| UniProt ID | IF5A2_ARATH | |
|---|---|---|
| UniProt AC | Q93VP3 | |
| Protein Name | Eukaryotic translation initiation factor 5A-2 | |
| Gene Name | ELF5A-2 | |
| Organism | Arabidopsis thaliana (Mouse-ear cress). | |
| Sequence Length | 159 | |
| Subcellular Localization | Cytoplasm . Nucleus . | |
| Protein Description | The precise role of eIF-5A in protein biosynthesis is not known but it may function as a bimodular protein capable of binding to both RNA and proteins. Regulates cytokinin-mediated root protoxylem specification and represses secifically the expression of AHP6. Regulates the induction of programmed cell death caused by infection with virulent pathogen.. | |
| Protein Sequence | MSDDEHHFEASESGASKTYPQSAGNIRKGGHIVIKNRPCKVVEVSTSKTGKHGHAKCHFVAIDIFTAKKLEDIVPSSHNCDVPHVNRVDYQLIDITEDGFVSLLTDSGGTKDDLKLPTDDGLTAQMRLGFDEGKDIVVSVMSSMGEEQICAVKEVGGGK | |
| 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 |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MSDDEHHFE ------CCCCCCCEE | 54.49 | 30291188 | |
| 11 | Phosphorylation | DEHHFEASESGASKT CCCCEECCCCCCCCC | 25.71 | 23172892 | |
| 13 | Phosphorylation | HHFEASESGASKTYP CCEECCCCCCCCCCC | 36.84 | 25561503 | |
| 16 | Phosphorylation | EASESGASKTYPQSA ECCCCCCCCCCCCCC | 29.11 | 25561503 | |
| 51 | Hypusine | VSTSKTGKHGHAKCH EECCCCCCCCCCEEE | 52.20 | - | |
| 51 | Other | VSTSKTGKHGHAKCH EECCCCCCCCCCEEE | 52.20 | - | |
| 76 | Phosphorylation | KLEDIVPSSHNCDVP HHHHCCCCCCCCCCC | 33.08 | 19880383 | |
| 77 | Phosphorylation | LEDIVPSSHNCDVPH HHHCCCCCCCCCCCC | 16.79 | 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 IF5A2_ARATH !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of IF5A2_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 IF5A2_ARATH !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| AHP1_ARATH | AHP1 | physical | 24163315 | |
| AHK4_ARATH | WOL | physical | 24163315 |
| 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 SER-2, AND MASSSPECTROMETRY. | |