Q05D44 (IF2P_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
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: Eukaryotic translation initiation factor 5B Short name=eIF-5B Alternative name(s): Translation initiation factor IF-2 | ||||
| Gene names |
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| Organism | Mus musculus (Mouse) [Reference proteome] | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus![]() |
Protein attributes
| Sequence length | 1216 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Function in general translation initiation by promoting the binding of the formylmethionine-tRNA to ribosomes. Seems to function along with eIF-2 By similarity. |
| Subunit structure | Interacts with ANXA5 in a calcium and phospholipid-dependent manner By similarity. |
| Subcellular location | |
| Sequence similarities | Belongs to the IF-2 family. |
| Sequence caution | The sequence AAH18347.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence. The sequence AAH37150.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence. The sequence AAH40746.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence. The sequence AAH60288.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | GTP-binding Nucleotide-binding |
| Molecular function | Initiation factor |
| PTM | Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | GTP catabolic process Inferred from electronic annotation. Source: GOC |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activityInferred from electronic annotation. Source: InterPro translation initiation factor activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1216 | 1216 | Eukaryotic translation initiation factor 5B | PRO_0000354071 | |||||
Regions | |||||||||
| Nucleotide binding | 634 – 641 | 8 | GTP By similarity | ||||||
| Compositional bias | 39 – 452 | 414 | Lys-rich | ||||||
| Compositional bias | 235 – 561 | 327 | Glu-rich | ||||||
Amino acid modifications | |||||||||
| Modified residue | 108 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 114 | 1 | Phosphoserine Ref.6 Ref.8 Ref.10 Ref.12 | ||||||
| Modified residue | 137 | 1 | Phosphoserine Ref.8 Ref.9 Ref.10 Ref.12 | ||||||
| Modified residue | 139 | 1 | Phosphoserine Ref.8 Ref.12 | ||||||
| Modified residue | 165 | 1 | Phosphoserine Ref.10 Ref.11 | ||||||
| Modified residue | 172 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 179 | 1 | Phosphoserine Ref.7 | ||||||
| Modified residue | 183 | 1 | Phosphoserine Ref.7 Ref.10 | ||||||
| Modified residue | 184 | 1 | Phosphoserine Ref.7 Ref.10 | ||||||
| Modified residue | 187 | 1 | Phosphoserine Ref.7 Ref.8 Ref.10 | ||||||
| Modified residue | 191 | 1 | Phosphoserine Ref.7 Ref.8 Ref.10 | ||||||
| Modified residue | 215 | 1 | Phosphoserine Ref.5 Ref.6 Ref.8 Ref.11 Ref.12 | ||||||
| Modified residue | 300 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 497 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 556 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 584 | 1 | Phosphoserine Ref.7 | ||||||
| Modified residue | 585 | 1 | Phosphoserine Ref.7 | ||||||
| Modified residue | 587 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 591 | 1 | Phosphoserine Ref.7 | ||||||
Experimental info | |||||||||
| Sequence conflict | 121 | 1 | D → N in BAE26259. Ref.2 | ||||||
| Sequence conflict | 188 | 1 | G → C in BAE26259. Ref.2 | ||||||
| Sequence conflict | 254 | 1 | M → L in BAE26259. Ref.2 | ||||||
| Sequence conflict | 302 | 1 | A → V in BAE26259. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. Ponting C.P.PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J. |
| [2] | "The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y.Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-771. Strain: C57BL/6J. Tissue: Corpora quadrigemina and Mammary gland. |
| [3] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-402. Strain: FVB/N. Tissue: Limb and Mammary tumor. |
