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Protein

Translation initiation factor eIF-2B subunit gamma

Gene

GCD1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 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. GCD1 stabilizes the interaction between eIF-2 and GCD6 and stimulates the catalytic activity in vitro.2 Publications

GO - Molecular functioni

  • translation initiation factor activity Source: SGD

GO - Biological processi

  • negative regulation of cellular response to amino acid starvation Source: SGD
  • positive regulation of GTPase 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-33751-MONOMER.
ReactomeiR-SCE-72731. Recycling of eIF2:GDP.

Names & Taxonomyi

Protein namesi
Recommended name:
Translation initiation factor eIF-2B subunit gamma
Alternative name(s):
GCD complex subunit GCD1
Guanine nucleotide exchange factor subunit GCD1
eIF-2B GDP-GTP exchange factor subunit gamma
Gene namesi
Name:GCD1
Synonyms:TIF223, TRA3
Ordered Locus Names:YOR260W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR260W.
SGDiS000005786. GCD1.

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 – 578578Translation initiation factor eIF-2B subunit gammaPRO_0000156083Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei296 – 2961PhosphoserineCombined sources
Modified residuei300 – 3001PhosphoserineCombined sources
Modified residuei306 – 3061PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP09032.

PTM databases

iPTMnetiP09032.

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 catalytic subcomplex comprising GCD1 and GCD6 interacts with both, phosphorylated and non-phosphorylated eIF-2 and has exchange activity in vitro.2 Publications

Protein-protein interaction databases

BioGridi34650. 34 interactions.
DIPiDIP-1327N.
IntActiP09032. 18 interactions.
MINTiMINT-400094.

Structurei

3D structure databases

ProteinModelPortaliP09032.
SMRiP09032. Positions 425-516.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00510000047486.
HOGENOMiHOG000248845.
InParanoidiP09032.
KOiK03241.
OMAiTNCYVEG.
OrthoDBiEOG7008K9.

Family and domain databases

Gene3Di3.90.550.10. 4 hits.
InterProiIPR029044. Nucleotide-diphossugar_trans.
IPR011004. Trimer_LpxA-like.
[Graphical view]
SUPFAMiSSF51161. SSF51161. 1 hit.
SSF53448. SSF53448. 3 hits.

Sequencei

Sequence statusi: Complete.

P09032-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIQAFVFCG KGSNLAPFTQ PDFPFQTQNK DSTAATSGDK LNELVNSALD
60 70 80 90 100
STVINEFMQH STRLPKALLP IGNRPMIEYV LDWCDQADFK EISVVAPVDE
110 120 130 140 150
IELIESGLTS FLSLRKQQFE LIYKALSNSN HSHHLQDPKK INFIPSKANS
160 170 180 190 200
TGESLQKELL PRINGDFVIL PCDFVTDIPP QVLVDQFRNR DDNNLAMTIY
210 220 230 240 250
YKNSLDSSID KKQQQKQKQQ QFFTVYSENE DSERQPILLD VYSQRDVTKT
260 270 280 290 300
KYLQIRSHLL WNYPNLTVST KLLNSFIYFC SFELCQLLKL GPQSMSRQAS
310 320 330 340 350
FKDPFTGNQQ QQNPPTTDDD EDRNHDDDDD YKPSATSIQP TYFKKKNDLI
360 370 380 390 400
LDPINCNKSL SKVFRDLSRR SWQHSKPREP IGIFILPNET LFIRANNLNA
410 420 430 440 450
YMDANRFVLK IKSQTMFTKN IQIQSAAIGA DAIVDPKCQI SAHSNVKMSV
460 470 480 490 500
LGTQANIGSR CRVAGSLLFP GVHLGDEVIL ENCIIGPMAK IGSKCKLSNC
510 520 530 540 550
YIEGHYVVEP KNNFKGETLA NVYLDEDEED ELIYDDSVIA GESEIAEETD
560 570
SDDRSDEDSD DSEYTDEYEY EDDGLFER
Length:578
Mass (Da):65,700
Last modified:November 1, 1997 - v3
Checksum:iEC25BAE00F4D1E94
GO

Sequence cautioni

The sequence CAA30693.1 differs from that shown. Reason: Frameshift at position 503. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti217 – 24024QKQQQ…PILLD → AKNNSNFSLFIQKTKTQRGS QYFWN in CAA30693 (PubMed:3050897).CuratedAdd
BLAST
Sequence conflicti491 – 4922IG → SV in CAA30693 (PubMed:3050897).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07846 Genomic DNA. Translation: CAA30693.1. Frameshift.
Z75168 Genomic DNA. Translation: CAA99482.1.
BK006948 Genomic DNA. Translation: DAA11027.1.
PIRiS67157. BVBYD1.
RefSeqiNP_014903.1. NM_001183679.1.

Genome annotation databases

EnsemblFungiiYOR260W; YOR260W; YOR260W.
GeneIDi854434.
KEGGisce:YOR260W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07846 Genomic DNA. Translation: CAA30693.1. Frameshift.
Z75168 Genomic DNA. Translation: CAA99482.1.
BK006948 Genomic DNA. Translation: DAA11027.1.
PIRiS67157. BVBYD1.
RefSeqiNP_014903.1. NM_001183679.1.

3D structure databases

ProteinModelPortaliP09032.
SMRiP09032. Positions 425-516.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34650. 34 interactions.
DIPiDIP-1327N.
IntActiP09032. 18 interactions.
MINTiMINT-400094.

PTM databases

iPTMnetiP09032.

Proteomic databases

MaxQBiP09032.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR260W; YOR260W; YOR260W.
GeneIDi854434.
KEGGisce:YOR260W.

Organism-specific databases

EuPathDBiFungiDB:YOR260W.
SGDiS000005786. GCD1.

Phylogenomic databases

GeneTreeiENSGT00510000047486.
HOGENOMiHOG000248845.
InParanoidiP09032.
KOiK03241.
OMAiTNCYVEG.
OrthoDBiEOG7008K9.

Enzyme and pathway databases

BioCyciYEAST:G3O-33751-MONOMER.
ReactomeiR-SCE-72731. Recycling of eIF2:GDP.

Miscellaneous databases

PROiP09032.

Family and domain databases

Gene3Di3.90.550.10. 4 hits.
InterProiIPR029044. Nucleotide-diphossugar_trans.
IPR011004. Trimer_LpxA-like.
[Graphical view]
SUPFAMiSSF51161. SSF51161. 1 hit.
SSF53448. SSF53448. 3 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization of GCD1, a yeast gene required for general control of amino acid biosynthesis and cell-cycle initiation."
    Hill D.E., Struhl K.
    Nucleic Acids Res. 16:9253-9265(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cigan A.M., Pavitt G.
    Submitted (NOV-1994) to UniProtKB
    Cited for: SEQUENCE REVISION TO C-TERMINUS.
  3. "Sequencing analysis of a 36.8 kb fragment of yeast chromosome XV reveals 26 open reading frames including SEC63, CDC31, SUG2, GCD1, RBL2, PNT1, PAC1 and VPH1."
    Poirey R., Jauniaux J.-C.
    Yeast 13:483-487(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. "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.
  7. "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.
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "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-296 AND SER-300, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-306, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiEI2BG_YEAST
AccessioniPrimary (citable) accession number: P09032
Secondary accession number(s): D6W2W1, Q08721
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1997
Last modified: July 6, 2016
This is version 147 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 9530 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 XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: 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.