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P83268

- IF2A_RABIT

UniProt

P83268 - IF2A_RABIT

Protein

Eukaryotic translation initiation factor 2 subunit 1

Gene

EIF2S1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. 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

    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.By similarity

    GO - Cellular componenti

    1. cytoplasmic stress granule Source: UniProtKB

    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 PKRBy 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.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.By similarity

    Protein-protein interaction databases

    IntActiP83268. 1 interaction.
    STRINGi9986.ENSOCUP00000010342.

    Structurei

    3D structure databases

    ProteinModelPortaliP83268.
    SMRiP83268. Positions 3-50.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini16 – ›52›37S1 motifPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence uncertaintyi10 – 101
    Sequence conflicti10 – 101H → R AA sequence (PubMed:3592677)Curated
    Sequence conflicti16 – 161E → Q AA sequence (PubMed:3745199)Curated
    Sequence uncertaintyi44 – 441
    Sequence uncertaintyi52 – 521
    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: October 1, 2014
    This is version 69 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