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Protein

Eukaryotic translation initiation factor 2A

Gene

YGR054W

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

Functions in the early steps of protein synthesis of a small number of specific mRNAs. Acts by directing the binding of methionyl-tRNAi to 40S ribosomal subunits. In contrast to the eIF-2 complex, it binds methionyl-tRNAi to 40 S subunits in a codon-dependent manner, whereas the eIF-2 complex binds methionyl-tRNAi to 40 S subunits in a GTP-dependent manner. May act by impiging the expression of specific proteins. Specifically associates with both 40S subunits and 80 S ribosomes.2 Publications

GO - Molecular functioni

  • translation initiation factor activity Source: SGD

GO - Biological processi

  • regulation of translation Source: UniProtKB-KW
  • 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-30771-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 2A
Short name:
eIF-2A
Gene namesi
Ordered Locus Names:YGR054W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGR054W.
SGDiS000003286. YGR054W.

Subcellular locationi

GO - Cellular componenti

  • cytosolic ribosome Source: SGD
  • cytosolic small ribosomal subunit Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 642642Eukaryotic translation initiation factor 2APRO_0000202800Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei564 – 5641PhosphoserineCombined sources
Modified residuei567 – 5671PhosphoserineCombined sources
Modified residuei572 – 5721PhosphoserineCombined sources

Post-translational modificationi

Ubiquitinated, probably leading to its degradation. May explain why it has a short half-life of 17 minutes.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP53235.
PeptideAtlasiP53235.

PTM databases

iPTMnetiP53235.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
XRN1P221474EBI-23172,EBI-9642

Protein-protein interaction databases

BioGridi33299. 73 interactions.
DIPiDIP-5518N.
IntActiP53235. 14 interactions.
MINTiMINT-562628.

Structurei

3D structure databases

ProteinModelPortaliP53235.
SMRiP53235. Positions 3-430.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati69 – 11547WD 1Add
BLAST
Repeati186 – 22439WD 2Add
BLAST
Repeati289 – 33143WD 3Add
BLAST
Repeati374 – 41946WD 4Add
BLAST

Sequence similaritiesi

Belongs to the WD repeat EIF2A family.Curated
Contains 4 WD repeats.Curated

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

GeneTreeiENSGT00730000111053.
HOGENOMiHOG000193775.
InParanoidiP53235.
KOiK15026.
OMAiICTIESG.
OrthoDBiEOG7XWPZ7.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR011387. TIF2A.
IPR013979. TIF_beta_prop-like.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
PfamiPF08662. eIF2A. 1 hit.
[Graphical view]
PIRSFiPIRSF017222. eIF2A. 1 hit.

Sequencei

Sequence statusi: Complete.

P53235-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSQFFLKTS QDIELFQSYP TFEQSNTNSK DFPVISSVLS PCGRFLALST
60 70 80 90 100
KENVKVFTGP CLDNVLLTMK LSDVYDLHFS PAGNYLSTWE RASIQDPNHK
110 120 130 140 150
NVKVWYLNKP FKKDCVSEDI VPAYEYQAKS QSGWFLQFSK LDNYGLRLFK
160 170 180 190 200
HDLKIVKLSS ANADNFDFQS PFAVLSDDET SQHFTTYLIS PAEHPTICTF
210 220 230 240 250
TPEKGGKPAQ LIIWALSEGK ITKKIASKTF FKADSCQLKW NPLGNAILCL
260 270 280 290 300
AITDFDSSNK SYYGENTLYL LSFQGVNGTL GGNSVRVSLT TGPVHDFTWS
310 320 330 340 350
PTSRQFGVIA GYMPATISFF DLRGNVVHSL PQQAKNTMLF SPSGHYILIA
360 370 380 390 400
GFGNLQGSVE ILDRLDKFKC VSKFDATNTS VCKWSPGGEF IMTATTSPRL
410 420 430 440 450
RVDNGVKIWH VSGSLVFVKE FKELLKVDWR SPCNYKTLEN KDEAFFENHI
460 470 480 490 500
INNWEPLPDS TTSSLDPKIS NKSELQIHSS VQEYISQHPS REASSNGNGS
510 520 530 540 550
KAKAGGAYKP PHARRTGGGR IVPGVPPGAA KKTIPGLVPG MSANKDANTK
560 570 580 590 600
NRRRRANKKS SETSPDSTPA PSAPASTNAP TNNKETSPEE KKIRSLLKKL
610 620 630 640
RAIETLKERQ AVGDKLEDTQ VLKIQTEEKV LKDLEKLGWK DE
Length:642
Mass (Da):71,305
Last modified:October 1, 1996 - v1
Checksum:iF3C2E78504D83418
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti145 – 1451G → A in strain: SK1. 1 Publication
Natural varianti165 – 1651N → K in strain: SK1. 1 Publication
Natural varianti569 – 5691P → S in strain: SK1. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ115391 Genomic DNA. Translation: AAZ22467.1.
Z72839 Genomic DNA. Translation: CAA97054.1.
Z72840 Genomic DNA. Translation: CAA97056.1.
BK006941 Genomic DNA. Translation: DAA08150.1.
PIRiS64348.
RefSeqiNP_011568.3. NM_001181183.4.

