| UniProt ID | EIF3D_ARATH | |
|---|---|---|
| UniProt AC | P56820 | |
| Protein Name | Eukaryotic translation initiation factor 3 subunit D {ECO:0000255|HAMAP-Rule:MF_03003} | |
| Gene Name | TIF3D1 | |
| Organism | Arabidopsis thaliana (Mouse-ear cress). | |
| Sequence Length | 591 | |
| Subcellular Localization | Cytoplasm . | |
| Protein Description | mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. In the eIF-3 complex, eif3d specifically recognizes and binds the 7-methylguanosine cap of a subset of mRNAs.. | |
| Protein Sequence | MVTEAFEFVAVPFNSDGWGPPDASDVSSSASPTSVAAANLLPNVPFASFSRSDKLGRVADWTRNLSNPSARPNTGSKSDPSAVFDFSAFAIDEGFGLASSGGNPDEDAAFRLVDGKPPPRPKFGPKWRFNPHHNRNQLPQRRDEEVEAKKRDAEKERARRDRLYNNNRNNIHHQRREAAAFKSSVDIQPEWNMLEQIPFSTFSKLSYTVQEPEDLLLCGGLEYYNRLFDRITPKNERRLERFKNRNFFKVTTSDDPVIRRLAKEDKATVFATDAILAALMCAPRSVYSWDIVIQRVGNKLFFDKRDGSQLDLLSVHETSQEPLPESKDDINSAHSLGVEAAYINQNFSQQVLVRDGKKETFDEANPFANEGEEIASVAYRYRRWKLDDNMHLVARCELQSVADLNNQRSFLTLNALNEFDPKYSGVDWRQKLETQRGAVLATELKNNGNKLAKWTAQALLANADMMKIGFVSRVHPRDHFNHVILSVLGYKPKDFAGQINLNTSNMWGIVKSIVDLCMKLSEGKYVLVKDPSKPQVRIYEVPPDAFENDYVEEPLPEDEQVQPTEENTEGAEASVAATKETEEKKADDAQA | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 66 | Phosphorylation | ADWTRNLSNPSARPN HHHHHCCCCCCCCCC | 50.69 | 19376835 | |
| 69 | Phosphorylation | TRNLSNPSARPNTGS HHCCCCCCCCCCCCC | 40.95 | 23776212 | |
| 74 | Phosphorylation | NPSARPNTGSKSDPS CCCCCCCCCCCCCHH | 45.58 | 30291188 | |
| 76 | Phosphorylation | SARPNTGSKSDPSAV CCCCCCCCCCCHHHE | 27.26 | 23776212 | |
| 412 | Phosphorylation | NNQRSFLTLNALNEF CCCCCEEHHHHHCCC | 18.89 | 19880383 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of EIF3D_ARATH !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of EIF3D_ARATH !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of EIF3D_ARATH !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of EIF3D_ARATH !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks."; Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.; Plant Physiol. 150:889-903(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-74, AND MASSSPECTROMETRY. | |