dbPTM

PDPK1_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PDPK1_ARATH
UniProt AC	Q9XF67
Protein Name	3-phosphoinositide-dependent protein kinase 1
Gene Name	PDPK1
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	491
Subcellular Localization	Cytoplasm. Membrane Peripheral membrane protein. Membrane-associated after cell stimulation..
Protein Description	May couple lipid signals to the activation-loop phosphorylation of several protein kinases of the so-called AGC kinase family. Interacts via its pleckstrin homology domain with phosphatidic acid, PtdIns3P and PtdIns(3,4)P2 and to a lesser extent with PtdIns(4,5)P2 and PtdIns4P. May play a general role in signaling processes controlling the pathogen/stress response, polar auxin transport and development. Transphosphorylates the AGC protein kinases OXI1/AGC2-1, PK1/S6K1, PK19/S6K2 and PID resulting in their activation..
Protein Sequence	MLAMEKEFDSKLVLQGNSSNGANVSRSKSFSFKAPQENFTSHDFEFGKIYGVGSYSKVVRAKKKETGTVYALKIMDKKFITKENKTAYVKLERIVLDQLEHPGIIKLYFTFQDTSSLYMALESCEGGELFDQITRKGRLSEDEARFYTAEVVDALEYIHSMGLIHRDIKPENLLLTSDGHIKIADFGSVKPMQDSQITVLPNAASDDKACTFVGTAAYVPPEVLNSSPATFGNDLWALGCTLYQMLSGTSPFKDASEWLIFQRIIARDIKFPNHFSEAARDLIDRLLDTEPSRRPGAGSEGYVALKRHPFFNGVDWKNLRSQTPPKLAPDPASQTASPERDDTHGSPWNLTHIGDSLATQNEGHSAPPTSSESSGSITRLASIDSFDSRWQQFLEPGESVLMISAVKKLQKITSKKVQLILTNKPKLIYVDPSKLVVKGNIIWSDNSNDLNVVVTSPSHFKICTPKKVLSFEDAKQRASVWKKAIETLQNR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
18	Phosphorylation	KLVLQGNSSNGANVS EEEEECCCCCCCCCC	31.82	19880383
19	Phosphorylation	LVLQGNSSNGANVSR EEEECCCCCCCCCCC	43.19	19880383
27	Phosphorylation	NGANVSRSKSFSFKA CCCCCCCCCCCCEEC	25.75	23776212
29	Phosphorylation	ANVSRSKSFSFKAPQ CCCCCCCCCCEECCC	27.63	23776212
31	Phosphorylation	VSRSKSFSFKAPQEN CCCCCCCCEECCCCC	32.69	23776212
54	Phosphorylation	GKIYGVGSYSKVVRA CEEEEECCCCEEEEE	24.67	19880383
177	Phosphorylation	PENLLLTSDGHIKIA HHHEEECCCCCEEEC	41.38	16125835
211	Phosphorylation	ASDDKACTFVGTAAY CCCCCCCCEEECEEE	26.64	16125835
276	Phosphorylation	IKFPNHFSEAARDLI CCCCCHHHHHHHHHH	20.83	16125835
333	Phosphorylation	KLAPDPASQTASPER CCCCCCCCCCCCCCC	33.19	23776212
335	Phosphorylation	APDPASQTASPERDD CCCCCCCCCCCCCCC	26.97	23776212
337	Phosphorylation	DPASQTASPERDDTH CCCCCCCCCCCCCCC	30.59	23776212
382	Phosphorylation	GSITRLASIDSFDSR CCCEEEEECCCCHHH	31.36	30291188
385	Phosphorylation	TRLASIDSFDSRWQQ EEEEECCCCHHHHHH	29.32	23776212
388	Phosphorylation	ASIDSFDSRWQQFLE EECCCCHHHHHHHCC	33.15	23776212

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
211	T	Phosphorylation	Kinase	PDK1	Q9XF67	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
211	T	Phosphorylation	16125835
PDK1 itself can autophosphorylate Thr-211, leading to its own activation.
211	T	Phosphorylation	16125835
Phosphorylation on Thr-211 in the activation loop is required for full activity.

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 PDPK1_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
OXI1_ARATH	AGC2-1	physical	17040918
OXI1_ARATH	AGC2-1	physical	14749726
PGP2_ARATH	PGLP2	physical	16973627
D6KL3_ARATH	ATPK7	physical	16973627
D6KL1_ARATH	D6PKL1	physical	16973627
AGC17_ARATH	AGC1.7	physical	16973627
AGC15_ARATH	AGC1.5	physical	16973627
PID2_ARATH	PID2	physical	16973627

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PDPK1_ARATH

Related Literatures of Post-Translational Modification

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-337, AND IDENTIFICATIONBY MASS SPECTROMETRY.	19376835 [Abstract]
"Phosphoproteomic analysis of nuclei-enriched fractions fromArabidopsis thaliana."; Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,Andreasson E., Rathjen J.P., Peck S.C.; J. Proteomics 72:439-451(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-382, AND IDENTIFICATIONBY MASS SPECTROMETRY.	19245862 [Abstract]
"Arabidopsis PDK1: identification of sites important for activity anddownstream phosphorylation of S6 kinase."; Otterhag L., Gustavsson N., Alsterfjord M., Pical C., Lehrach H.,Gobom J., Sommarin M.; Biochimie 88:11-21(2006). Cited for: PHOSPHORYLATION AT SER-177; SER-276 AND SER-382, IDENTIFICATION BYMASS SPECTROMETRY, AND MUTAGENESIS OF ASP-167; THR-176; SER-177;THR-211; SER-276 AND SER-382.	16125835 [Abstract]