P83268 (IF2A_RABIT) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 65.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | 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 names |
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| Organism | Oryctolagus cuniculus (Rabbit) [Reference proteome] | ||||
| Taxonomic identifier | 9986 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus![]() |
Protein attributes
| Sequence length | 52 AA. |
| Sequence status | Fragment. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | 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. |
| Subunit structure | 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. |
| Subcellular location | 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. Co-localizes with NANOS3 in the stress granules By similarity. |
| Post-translational modification | 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. |
| Sequence similarities | Belongs to the eIF-2-alpha family. Contains 1 S1 motif domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis Translation regulation |
| Ligand | RNA-binding |
| Molecular function | Initiation factor |
| PTM | Phosphoprotein |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | regulation of translation Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | cytoplasmic stress granule Inferred from sequence or structural similarity. Source: UniProtKB |
| Molecular_function | GTP binding Non-traceable author statement Ref.2Ref.1. Source: UniProtKB ribosome bindingInferred from sequence or structural similarity. Source: UniProtKB translation initiation factor activityNon-traceable author statement Ref.2Ref.1. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – ›52 | ›52 | Eukaryotic translation initiation factor 2 subunit 1 | PRO_0000137385 | |||||
Regions | |||||||||
| Domain | 16 – ›52 | ›37 | S1 motif | ||||||
Amino acid modifications | |||||||||
| Modified residue | 48 | 1 | Phosphoserine; by HRI Ref.1 | ||||||
| Modified residue | 51 | 1 | Phosphoserine; by EIF2AK3, GCN2, HRI and PKR By similarity | ||||||
Experimental info | |||||||||
| Sequence uncertainty | 10 | 1 | |||||||
| Sequence uncertainty | 44 | 1 | |||||||
| Sequence uncertainty | 52 | 1 | |||||||
| Sequence conflict | 10 | 1 | H → R AA sequence Ref.2 | ||||||
| Sequence conflict | 16 | 1 | E → Q AA sequence Ref.1 | ||||||
| Non-terminal residue | 52 | 1 | |||||||
Sequences
References
| [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. |
Cross-references
3D structure databases | |
|---|---|
| ProteinModelPortal | P83268. |
| SMR | P83268. Positions 3-50. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P83268. 1 interaction. |
| STRING | 9986.ENSOCUP00000010342. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| eggNOG | COG1093. |
| HOGENOM | HOG000199476. |
| OrthoDB | EOG4BZN35. |
Family and domain databases | |
| Gene3D | 2.40.50.140. 1 hit. |
| InterPro | IPR012340. NA-bd_OB-fold. IPR003029. Rbsml_prot_S1_RNA-bd_dom. [Graphical view] |
| Pfam | PF00575. S1. 1 hit. [Graphical view] |
| SUPFAM | SSF50249. Nucleic_acid_OB. 1 hit. |
| PROSITE | PS50126. S1. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | IF2A_RABIT | ||||||||
| Accession | Primary (citable) accession number: P83268 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| Translation initiation factors List of translation initiation factor entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with
