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 | ||
* 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. |