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P83268

- IF2A_RABIT

UniProt

P83268 - IF2A_RABIT

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Protein

Eukaryotic translation initiation factor 2 subunit 1

Gene
EIF2S1, EIF2A
Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S preinitiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B.

GO - Molecular functioni

  1. GTP binding Source: UniProtKB
  2. ribosome binding Source: UniProtKB
  3. translation initiation factor activity Source: UniProtKB

GO - Biological processi

  1. regulation of translation Source: UniProtKB-KW
  2. translational initiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis, Translation regulation

Keywords - Ligandi

RNA-binding

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
Short name:
eIF-2A
Short name:
eIF-2alpha
Gene namesi
Name:EIF2S1
Synonyms:EIF2A
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811: Unplaced

Subcellular locationi

Cytoplasmic granule By similarity
Note: The cytoplasmic granules are stress granules which are a dense aggregation in the cytosol composed of proteins and RNAs that appear when the cell is under stress. Colocalizes with NANOS3 in the stress granules By similarity.

GO - Cellular componenti

  1. cytoplasmic stress granule Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›52›52Eukaryotic translation initiation factor 2 subunit 1PRO_0000137385Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei48 – 481Phosphoserine; by HRI1 Publication
Modified residuei51 – 511Phosphoserine; by EIF2AK3, GCN2, HRI and PKR By similarity

Post-translational modificationi

Substrate for at least 4 kinases: EIF2AK3/PERK, GCN2, HRI and PKR. Phosphorylation stabilizes the eIF-2/GDP/eIF-2B complex and prevents GDP/GTP exchange reaction, thus impairing the recycling of eIF-2 between successive rounds of initiation and leading to global inhibition of translation By similarity.

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

Heterotrimer composed of an alpha, a beta and a gamma chain. Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. Interacts with ABCF1. Associates with ribosomes. Interaction with METAP2 protects EIF2S1 from inhibitory phosphorylation By similarity.

Protein-protein interaction databases

IntActiP83268. 1 interaction.
STRINGi9986.ENSOCUP00000010342.

Structurei

3D structure databases

ProteinModelPortaliP83268.
SMRiP83268. Positions 3-50.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – ›52›37S1 motifAdd
BLAST

Sequence similaritiesi

Belongs to the eIF-2-alpha family.
Contains 1 S1 motif domain.

Phylogenomic databases

eggNOGiCOG1093.
HOGENOMiHOG000199476.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR003029. Rbsml_prot_S1_RNA-bd_dom.
[Graphical view]
PfamiPF00575. S1. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
PROSITEiPS50126. S1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

P83268-1 [UniParc]FASTAAdd to Basket

« Hide

PGLSCRFYQH KFPEVEDVVM VNVRSIAEMG AYVSLLEYNN IEGRILLSEL   50
SR 52
Length:52
Mass (Da):5,974
Last modified:March 1, 2002 - v1
Checksum:i52E63D8DCEA6B804
GO

Sequence uncertainty

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence uncertaintyi10 – 101
Sequence uncertaintyi44 – 441
Sequence uncertaintyi52 – 521

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101H → R AA sequence 1 Publication
Sequence conflicti16 – 161E → Q AA sequence 1 Publication

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei52 – 521

Cross-referencesi

3D structure databases

ProteinModelPortali P83268.
SMRi P83268. Positions 3-50.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P83268. 1 interaction.
STRINGi 9986.ENSOCUP00000010342.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG1093.
HOGENOMi HOG000199476.

Family and domain databases

Gene3Di 2.40.50.140. 1 hit.
InterProi IPR012340. NA-bd_OB-fold.
IPR003029. Rbsml_prot_S1_RNA-bd_dom.
[Graphical view ]
Pfami PF00575. S1. 1 hit.
[Graphical view ]
SUPFAMi SSF50249. SSF50249. 1 hit.
PROSITEi PS50126. S1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The NH2-terminal sequence of the alpha and gamma subunits of eukaryotic initiation factor 2 and the phosphorylation site for the heme-regulated eIF-2 alpha kinase."
    Wettenhall R.E.H., Kudlicki W., Kramer G., Hardesty B.
    J. Biol. Chem. 261:12444-12447(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, PHOSPHORYLATION AT SER-48.
    Tissue: Reticulocyte.
  2. "The purification and characterization of subunits alpha, beta, and gamma from the rabbit reticulocyte eukaryotic initiation factor 2."
    Schafer M.P., Fairwell T., Parker D.S., Knight M., Anderson W.F., Safer B.
    Arch. Biochem. Biophys. 255:337-346(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-23.
    Tissue: Reticulocyte.

Entry informationi

Entry nameiIF2A_RABIT
AccessioniPrimary (citable) accession number: P83268
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: March 1, 2002
Last modified: April 16, 2014
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Translation initiation factors
    List of translation initiation factor entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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