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P32501

- EI2BE_YEAST

UniProt

P32501 - EI2BE_YEAST

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Protein

Translation initiation factor eIF-2B subunit epsilon

Gene

GCD6

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  1. guanyl-nucleotide exchange factor activity Source: SGD
  2. nucleotidyltransferase activity Source: InterPro
  3. translation initiation factor activity Source: SGD

GO - Biological processi

  1. positive regulation of GTPase activity Source: GOC
  2. 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-29793-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:GCD6
Synonyms:TIF225
Ordered Locus Names:YDR211W
ORF Names:YD8142.12, YD8142B.03
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

CYGDiYDR211w.
SGDiS000002619. GCD6.

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi552 – 5521T → I: Reduced exchange activity. 1 Publication
Mutagenesisi569 – 5691E → A: Lethal. 1 Publication
Mutagenesisi576 – 5761S → N: Reduced exchange activity. 1 Publication
Mutagenesisi655 – 67723LFSAL…IYKWW → AFSAAVSAADNDAAEAAVAA KWA: Abolishes binding to SUI3. 1 PublicationAdd
BLAST
Mutagenesisi696 – 70611WVEWLQNADEE → AAEAAQNAAAA: Abolishes binding to SUI3; probably impairs the conversion of eIF-2-GDP to eIF-2-GTP. 1 PublicationAdd
BLAST

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 712712Translation initiation factor eIF-2B subunit epsilonPRO_0000156078Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei478 – 4781Phosphoserine2 Publications
Modified residuei481 – 4811Phosphoserine2 Publications
Modified residuei507 – 5071Phosphoserine1 Publication
Modified residuei525 – 5251Phosphoserine1 Publication
Modified residuei538 – 5381Phosphoserine2 Publications
Modified residuei707 – 7071Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP32501.
PaxDbiP32501.
PeptideAtlasiP32501.

Expressioni

Gene expression databases

GenevestigatoriP32501.

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. GCD6 interacts with SUI3.3 Publications

Protein-protein interaction databases

BioGridi32265. 48 interactions.
DIPiDIP-2328N.
IntActiP32501. 29 interactions.
MINTiMINT-527627.
STRINGi4932.YDR211W.

Structurei

Secondary structure

1
712
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi545 – 55814
Helixi563 – 57614
Helixi581 – 60121
Helixi607 – 61812
Helixi619 – 6246
Helixi629 – 64618
Helixi651 – 66414
Helixi670 – 6789
Helixi684 – 6863
Helixi687 – 70216

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PAQX-ray2.30A524-712[»]
ProteinModelPortaliP32501.
SMRiP32501. Positions 36-149, 343-433, 544-704.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32501.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini539 – 710172W2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 W2 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG1208.
GeneTreeiENSGT00510000047568.
HOGENOMiHOG000216610.
InParanoidiP32501.
KOiK03240.
OMAiEGKGYIW.
OrthoDBiEOG7NSBB4.

