UniProt ID | RS32_ARATH | |
---|---|---|
UniProt AC | Q9M339 | |
Protein Name | 40S ribosomal protein S3-2 | |
Gene Name | RPS3B | |
Organism | Arabidopsis thaliana (Mouse-ear cress). | |
Sequence Length | 249 | |
Subcellular Localization | ||
Protein Description | ||
Protein Sequence | MTTQISKKRKFVADGVFYAELNEVLTRELAEDGYSGVEVRVTPMRTEIIIRATRTQNVLGEKGRRIRELTSLVQKRFKFPVDSVELYAEKVNNRGLCAIAQAESLRYKLLGGLAVRRACYGVLRFVMESGAKGCEVIVSGKLRAARAKSMKFKDGYMVSSGQPTKEYIDSAVRHVLLRQGVLGIKVKVMLDWDPKGISGPKTPLPDVVIIHSPKEEEAIYAPAQVAAPAALVADAPLTAVDYPAMIPVA | |
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 |
---|---|---|---|---|---|
26 | Phosphorylation | AELNEVLTRELAEDG HHHHHHHHHHHHHCC | 27.55 | 19880383 | |
62 | Ubiquitination | TQNVLGEKGRRIREL CCCCCCHHHHHHHHH | 56.79 | - | |
134 | S-nitrosylation | MESGAKGCEVIVSGK HHCCCCCCEEEECCC | 3.58 | 22115780 | |
212 | Phosphorylation | PDVVIIHSPKEEEAI CCEEEECCCCHHHCC | 27.53 | 30291188 | |
214 | Sumoylation | VVIIHSPKEEEAIYA EEEECCCCHHHCCCC | 79.40 | - |
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 RS32_ARATH !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RS32_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 RS32_ARATH !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
SUMO3_ARATH | SUMO3 | physical | 20855607 |
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-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. |