A1ZAX1 (EIF3C_DROME) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 53.
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 3 subunit C Short name=eIF3c Alternative name(s): Eukaryotic translation initiation factor 3 subunit 8 | ||||
| Gene names |
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| Organism | Drosophila melanogaster (Fruit fly) [Reference proteome] | ||||
| Taxonomic identifier | 7227 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora › ![]() |
Protein attributes
| Sequence length | 910 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. HAMAP-Rule MF_03002 |
| Subunit structure | Component of the eukaryotic translation initiation factor 3 (eIF-3) complex. The eIF-3 complex interacts with pix. Ref.5 |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the eIF-3 subunit C family. Contains 1 PCI domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis |
| Cellular component | Cytoplasm |
| Molecular function | Initiation factor |
| PTM | Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Cellular_component | cytosol Inferred from sequence or structural similarity PubMed 10908586. Source: FlyBase eukaryotic translation initiation factor 3 complexInferred from sequence or structural similarity PubMed 10908586. Source: FlyBase |
| Molecular_function | translation initiation factor activity Inferred from sequence or structural similarity PubMed 10908586. Source: FlyBase |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 910 | 910 | Eukaryotic translation initiation factor 3 subunit C HAMAP-Rule MF_03002 | PRO_0000365388 | |||||
Regions | |||||||||
| Domain | 678 – 812 | 135 | PCI | ||||||
Amino acid modifications | |||||||||
| Modified residue | 34 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 165 | 1 | Phosphoserine Ref.7 | ||||||
| Modified residue | 176 | 1 | Phosphoserine Ref.7 | ||||||
| Modified residue | 185 | 1 | Phosphoserine Ref.7 | ||||||
Experimental info | |||||||||
| Sequence conflict | 293 | 1 | K → N in AAM52637. Ref.3 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. Venter J.C.Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley. |
| [2] | "Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. Lewis S.E.Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley. |
| [3] | "A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Head. |
| [4] | Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E. Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. |
| [5] | "The essential Drosophila ATP-binding cassette domain protein, pixie, binds the 40 S ribosome in an ATP-dependent manner and is required for translation initiation." Andersen D.S., Leevers S.J. J. Biol. Chem. 282:14752-14760(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PIX, ASSOCIATION WITH THE 40S RIBOSOME. |
| [6] | "An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells." Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A. Mol. Biosyst. 3:275-286(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, MASS SPECTROMETRY. |
| [7] | "Phosphoproteome analysis of Drosophila melanogaster embryos." Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P. J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165; SER-176 AND SER-185, MASS SPECTROMETRY. Tissue: Embryo. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE013599 Genomic DNA. Translation: AAF57818.1. AY122125 mRNA. Translation: AAM52637.1. BT044242 mRNA. Translation: ACH92307.1. |
| RefSeq | NP_611242.1. NM_137398.1. |
| UniGene | Dm.7296. |
3D structure databases | |
| ProteinModelPortal | A1ZAX1. |
| SMR | A1ZAX1. Positions 742-815. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | A1ZAX1. 10 interactions. |
| STRING | 7227.FBpp0086013. |
Proteomic databases | |
| PaxDb | A1ZAX1. |
| PRIDE | A1ZAX1. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblMetazoa | FBtr0086836; FBpp0086013; FBgn0034258. |
| GeneID | 37005. |
| KEGG | dme:Dmel_CG4954. |
| UCSC | CG4954-RA. d. melanogaster. |
Organism-specific databases | |
| CTD | 37005. |
| FlyBase | FBgn0034258. eIF3-S8. |
Phylogenomic databases | |
| eggNOG | NOG305883. |
| GeneTree | ENSGT00390000017900. |
| InParanoid | A1ZAX1. |
| KO | K03252. |
| OMA | ESHITNY. |
| OrthoDB | EOG4SQVBM. |
| PhylomeDB | A1ZAX1. |
Gene expression databases | |
| Bgee | A1ZAX1. |
Family and domain databases | |
| Gene3D | 1.10.10.10. 1 hit. |
| HAMAP | MF_03002. eIF3c. |
| InterPro | IPR008905. eIF3c_N. IPR000717. PCI_dom. IPR011991. WHTH_DNA-bd_dom. [Graphical view] |
| Pfam | PF05470. eIF-3c_N. 1 hit. PF01399. PCI. 1 hit. [Graphical view] |
| SMART | SM00088. PINT. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| ChiTaRS | eIF3-S8. drosophila. |
| GenomeRNAi | 37005. |
| NextBio | 801456. |
Entry information
| Entry name | EIF3C_DROME | ||||||||
| Accession | Primary (citable) accession number: A1ZAX1 Secondary accession number(s): Q8MR49 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Drosophila annotation project | ||||||||
Relevant documents
| Translation initiation factors List of translation initiation factor entries |
| Drosophila Drosophila: entries, gene names and cross-references to FlyBase |
| SIMILARITY comments Index of protein domains and families |

Clusters with