Genome annotation databases

EnsemblFungiiYGR054W; YGR054W; YGR054W.
GeneIDi852945.
KEGGisce:YGR054W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ115391 Genomic DNA. Translation: AAZ22467.1.
Z72839 Genomic DNA. Translation: CAA97054.1.
Z72840 Genomic DNA. Translation: CAA97056.1.
BK006941 Genomic DNA. Translation: DAA08150.1.
PIRiS64348.
RefSeqiNP_011568.3. NM_001181183.4.

3D structure databases

ProteinModelPortaliP53235.
SMRiP53235. Positions 3-430.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33299. 73 interactions.
DIPiDIP-5518N.
IntActiP53235. 14 interactions.
MINTiMINT-562628.

PTM databases

iPTMnetiP53235.

Proteomic databases

MaxQBiP53235.
PeptideAtlasiP53235.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGR054W; YGR054W; YGR054W.
GeneIDi852945.
KEGGisce:YGR054W.

Organism-specific databases

EuPathDBiFungiDB:YGR054W.
SGDiS000003286. YGR054W.

Phylogenomic databases

GeneTreeiENSGT00730000111053.
HOGENOMiHOG000193775.
InParanoidiP53235.
KOiK15026.
OMAiICTIESG.
OrthoDBiEOG7XWPZ7.

Enzyme and pathway databases

BioCyciYEAST:G3O-30771-MONOMER.

Miscellaneous databases

NextBioi972690.
PROiP53235.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR011387. TIF2A.
IPR013979. TIF_beta_prop-like.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
PfamiPF08662. eIF2A. 1 hit.
[Graphical view]
PIRSFiPIRSF017222. eIF2A. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Quantitative trait loci mapped to single-nucleotide resolution in yeast."
    Deutschbauer A.M., Davis R.W.
    Nat. Genet. 37:1333-1340(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-145; LYS-165 AND SER-569.
    Strain: SK1.
  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. "Characterization of mammalian eIF2A and identification of the yeast homolog."
    Zoll W.L., Horton L.E., Komar A.A., Hensold J.O., Merrick W.C.
    J. Biol. Chem. 277:37079-37087(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS].
    Strain: SUB592.
  6. "Novel characteristics of the biological properties of the yeast Saccharomyces cerevisiae eukaryotic initiation factor 2A."
    Komar A.A., Gross S.R., Barth-Baus D., Strachan R., Hensold J.O., Goss Kinzy T., Merrick W.C.
    J. Biol. Chem. 280:15601-15611(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "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-564, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  8. "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].
  9. "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-564; SER-567 AND SER-572, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiEIF2A_YEAST
AccessioniPrimary (citable) accession number: P53235
Secondary accession number(s): D6VUI9, Q45U32
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 11, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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.