UniProt ID | PBS1_ARATH | |
---|---|---|
UniProt AC | Q9FE20 | |
Protein Name | Serine/threonine-protein kinase PBS1 {ECO:0000303|PubMed:11359614} | |
Gene Name | PBS1 {ECO:0000303|PubMed:11359614} | |
Organism | Arabidopsis thaliana (Mouse-ear cress). | |
Sequence Length | 456 | |
Subcellular Localization |
Cell membrane Lipid-anchor . |
|
Protein Description | Protein kinase required for plant defense mechanism mediated by the disease resistance (R) protein RPS5. In case of infection by Pseudomonas syringae, AvrPphB triggers RPS5-mediated defense mechanism via the cleavage of PBS1. Both kinase activity and cleavage by avrPphB are independently required to trigger the RPS5-mediated resistance. Contributes to PAMP-triggered immunity (PTI) signaling and defense responses downstream of FLS2.. | |
Protein Sequence | MGCFSCFDSSDDEKLNPVDESNHGQKKQSQPTVSNNISGLPSGGEKLSSKTNGGSKRELLLPRDGLGQIAAHTFAFRELAAATMNFHPDTFLGEGGFGRVYKGRLDSTGQVVAVKQLDRNGLQGNREFLVEVLMLSLLHHPNLVNLIGYCADGDQRLLVYEFMPLGSLEDHLHDLPPDKEALDWNMRMKIAAGAAKGLEFLHDKANPPVIYRDFKSSNILLDEGFHPKLSDFGLAKLGPTGDKSHVSTRVMGTYGYCAPEYAMTGQLTVKSDVYSFGVVFLELITGRKAIDSEMPHGEQNLVAWARPLFNDRRKFIKLADPRLKGRFPTRALYQALAVASMCIQEQAATRPLIADVVTALSYLANQAYDPSKDDSRRNRDERGARLITRNDDGGGSGSKFDLEGSEKEDSPRETARILNRDINRERAVAEAKMWGESLREKRRQSEQGTSESNSTG | |
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 |
---|---|---|---|---|---|
2 | Myristoylation | ------MGCFSCFDS ------CCCCCCCCC | 22.60 | 22046960 | |
3 | S-palmitoylation | -----MGCFSCFDSS -----CCCCCCCCCC | 1.88 | 24225654 | |
6 | S-palmitoylation | --MGCFSCFDSSDDE --CCCCCCCCCCCCC | 1.89 | 24225654 | |
9 | Phosphorylation | GCFSCFDSSDDEKLN CCCCCCCCCCCCCCC | 18.53 | 19880383 | |
10 | Phosphorylation | CFSCFDSSDDEKLNP CCCCCCCCCCCCCCC | 51.42 | 19880383 | |
21 | Phosphorylation | KLNPVDESNHGQKKQ CCCCCCCCCCCCCCC | 29.66 | 30291188 | |
29 | Phosphorylation | NHGQKKQSQPTVSNN CCCCCCCCCCCCCCC | 47.18 | 27545962 | |
32 | Phosphorylation | QKKQSQPTVSNNISG CCCCCCCCCCCCCCC | 29.00 | 27545962 | |
34 | Phosphorylation | KQSQPTVSNNISGLP CCCCCCCCCCCCCCC | 27.00 | 27545962 | |
38 | Phosphorylation | PTVSNNISGLPSGGE CCCCCCCCCCCCCCC | 36.08 | 27545962 | |
42 | Phosphorylation | NNISGLPSGGEKLSS CCCCCCCCCCCCCCC | 65.55 | 27545962 | |
160 | Phosphorylation | GDQRLLVYEFMPLGS CCCEEEEEEEEECCC | 11.92 | - | |
217 | Phosphorylation | IYRDFKSSNILLDEG EEECCCCCCEEECCC | 28.60 | - | |
244 | Phosphorylation | LGPTGDKSHVSTRVM CCCCCCCCCCCCEEC | 33.58 | 25561503 | |
247 | Phosphorylation | TGDKSHVSTRVMGTY CCCCCCCCCEECCCC | 12.69 | 30300945 | |
248 | Phosphorylation | GDKSHVSTRVMGTYG CCCCCCCCEECCCCC | 26.62 | - | |
253 | Phosphorylation | VSTRVMGTYGYCAPE CCCEECCCCCEECCC | 8.83 | 27679653 | |
261 | Phosphorylation | YGYCAPEYAMTGQLT CCEECCCCEECCCEE | 10.70 | - | |
396 | Phosphorylation | RNDDGGGSGSKFDLE ECCCCCCCCCCCCCC | 43.07 | 27545962 | |
398 | Phosphorylation | DDGGGSGSKFDLEGS CCCCCCCCCCCCCCC | 31.67 | 19880383 | |
405 | Phosphorylation | SKFDLEGSEKEDSPR CCCCCCCCCCCCCHH | 35.80 | 30291188 | |
410 | Phosphorylation | EGSEKEDSPRETARI CCCCCCCCHHHHHHH | 27.27 | 23111157 | |
437 | Phosphorylation | EAKMWGESLREKRRQ HHHHHHHHHHHHHHH | 28.87 | 25561503 |
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 PBS1_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 PBS1_ARATH !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
RPS5_ARATH | RPS5 | physical | 17277084 |
Kegg Drug | ||||||
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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-21, AND MASSSPECTROMETRY. |