Q10119 (EF1A2_SCHPO) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 108.
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-alpha-B/C Short name=EF-1-alpha-B/C | |||||||||||||
| Gene names |
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| Organism | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome] | |||||||||||||
| Taxonomic identifier | 284812 [NCBI] | |||||||||||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › ![]() |
Protein attributes
| Sequence length | 460 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. |
| Subcellular location | |
| Sequence similarities | Belongs to the GTP-binding elongation factor family. EF-Tu/EF-1A subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | GTP-binding Nucleotide-binding |
| Molecular function | Elongation factor |
| PTM | Phosphoprotein |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | GTP catabolic process Inferred from electronic annotation. Source: GOC cytoplasmic translational elongationNon-traceable author statement. Source: PomBase |
| Cellular_component | cytosol Inferred from direct assay PubMed 16823372. Source: PomBase eukaryotic translation elongation factor 1 complexInferred from sequence orthology. Source: PomBase nucleusInferred from direct assay PubMed 16823372. Source: PomBase |
| Molecular_function | GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activityInferred from electronic annotation. Source: InterPro translation elongation factor activityInferred from sequence orthology. Source: PomBase |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 460 | 460 | Elongation factor 1-alpha-B/C | PRO_0000090969 | |||||
Regions | |||||||||
| Nucleotide binding | 14 – 21 | 8 | GTP By similarity | ||||||
| Nucleotide binding | 91 – 95 | 5 | GTP By similarity | ||||||
| Nucleotide binding | 153 – 156 | 4 | GTP By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 23 | 1 | Phosphothreonine Ref.6 | ||||||
| Modified residue | 24 | 1 | Phosphothreonine Ref.6 | ||||||
| Modified residue | 158 | 1 | Phosphothreonine Ref.6 | ||||||
| Modified residue | 289 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 296 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 314 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 388 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 394 | 1 | Phosphoserine Ref.6 | ||||||
Experimental info | |||||||||
| Sequence conflict | 21 | 1 | S → F in BAA11571. Ref.1 | ||||||
| Sequence conflict | 139 | 1 | L → R in BAA11571. Ref.1 | ||||||
| Sequence conflict | 139 | 1 | L → V in BAA19867. Ref.2 | ||||||
| Sequence conflict | 388 | 1 | S → A in AAP86554. Ref.4 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Comprehensive cloning of Schizosaccharomyces pombe genes encoding translation elongation factors." Mita K., Morimyo M., Ito K., Sugaya K., Ebihara K., Hongo E., Higashi T., Hirayama Y., Nakamura Y. Gene 187:259-266(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (TEF1B AND TEF1C). Strain: 972 / ATCC 24843. |
| [2] | "Identification of open reading frames in Schizosaccharomyces pombe cDNAs." Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H. DNA Res. 4:363-369(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: PR745. |
| [3] | "The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. Nurse P.Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (TEF1B AND TEF1C). Strain: 972 / ATCC 24843. |
| [4] | "Phylogenetic relationships among yeasts of the 'Saccharomyces complex' determined from multigene sequence analyses." Kurtzman C.P., Robnett C.J. FEMS Yeast Res. 3:417-432(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-397. Strain: NRRL Y-12796. |
| [5] | "Peptide elongation factor 1 from yeasts: purification and biochemical characterization of peptide elongation factors 1alpha and 1beta(gamma) from Saccharomyces carlsbergensis and Schizosaccharomyces pombe." Miyazaki M., Uritani M., Fujimura K., Yamakatsu H., Kageyama T., Takahashi K. J. Biochem. 103:508-521(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 64-94. |
| [6] | "Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-23; THR-24; THR-158; SER-289; SER-296; SER-314; SER-388 AND SER-394, MASS SPECTROMETRY. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | D82572 mRNA. Translation: BAA11570.1. D82573 mRNA. Translation: BAA11571.1. D89112 mRNA. Translation: BAA19867.1. CU329670 Genomic DNA. Translation: CAA16984.1. CU329671 Genomic DNA. Translation: CAB46708.1. AF402093 Genomic DNA. Translation: AAP86554.1. |
| PIR | B41453. T38230. T42089. |
| RefSeq | NP_594440.1. NM_001019869.2. NP_595255.1. NM_001021161.2. |
3D structure databases | |
| ProteinModelPortal | Q10119. |
| SMR | Q10119. Positions 2-441. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q10119. 1 interaction. |
| STRING | 4896.SPBC839.15c-1. |
Proteomic databases | |
| PRIDE | Q10119. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblFungi | SPAC23A1.10.1; SPAC23A1.10.1:pep; SPAC23A1.10. SPBC839.15c.1; SPBC839.15c.1:pep; SPBC839.15c. |
| GeneID | 2539917. 2541984. |
| KEGG | spo:SPAC23A1.10. spo:SPBC839.15c. |
Organism-specific databases | |
| PomBase | SPAC23A1.10. SPBC839.15c. |
Phylogenomic databases | |
| HOGENOM | HOG000229291. |
| KO | K03231. |
| OMA | LEPSANC. |
| OrthoDB | EOG4BS0V0. |
Family and domain databases | |
| InterPro | IPR000795. EF_GTP-bd_dom. IPR009001. Transl_elong_EF1A/Init_IF2_C. IPR004539. Transl_elong_EF1A_euk/arc. IPR004161. Transl_elong_EFTu/EF1A_2. IPR004160. Transl_elong_EFTu/EF1A_C. IPR009000. Transl_elong_init/rib_B-barrel. [Graphical view] |
| Pfam | PF00009. GTP_EFTU. 1 hit. PF03144. GTP_EFTU_D2. 1 hit. PF03143. GTP_EFTU_D3. 1 hit. [Graphical view] |
| PRINTS | PR00315. ELONGATNFCT. |
| SUPFAM | SSF50465. Elong_init_C. 1 hit. SSF50447. Translat_factor. 1 hit. |
| TIGRFAMs | TIGR00483. EF-1_alpha. 1 hit. |
| PROSITE | PS00301. EFACTOR_GTP. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 20801060. |
Entry information
| Entry name | EF1A2_SCHPO | ||||||||
| Accession | Primary (citable) accession number: Q10119 Secondary accession number(s): P78764 Q7Z8V5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| Schizosaccharomyces pombe Schizosaccharomyces pombe: entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with
