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P33887

- IF2G_RABIT

UniProt

P33887 - IF2G_RABIT

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Protein
Eukaryotic translation initiation factor 2 subunit 3
Gene
EIF2S3, EIF2G
Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

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 – 544GTP By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. translational initiation Source: UniProtKB
Complete GO annotation...

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 3
PRO_0000137442Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylalanine By 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

« Hide

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

Sequence uncertainty

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence uncertaintyi20 – 201

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31G → T AA sequence 1 Publication
Sequence conflicti112 – 1121Q → W AA sequence 1 Publication

Non-adjacent residues

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-adjacent residuesi22 – 232
Non-adjacent residuesi29 – 302
Non-adjacent residuesi41 – 422
Non-adjacent residuesi81 – 822
Non-adjacent residuesi101 – 1022
Non-adjacent residuesi137 – 1382

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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: April 16, 2014
This is version 58 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