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Protein

Eukaryotic translation initiation factor 2 subunit 1

Gene

eIF-2alpha

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This preinitiation complex mediates ribosomal recognition of a start codon during the scanning process of the leader region.

GO - Molecular functioni

  • GTP binding Source: FlyBase
  • translation initiation factor activity Source: FlyBase
  • tRNA binding Source: FlyBase

GO - Biological processi

  • formation of translation initiation ternary complex Source: FlyBase
  • mitotic spindle elongation Source: FlyBase
  • mitotic spindle organization Source: FlyBase
  • translational initiation Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-DME-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-DME-381042. PERK regulates gene expression.
R-DME-382556. ABC-family proteins mediated transport.
R-DME-72649. Translation initiation complex formation.
R-DME-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-DME-72702. Ribosomal scanning and start codon recognition.
R-DME-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-DME-72731. Recycling of eIF2:GDP.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 2 subunit 1
Alternative name(s):
Eukaryotic translation initiation factor 2 subunit alpha
Short name:
eIF-2-alpha
Gene namesi
Name:eIF-2alpha
Synonyms:eIF2a
ORF Names:CG9946
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0261609. eIF-2alpha.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: FlyBase
  • eukaryotic translation initiation factor 2B complex Source: FlyBase
  • eukaryotic translation initiation factor 2 complex Source: FlyBase
  • microtubule associated complex Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 341341Eukaryotic translation initiation factor 2 subunit 1PRO_0000137387Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei51 – 511PhosphoserineBy similarity

Post-translational modificationi

Phosphorylation of eIF-2-alpha impairs the recycling of eIF-2 between successive rounds of initiation and thus leads to inhibition of translation.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP41374.
PRIDEiP41374.

PTM databases

iPTMnetiP41374.

Expressioni

Gene expression databases

BgeeiP41374.
ExpressionAtlasiP41374. differential.
GenevisibleiP41374. DM.

Interactioni

Subunit structurei

Heterotrimer composed of an alpha, a beta and a gamma chain.

Protein-protein interaction databases

BioGridi58956. 11 interactions.
DIPiDIP-23926N.
IntActiP41374. 3 interactions.
MINTiMINT-970949.
STRINGi7227.FBpp0074075.

Structurei

3D structure databases

ProteinModelPortaliP41374.
SMRiP41374. Positions 3-301.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 8772S1 motifPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the eIF-2-alpha family.Curated
Contains 1 S1 motif domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2916. Eukaryota.
COG1093. LUCA.
InParanoidiP41374.
KOiK03237.
OMAiGHPYDAF.
OrthoDBiEOG7FZ012.
PhylomeDBiP41374.

Family and domain databases

Gene3Di1.10.150.190. 1 hit.
2.40.50.140. 1 hit.
3.30.70.1130. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR022967. S1_dom.
IPR003029. S1_domain.
IPR024055. TIF2_asu_C.
IPR024054. TIF2_asu_middle.
IPR011488. TIF_2_asu.
[Graphical view]
PfamiPF07541. EIF_2_alpha. 1 hit.
PF00575. S1. 1 hit.
[Graphical view]
SMARTiSM00316. S1. 1 hit.
[Graphical view]
SUPFAMiSSF110993. SSF110993. 1 hit.
SSF116742. SSF116742. 1 hit.
SSF50249. SSF50249. 1 hit.
PROSITEiPS50126. S1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P41374-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALTSRFYNE RYPEIEDVVM VNVLSIAEMG AYVHLLEYNN IEGMILLSEL
60 70 80 90 100
SRRRIRSINK LIRVGKTEPV VVIRVDKEKG YIDLSKRRVS PEDVEKCTER
110 120 130 140 150
FAKAKAINSL LRHVADILGF EGNEKLEDLY QKTAWHFEKK YNNKTVAYDI
160 170 180 190 200
FKQSVTDPTV FDECNLEPET KEVLLSNIKR KLVSPTVKIR ADIECSCYGY
210 220 230 240 250
EGIDAVKASL TKGLELSTEE LPIRINLIAP PLYVMTTSTT KKTDGLKALE
260 270 280 290 300
VAIEHIRAKT SEYDGEFKVI MAPKLVTAID EADLARRLER AEAENAQVAG
310 320 330 340
DDDEEDGADQ EGMQFDPEKE FNHKGSGAGR ANEEDEEEEE D
Length:341
Mass (Da):38,646
Last modified:November 1, 1995 - v1
Checksum:iD06D1B6FBC628DF6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19196 mRNA. Translation: AAA53627.1.
AE014298 Genomic DNA. Translation: AAF48615.1.
AF145633 mRNA. Translation: AAD38608.1.
RefSeqiNP_001285329.1. NM_001298400.1.
NP_573130.1. NM_132902.4.
UniGeneiDm.3157.

