PBS1_ARATH - dbPTM
PBS1_ARATH - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Myristoylation------MGCFSCFDS
------CCCCCCCCC
22.6022046960
3S-palmitoylation-----MGCFSCFDSS
-----CCCCCCCCCC
1.8824225654
6S-palmitoylation--MGCFSCFDSSDDE
--CCCCCCCCCCCCC
1.8924225654
9PhosphorylationGCFSCFDSSDDEKLN
CCCCCCCCCCCCCCC
18.5319880383
10PhosphorylationCFSCFDSSDDEKLNP
CCCCCCCCCCCCCCC
51.4219880383
21PhosphorylationKLNPVDESNHGQKKQ
CCCCCCCCCCCCCCC
29.6630291188
29PhosphorylationNHGQKKQSQPTVSNN
CCCCCCCCCCCCCCC
47.1827545962
32PhosphorylationQKKQSQPTVSNNISG
CCCCCCCCCCCCCCC
29.0027545962
34PhosphorylationKQSQPTVSNNISGLP
CCCCCCCCCCCCCCC
27.0027545962
38PhosphorylationPTVSNNISGLPSGGE
CCCCCCCCCCCCCCC
36.0827545962
42PhosphorylationNNISGLPSGGEKLSS
CCCCCCCCCCCCCCC
65.5527545962
160PhosphorylationGDQRLLVYEFMPLGS
CCCEEEEEEEEECCC
11.92-
217PhosphorylationIYRDFKSSNILLDEG
EEECCCCCCEEECCC
28.60-
244PhosphorylationLGPTGDKSHVSTRVM
CCCCCCCCCCCCEEC
33.5825561503
247PhosphorylationTGDKSHVSTRVMGTY
CCCCCCCCCEECCCC
12.6930300945
248PhosphorylationGDKSHVSTRVMGTYG
CCCCCCCCEECCCCC
26.62-
253PhosphorylationVSTRVMGTYGYCAPE
CCCEECCCCCEECCC
8.8327679653
261PhosphorylationYGYCAPEYAMTGQLT
CCEECCCCEECCCEE
10.70-
396PhosphorylationRNDDGGGSGSKFDLE
ECCCCCCCCCCCCCC
43.0727545962
398PhosphorylationDDGGGSGSKFDLEGS
CCCCCCCCCCCCCCC
31.6719880383
405PhosphorylationSKFDLEGSEKEDSPR
CCCCCCCCCCCCCHH
35.8030291188
410PhosphorylationEGSEKEDSPRETARI
CCCCCCCCHHHHHHH
27.2723111157
437PhosphorylationEAKMWGESLREKRRQ
HHHHHHHHHHHHHHH
28.8725561503

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
3CPalmitoylation

22046960
6CPalmitoylation

22046960

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RPS5_ARATHRPS5physical
17277084

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PBS1_ARATH

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

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