Q3SZV3 (EF1G_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 52.
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: Elongation factor 1-gamma Short name=EF-1-gamma Alternative name(s): eEF-1B gamma | ||
| Gene names |
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| Organism | Bos taurus (Bovine) | ||
| Taxonomic identifier | 9913 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Protein attributes
| Sequence length | 440 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Probably plays a role in anchoring the complex to other cellular components By similarity. |
| Subunit structure | EF-1 is composed of four subunits: alpha, beta, delta, and gamma By similarity. |
| Sequence similarities | Contains 1 EF-1-gamma C-terminal domain. Contains 1 GST C-terminal domain. Contains 1 GST N-terminal domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis |
| Molecular function | Elongation factor |
| PTM | Acetylation Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Cellular component | eukaryotic translation elongation factor 1 complex Inferred from electronic annotation. Source: InterPro |
| Molecular function | translation elongation factor activity Inferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 440 | 439 | Elongation factor 1-gamma | PRO_0000284654 | |||||
Regions | |||||||||
| Domain | 2 – 87 | 86 | GST N-terminal | ||||||
| Domain | 88 – 216 | 129 | GST C-terminal | ||||||
| Domain | 279 – 440 | 162 | EF-1-gamma C-terminal | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylalanine By similarity | ||||||
| Modified residue | 43 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 46 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 132 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 147 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 437 | 1 | N6-acetyllysine By similarity | ||||||
Sequences
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References
| [1] | NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Testis. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BC102691 mRNA. Translation: AAI02692.1. |
| IPI | IPI00706632. |
| RefSeq | NP_001035577.1. NM_001040487.1. |
| UniGene | Bt.62921. |
3D structure databases | |
| ProteinModelPortal | Q3SZV3. |
| SMR | Q3SZV3. Positions 279-440. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q3SZV3. |
Proteomic databases | |
| PRIDE | Q3SZV3. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 326581. |
| KEGG | bta:326581. |
Organism-specific databases | |
| CTD | 1937. |
Phylogenomic databases | |
| HOVERGEN | HBG051444. |
| InParanoid | Q3SZV3. |
| OrthoDB | EOG43JC4V. |
| PhylomeDB | Q3SZV3. |
Family and domain databases | |
| InterPro | IPR010987. Glutathione-S-Trfase_C-like. IPR004045. Glutathione_S-Trfase_N. IPR017933. Glutathione_S_Trfase/Cl_chnl_C. IPR004046. GST_C. IPR012336. Thioredoxin-like_fold. IPR001662. Transl_elong_EF1_G_con. [Graphical view] |
| Gene3D | G3DSA:1.20.1050.10. GST_C_like. 1 hit. G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit. G3DSA:3.30.70.1010. Transl_elong_EF1_G_con. 1 hit. |
| KO | K03233. |
| Pfam | PF00647. EF1G. 1 hit. PF00043. GST_C. 1 hit. PF02798. GST_N. 1 hit. [Graphical view] |
| SUPFAM | SSF47616. GST_C_like. 1 hit. SSF52833. Thiordxn-like_fd. 1 hit. SSF89942. Transl_elong_EF1_G_con. 1 hit. |
| PROSITE | PS50040. EF1G_C. 1 hit. PS50405. GST_CTER. 1 hit. PS50404. GST_NTER. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | EF1G_BOVIN | ||||||||
| Accession | Primary (citable) accession number: Q3SZV3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with