| UniProt ID | RS33_ARATH | |
|---|---|---|
| UniProt AC | Q9FJA6 | |
| Protein Name | 40S ribosomal protein S3-3 | |
| Gene Name | RPS3C | |
| Organism | Arabidopsis thaliana (Mouse-ear cress). | |
| Sequence Length | 248 | |
| Subcellular Localization | ||
| Protein Description | ||
| Protein Sequence | MATQISKKRKFVADGVFYAELNEVLTRELAEDGYSGVEVRVTPMRTEIIIRATRTQNVLGEKGRRIRELTSLVQKRFKFPQDSVELYAEKVANRGLCAIAQAESLRYKLLGGLAVRRACYGVLRFVMESGAKGCEVIVSGKLRAARAKSMKFKDGYMVSSGQPTKEYIDAAVRHVLLRQGVLGLKVKIMLDWDPKGKQGPMTPLPDVVIIHTPKEDDVYIAPAQVVTQAAFVPEAPLTTTDYPAMPVA | |
| 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 |
|---|---|---|---|---|---|
| 26 | Phosphorylation | AELNEVLTRELAEDG HHHHHHHHHHHHHCC | 27.55 | 19880383 | |
| 62 | Ubiquitination | TQNVLGEKGRRIREL CCCCCCHHHHHHHHH | 56.79 | - | |
| 212 | Phosphorylation | PDVVIIHTPKEDDVY CCEEEEECCCCCCEE | 26.16 | 19376835 |
| 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 RS33_ARATH !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RS33_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 RS33_ARATH !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of RS33_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-212, AND MASSSPECTROMETRY. | |
| Ubiquitylation | |
| Reference | PubMed |
| "Tandem affinity purification and mass spectrometric analysis ofubiquitylated proteins in Arabidopsis."; Saracco S.A., Hansson M., Scalf M., Walker J.M., Smith L.M.,Vierstra R.D.; Plant J. 59:344-358(2009). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-62, AND IDENTIFICATION BYMASS SPECTROMETRY. | |