Genome annotation databases

EnsemblMetazoaiFBtr0074300; FBpp0074075; FBgn0261609.
FBtr0343016; FBpp0309768; FBgn0261609.
GeneIDi32617.
KEGGidme:Dmel_CG9946.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19196 mRNA. Translation: AAA53627.1.
AE014298 Genomic DNA. Translation: AAF48615.1.
AF145633 mRNA. Translation: AAD38608.1.
RefSeqiNP_001285329.1. NM_001298400.1.
NP_573130.1. NM_132902.4.
UniGeneiDm.3157.

3D structure databases

ProteinModelPortaliP41374.
SMRiP41374. Positions 3-301.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi58956. 11 interactions.
DIPiDIP-23926N.
IntActiP41374. 3 interactions.
MINTiMINT-970949.
STRINGi7227.FBpp0074075.

PTM databases

iPTMnetiP41374.

Proteomic databases

PaxDbiP41374.
PRIDEiP41374.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0074300; FBpp0074075; FBgn0261609.
FBtr0343016; FBpp0309768; FBgn0261609.
GeneIDi32617.
KEGGidme:Dmel_CG9946.

Organism-specific databases

CTDi32617.
FlyBaseiFBgn0261609. eIF-2alpha.

Phylogenomic databases

eggNOGiKOG2916. Eukaryota.
COG1093. LUCA.
InParanoidiP41374.
KOiK03237.
OMAiGHPYDAF.
OrthoDBiEOG7FZ012.
PhylomeDBiP41374.

Enzyme and pathway databases

ReactomeiR-DME-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-DME-381042. PERK regulates gene expression.
R-DME-382556. ABC-family proteins mediated transport.
R-DME-72649. Translation initiation complex formation.
R-DME-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-DME-72702. Ribosomal scanning and start codon recognition.
R-DME-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-DME-72731. Recycling of eIF2:GDP.

Miscellaneous databases

GenomeRNAii32617.
PROiP41374.

Gene expression databases

BgeeiP41374.
ExpressionAtlasiP41374. differential.
GenevisibleiP41374. DM.

Family and domain databases

Gene3Di1.10.150.190. 1 hit.
2.40.50.140. 1 hit.
3.30.70.1130. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR022967. S1_dom.
IPR003029. S1_domain.
IPR024055. TIF2_asu_C.
IPR024054. TIF2_asu_middle.
IPR011488. TIF_2_asu.
[Graphical view]
PfamiPF07541. EIF_2_alpha. 1 hit.
PF00575. S1. 1 hit.
[Graphical view]
SMARTiSM00316. S1. 1 hit.
[Graphical view]
SUPFAMiSSF110993. SSF110993. 1 hit.
SSF116742. SSF116742. 1 hit.
SSF50249. SSF50249. 1 hit.
PROSITEiPS50126. S1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of the Drosophila melanogaster eIF-2 alpha gene encoding the alpha subunit of translation initiation factor eIF-2."
    Qu S., Cavener D.R.
    Gene 140:239-242(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Oregon-R.
    Tissue: Embryo.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. "A Drosophila full-length cDNA resource."
    Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.

Entry informationi

Entry nameiIF2A_DROME
AccessioniPrimary (citable) accession number: P41374
Secondary accession number(s): Q9V3G2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 8, 2016
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. Translation initiation factors
    List of translation initiation factor entries
  3. SIMILARITY comments
    Index of protein domains and families

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.