| [4] | "Exp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm." Bohnsack M.T., Regener K., Schwappach B., Saffrich R., Paraskeva E., Hartmann E., Goerlich D. EMBO J. 21:6205-6215(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION. |
| [5] | "Phosphoproteomic analysis of the developing mouse brain." Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P. Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, MASS SPECTROMETRY. Tissue: Embryonic brain. |
| [6] | "Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND SER-215, MASS SPECTROMETRY. Tissue: Liver. |
| [7] | "A differential phosphoproteomic analysis of retinoic acid-treated P19 cells." Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D. J. Proteome Res. 6:3174-3186(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179; SER-183; SER-184; SER-187; SER-191; SER-584; SER-585 AND SER-591, MASS SPECTROMETRY. Tissue: Teratocarcinoma. |
| [8] | "Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-137; SER-139; SER-187; SER-191 AND SER-215, MASS SPECTROMETRY. Tissue: Liver. |
| [9] | "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis." Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H. J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, MASS SPECTROMETRY. Tissue: Liver. |
| [10] | "Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-137; SER-165; SER-183; SER-184; SER-187 AND SER-191, MASS SPECTROMETRY. Tissue: Melanoma. |
| [11] | "The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165 AND SER-215, MASS SPECTROMETRY. Tissue: Macrophage. |
| [12] | "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-137; SER-139 AND SER-215, MASS SPECTROMETRY. Tissue: Embryonic fibroblast. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AC114583 Genomic DNA. No translation available. AK145146 mRNA. Translation: BAE26259.1. AK145732 mRNA. Translation: BAE26614.1. AK163527 mRNA. Translation: BAE37384.1. BC018347 mRNA. Translation: AAH18347.1. Sequence problems. BC037150 mRNA. Translation: AAH37150.1. Sequence problems. BC040746 mRNA. Translation: AAH40746.1. Sequence problems. BC060288 mRNA. Translation: AAH60288.1. Sequence problems. |
| IPI | IPI00756424. |
| RefSeq | NP_938045.2. NM_198303.2. |
| UniGene | Mm.260943. |
3D structure databases | |
| ProteinModelPortal | Q05D44. |
| SMR | Q05D44. Positions 624-1211. |
| ModBase | Search... |
PTM databases | |
| PhosphoSite | Q05D44. |
Proteomic databases | |
| PaxDb | Q05D44. |
| PRIDE | Q05D44. |
Protocols and materials databases | |
| DNASU | 226982. |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000027252; ENSMUSP00000027252; ENSMUSG00000026083. |
| GeneID | 226982. |
| KEGG | mmu:226982. |
| UCSC | uc007aso.1. mouse. |
Organism-specific databases | |
| CTD | 9669. |
| MGI | MGI:2441772. Eif5b. |
Phylogenomic databases | |
| eggNOG | COG0532. |
| GeneTree | ENSGT00690000102102. |
| HOVERGEN | HBG019036. |
| InParanoid | Q8CFF4. |
| KO | K03243. |
| OMA | VMGVIVE. |
| OrthoDB | EOG44BB1J. |
Gene expression databases | |
| ArrayExpress | Q05D44. |
| Bgee | Q05D44. |
| Genevestigator | Q05D44. |
Family and domain databases | |
| Gene3D | 3.40.50.10050. 1 hit. |
| InterPro | IPR000795. EF_GTP-bd_dom. IPR005225. Small_GTP-bd_dom. IPR015760. TIF_IF2. IPR023115. TIF_IF2_dom3. IPR004161. Transl_elong_EFTu/EF1A_2. IPR009000. Transl_elong_init/rib_B-barrel. [Graphical view] |
| PANTHER | PTHR23115:SF41. PTHR23115:SF41. 1 hit. |
| Pfam | PF00009. GTP_EFTU. 1 hit. PF03144. GTP_EFTU_D2. 1 hit. PF11987. IF-2. 1 hit. [Graphical view] |
| PRINTS | PR00315. ELONGATNFCT. |
| SUPFAM | SSF52156. TIF_IF2_dom3. 1 hit. SSF50447. Translat_factor. 1 hit. |
| TIGRFAMs | TIGR00231. small_GTP. 1 hit. |
| ProtoNet | Search... |
Other | |
| ChiTaRS | EIF5B. mouse. |
| NextBio | 378430. |
| SOURCE | Search... |
Entry information
| Entry name | IF2P_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q05D44 Secondary accession number(s): Q3SYI4 Q8CGD6 | ||||||||
| 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 |
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with