Family and domain databases

Gene3Di1.25.40.180. 1 hit.
3.90.550.10. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR001451. Hexapep_transf.
IPR016021. MIF4-like_typ_1/2/3.
IPR005835. NTP_transferase.
IPR029044. Nucleotide-diphossugar_trans.
IPR011004. Trimer_LpxA-like.
IPR003307. W2_domain.
[Graphical view]
PfamiPF00132. Hexapep. 2 hits.
PF00483. NTP_transferase. 1 hit.
PF02020. W2. 1 hit.
[Graphical view]
SMARTiSM00515. eIF5C. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF51161. SSF51161. 1 hit.
SSF53448. SSF53448. 2 hits.
PROSITEiPS51363. W2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32501-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAGKKGQKKS GLGNHGKNSD MDVEDRLQAV VLTDSYETRF MPLTAVKPRC
60 70 80 90 100
LLPLANVPLI EYTLEFLAKA GVHEVFLICS SHANQINDYI ENSKWNLPWS
110 120 130 140 150
PFKITTIMSP EARCTGDVMR DLDNRGIITG DFILVSGDVL TNIDFSKMLE
160 170 180 190 200
FHKKMHLQDK DHISTMCLSK ASTYPKTRTI EPAAFVLDKS TSRCIYYQDL
210 220 230 240 250
PLPSSREKTS IQIDPELLDN VDEFVIRNDL IDCRIDICTS HVPLIFQENF
260 270 280 290 300
DYQSLRTDFV KGVISSDILG KHIYAYLTDE YAVRVESWQT YDTISQDFLG
310 320 330 340 350
RWCYPLVLDS NIQDDQTYSY ESRHIYKEKD VVLAQSCKIG KCTAIGSGTK
360 370 380 390 400
IGEGTKIENS VIGRNCQIGE NIRIKNSFIW DDCIIGNNSI IDHSLIASNA
410 420 430 440 450
TLGSNVRLND GCIIGFNVKI DDNMDLDRNT KISASPLKNA GSRMYDNESN
460 470 480 490 500
EQFDQDLDDQ TLAVSIVGDK GVGYIYESEV SDDEDSSTEA CKEINTLSNQ
510 520 530 540 550
LDELYLSDDS ISSATKKTKK RRTMSVNSIY TDREEIDSEF EDEDFEKEGI
560 570 580 590 600
ATVERAMENN HDLDTALLEL NTLRMSMNVT YHEVRIATIT ALLRRVYHFI
610 620 630 640 650
ATQTLGPKDA VVKVFNQWGL LFKRQAFDEE EYIDLMNIIM EKIVEQSFDK
660 670 680 690 700
PDLILFSALV SLYDNDIIEE DVIYKWWDNV STDPRYDEVK KLTVKWVEWL
710
QNADEESSSE EE
Length:712
Mass (Da):81,161
Last modified:October 1, 1993 - v1
Checksum:iEFE87F6AE2941619
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L07115 Genomic DNA. Translation: AAA65498.1.
Z68194 Genomic DNA. Translation: CAA92354.1.
Z68195 Genomic DNA. Translation: CAA92362.1.
BK006938 Genomic DNA. Translation: DAA12055.1.
PIRiA48156.
RefSeqiNP_010497.3. NM_001180519.3.

Genome annotation databases

EnsemblFungiiYDR211W; YDR211W; YDR211W.
GeneIDi851797.
KEGGisce:YDR211W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L07115 Genomic DNA. Translation: AAA65498.1 .
Z68194 Genomic DNA. Translation: CAA92354.1 .
Z68195 Genomic DNA. Translation: CAA92362.1 .
BK006938 Genomic DNA. Translation: DAA12055.1 .
PIRi A48156.
RefSeqi NP_010497.3. NM_001180519.3.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1PAQ X-ray 2.30 A 524-712 [» ]
ProteinModelPortali P32501.
SMRi P32501. Positions 36-149, 343-433, 544-704.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32265. 48 interactions.
DIPi DIP-2328N.
IntActi P32501. 29 interactions.
MINTi MINT-527627.
STRINGi 4932.YDR211W.

Proteomic databases

MaxQBi P32501.
PaxDbi P32501.
PeptideAtlasi P32501.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDR211W ; YDR211W ; YDR211W .
GeneIDi 851797.
KEGGi sce:YDR211W.

Organism-specific databases

CYGDi YDR211w.
SGDi S000002619. GCD6.

Phylogenomic databases

eggNOGi COG1208.
GeneTreei ENSGT00510000047568.
HOGENOMi HOG000216610.
InParanoidi P32501.
KOi K03240.
OMAi EGKGYIW.
OrthoDBi EOG7NSBB4.

Enzyme and pathway databases

BioCyci YEAST:G3O-29793-MONOMER.

Miscellaneous databases

EvolutionaryTracei P32501.
NextBioi 969629.
PROi P32501.

Gene expression databases

Genevestigatori P32501.

Family and domain databases

Gene3Di 1.25.40.180. 1 hit.
3.90.550.10. 1 hit.
InterProi IPR016024. ARM-type_fold.
IPR001451. Hexapep_transf.
IPR016021. MIF4-like_typ_1/2/3.
IPR005835. NTP_transferase.
IPR029044. Nucleotide-diphossugar_trans.
IPR011004. Trimer_LpxA-like.
IPR003307. W2_domain.
[Graphical view ]
Pfami PF00132. Hexapep. 2 hits.
PF00483. NTP_transferase. 1 hit.
PF02020. W2. 1 hit.
[Graphical view ]
SMARTi SM00515. eIF5C. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 1 hit.
SSF51161. SSF51161. 1 hit.
SSF53448. SSF53448. 2 hits.
PROSITEi PS51363. W2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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 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.
    , 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. 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. 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.

Entry informationi

Entry nameiEI2BE_YEAST
AccessioniPrimary (citable) accession number: P32501
Secondary accession number(s): D6VSJ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: October 29, 2014
This is version 140 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 33800 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3