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P33887

- IF2G_RABIT

UniProt

P33887 - IF2G_RABIT

Protein

Eukaryotic translation initiation factor 2 subunit 3

Gene

EIF2S3

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 59 (01 Oct 2014)
      Sequence version 2 (27 May 2002)
      Previous versions | rss
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    Functioni

    eIF-2 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.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi51 – 544GTPBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. translational initiation Source: UniProtKB

    Keywords - Molecular functioni

    Initiation factor

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Eukaryotic translation initiation factor 2 subunit 3
    Alternative name(s):
    Eukaryotic translation initiation factor 2 subunit gamma
    Short name:
    eIF-2-gamma
    Gene namesi
    Name:EIF2S3
    Synonyms:EIF2G
    OrganismiOryctolagus cuniculus (Rabbit)
    Taxonomic identifieri9986 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
    ProteomesiUP000001811: Unplaced

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – ›152›152Eukaryotic translation initiation factor 2 subunit 3PRO_0000137442Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylalanineBy similarity

    Keywords - PTMi

    Acetylation

    Interactioni

    Subunit structurei

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

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR027417. P-loop_NTPase.
    IPR015256. TIF2_gsu_C.
    IPR009001. Transl_elong_EF1A/Init_IF2_C.
    [Graphical view]
    PfamiPF09173. eIF2_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF50465. SSF50465. 1 hit.

    Sequencei

    Sequence statusi: Fragments.

    P33887-1 [UniParc]FASTAAdd to Basket

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    AGGEAGVTLG QPSLVEQDSH SGFKNELERD GGLLLIAGNE SKLKHILILG    50
    NKIDLVKESQ AKEQYGQILA FVQETVAXGA TVGQVLGAVG ALPEIFTELX 100
    IVNIGSLSTG GQVSAVKADL GKIVLTNPVX TEVGEEKSVE KHWRLIGWGQ 150
    IR 152
    Length:152
    Mass (Da):16,014
    Last modified:May 27, 2002 - v2
    Checksum:iCA56E544FA684CA7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti3 – 31G → T AA sequence (PubMed:3745199)Curated
    Sequence uncertaintyi20 – 201
    Non-adjacent residuesi22 – 232Curated
    Non-adjacent residuesi29 – 302Curated
    Non-adjacent residuesi41 – 422Curated
    Non-adjacent residuesi81 – 822Curated
    Non-adjacent residuesi101 – 1022Curated
    Sequence conflicti112 – 1121Q → W AA sequence (PubMed:1911855)Curated
    Non-adjacent residuesi137 – 1382Curated
    Non-terminal residuei152 – 1521

    Cross-referencesi

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR015256. TIF2_gsu_C.
    IPR009001. Transl_elong_EF1A/Init_IF2_C.
    [Graphical view ]
    Pfami PF09173. eIF2_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50465. SSF50465. 1 hit.
    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 OF 1-22.
      Tissue: Reticulocyte.
    2. "Amino acid sequence analysis of the beta- and gamma-subunits of eukaryotic initiation factor eIF-2. Identification of regions interacting with GTP."
      Bommer U.-A., Kraft R., Kurzchalia T.V., Price N.T., Proud C.G.
      Biochim. Biophys. Acta 1079:308-315(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-15 AND 82-126.
      Tissue: Reticulocyte.
    3. "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 1-8.
      Tissue: Reticulocyte.
    4. "GCD11, a negative regulator of GCN4 expression, encodes the gamma subunit of eIF-2 in Saccharomyces cerevisiae."
      Hannig E.M., Cigan A.M., Freeman B.A., Kinzy T.G.
      Mol. Cell. Biol. 13:506-520(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 23-99 AND 102-152.

    Entry informationi

    Entry nameiIF2G_RABIT
    AccessioniPrimary (citable) accession number: P33887
    Secondary accession number(s): Q9TRV8, Q9TRV9, Q9TRW0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: May 27, 2002
    Last modified: October 1, 2014
    This is version 59 of the entry and version 2 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