085.1.
BK006941 Genomic DNA. Translation: DAA08176.1.
PIRiS05809. RGBYD2.
RefSeqiNP_011597.1. NM_001181212.1.

Genome annotation databases

EnsemblFungiiYGR083C; YGR083C; YGR083C.
GeneIDi852974.
KEGGisce:YGR083C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15658 Genomic DNA. Translation: CAA33693.1.
Z72868 Genomic DNA. Translation: CAA97085.1.
BK006941 Genomic DNA. Translation: DAA08176.1.
PIRiS05809. RGBYD2.
RefSeqiNP_011597.1. NM_001181212.1.

3D structure databases

ProteinModelPortaliP12754.
SMRiP12754. Positions 304-519.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33325. 53 interactions.
DIPiDIP-2343N.
IntActiP12754. 14 interactions.
MINTiMINT-485124.

PTM databases

iPTMnetiP12754.

Proteomic databases

MaxQBiP12754.
PeptideAtlasiP12754.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGR083C; YGR083C; YGR083C.
GeneIDi852974.
KEGGisce:YGR083C.

Organism-specific databases

EuPathDBiFungiDB:YGR083C.
SGDiS000003315. GCD2.

Phylogenomic databases

GeneTreeiENSGT00550000075009.
HOGENOMiHOG000176924.
InParanoidiP12754.
KOiK03680.
OMAiFEGRKMA.
OrthoDBiEOG7KSXK1.

Enzyme and pathway databases

BioCyciYEAST:G3O-30795-MONOMER.
ReactomeiR-SCE-72731. Recycling of eIF2:GDP.

Miscellaneous databases

NextBioi972768.
PROiP12754.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Amino acid sequence similarity between GCN3 and GCD2, positive and negative translational regulators of GCN4: evidence for antagonism by competition."
    Paddon C.J., Hanning E.M., Hinnebusch A.G.
    Genetics 122:551-559(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: S288c / GRF88.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(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].
  7. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiEI2BD_YEAST
AccessioniPrimary (citable) accession number: P12754
Secondary accession number(s): D6VUL5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: May 11, 2016
This is version 143 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 10300 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 VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: 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.