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P32501 (EI2BE_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Translation initiation factor eIF-2B subunit epsilon
Alternative name(s):
GCD complex subunit GCD6
Guanine nucleotide exchange factor subunit GCD6
eIF-2B GDP-GTP exchange factor subunit epsilon
Gene names
Name:GCD6
Synonyms:TIF225
Ordered Locus Names:YDR211W
ORF Names:YD8142.12, YD8142B.03
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length712 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a catalytic 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.4 Ref.5

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 catalytic subcomplex comprising GCD1 and GCD6 interacts with both, phosphorylated and non-phosphorylated eIF-2 and has exchange activity in vitro. GCD6 interacts with SUI3. Ref.4 Ref.5 Ref.6

Miscellaneous

Present with 33800 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the eIF-2B gamma/epsilon subunits family.

Contains 1 W2 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 712712Translation initiation factor eIF-2B subunit epsilon
PRO_0000156078

Regions

Domain539 – 710172W2

Amino acid modifications

Modified residue4781Phosphoserine Ref.9 Ref.11
Modified residue4811Phosphoserine Ref.9 Ref.11
Modified residue5071Phosphoserine Ref.9
Modified residue5251Phosphoserine Ref.11
Modified residue5381Phosphoserine Ref.10 Ref.11
Modified residue7071Phosphoserine Ref.11

Experimental info

Mutagenesis5521T → I: Reduced exchange activity. Ref.7
Mutagenesis5691E → A: Lethal. Ref.12
Mutagenesis5761S → N: Reduced exchange activity. Ref.7
Mutagenesis655 – 67723LFSAL…IYKWW → AFSAAVSAADNDAAEAAVAA KWA: Abolishes binding to SUI3. Ref.6
Mutagenesis696 – 70611WVEWLQNADEE → AAEAAQNAAAA: Abolishes binding to SUI3; probably impairs the conversion of eIF-2-GDP to eIF-2-GTP. Ref.6

Secondary structure

................... 712
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P32501 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: EFE87F6AE2941619

FASTA71281,161
        10         20         30         40         50         60 
MAGKKGQKKS GLGNHGKNSD MDVEDRLQAV VLTDSYETRF MPLTAVKPRC LLPLANVPLI 

        70         80         90        100        110        120 
EYTLEFLAKA GVHEVFLICS SHANQINDYI ENSKWNLPWS PFKITTIMSP EARCTGDVMR 

       130        140        150        160        170        180 
DLDNRGIITG DFILVSGDVL TNIDFSKMLE FHKKMHLQDK DHISTMCLSK ASTYPKTRTI 

       190        200        210        220        230        240 
EPAAFVLDKS TSRCIYYQDL PLPSSREKTS IQIDPELLDN VDEFVIRNDL IDCRIDICTS 

       250        260        270        280        290        300 
HVPLIFQENF DYQSLRTDFV KGVISSDILG KHIYAYLTDE YAVRVESWQT YDTISQDFLG 

       310        320        330        340        350        360 
RWCYPLVLDS NIQDDQTYSY ESRHIYKEKD VVLAQSCKIG KCTAIGSGTK IGEGTKIENS 

       370        380        390        400        410        420 
VIGRNCQIGE NIRIKNSFIW DDCIIGNNSI IDHSLIASNA TLGSNVRLND GCIIGFNVKI 

       430        440        450        460        470        480 
DDNMDLDRNT KISASPLKNA GSRMYDNESN EQFDQDLDDQ TLAVSIVGDK GVGYIYESEV 

       490        500        510        520        530        540 
SDDEDSSTEA CKEINTLSNQ LDELYLSDDS ISSATKKTKK RRTMSVNSIY TDREEIDSEF 

       550        560        570        580        590        600 
EDEDFEKEGI ATVERAMENN HDLDTALLEL NTLRMSMNVT YHEVRIATIT ALLRRVYHFI 

       610        620        630        640        650        660 
ATQTLGPKDA VVKVFNQWGL LFKRQAFDEE EYIDLMNIIM EKIVEQSFDK PDLILFSALV 

       670        680        690        700        710 
SLYDNDIIEE DVIYKWWDNV STDPRYDEVK KLTVKWVEWL QNADEESSSE EE 

« 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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]"Conserved bipartite motifs in yeast eIF5 and eIF2Bepsilon, GTPase-activating and GDP-GTP exchange factors in translation initiation, mediate binding to their common substrate eIF2."
Asano K., Krishnamoorthy T., Phan L., Pavitt G.D., Hinnebusch A.G.
EMBO J. 18:1673-1688(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SUI3, MUTAGENESIS OF 655-THR--TRP-677 AND 696-TRP--GLU-706.
[7]"Identification of domains and residues within the epsilon subunit of eukaryotic translation initiation factor 2B (eIF2Bepsilon) required for guanine nucleotide exchange reveals a novel activation function promoted by eIF2B complex formation."
Gomez E., Pavitt G.D.
Mol. Cell. Biol. 20:3965-3976(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF THR-552 AND SER-576.
[8]"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] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478; SER-481 AND SER-507, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538, 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 SER-478; SER-481; SER-525; SER-538 AND SER-707, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Structure of the catalytic fragment of translation initiation factor 2B and identification of a critically important catalytic residue."
Boesen T., Mohammad S.S., Pavitt G.D., Andersen G.R.
J. Biol. Chem. 279:10584-10592(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 524-712, MUTAGENESIS OF GLU-569.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L07115 Genomic DNA. Translation: AAA65498.1.
Z68194 Genomic DNA. Translation: CAA92354.1.
Z68195 Genomic DNA. Translation: CAA92362.1.
BK006938 Genomic DNA. Translation: DAA12055.1.
PIRA48156.
RefSeqNP_010497.3. NM_001180519.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PAQX-ray2.30A524-712[»]
ProteinModelPortalP32501.
SMRP32501. Positions 36-149, 325-426, 544-704.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32265. 47 interactions.
DIPDIP-2328N.
IntActP32501. 29 interactions.
MINTMINT-527627.
STRING4932.YDR211W.

Proteomic databases

PaxDbP32501.
PeptideAtlasP32501.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR211W; YDR211W; YDR211W.
GeneID851797.
KEGGsce:YDR211W.

Organism-specific databases

CYGDYDR211w.
SGDS000002619. GCD6.

Phylogenomic databases

eggNOGCOG1208.
GeneTreeENSGT00510000047568.
HOGENOMHOG000216610.
KOK03240.
OMARVSNLLM.
OrthoDBEOG7NSBB4.

Enzyme and pathway databases

BioCycYEAST:G3O-29793-MONOMER.

Gene expression databases

GenevestigatorP32501.

Family and domain databases

Gene3D1.25.40.180. 1 hit.
InterProIPR016024. ARM-type_fold.
IPR001451. Hexapep_transf.
IPR016021. MIF4-like_typ_1/2/3.
IPR005835. NTP_transferase.
IPR011004. Trimer_LpxA-like.
IPR003307. W2_domain.
[Graphical view]
PfamPF00132. Hexapep. 2 hits.
PF00483. NTP_transferase. 1 hit.
PF02020. W2. 1 hit.
[Graphical view]
SMARTSM00515. eIF5C. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
SSF51161. SSF51161. 1 hit.
PROSITEPS51363. W2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP32501.
NextBio969629.
PROP32501.

Entry information

Entry nameEI2BE_YEAST
AccessionPrimary (citable) accession number: P32501
Secondary accession number(s): D6VSJ5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: April 16, 2014
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Yeast

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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references