dbPTM

PDPK1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PDPK1_HUMAN
UniProt AC	O15530
Protein Name	3-phosphoinositide-dependent protein kinase 1
Gene Name	PDPK1
Organism	Homo sapiens (Human).
Sequence Length	556
Subcellular Localization	Cytoplasm. Nucleus. Cell membrane Peripheral membrane protein. Cell junction, focal adhesion. Tyrosine phosphorylation seems to occur only at the cell membrane. Translocates to the cell membrane following insulin stimulation by a mechanism that invo
Protein Description	Serine/threonine kinase which acts as a master kinase, phosphorylating and activating a subgroup of the AGC family of protein kinases. Its targets include: protein kinase B (PKB/AKT1, PKB/AKT2, PKB/AKT3), p70 ribosomal protein S6 kinase (RPS6KB1), p90 ribosomal protein S6 kinase (RPS6KA1, RPS6KA2 and RPS6KA3), cyclic AMP-dependent protein kinase (PRKACA), protein kinase C (PRKCD and PRKCZ), serum and glucocorticoid-inducible kinase (SGK1, SGK2 and SGK3), p21-activated kinase-1 (PAK1), protein kinase PKN (PKN1 and PKN2). Plays a central role in the transduction of signals from insulin by providing the activating phosphorylation to PKB/AKT1, thus propagating the signal to downstream targets controlling cell proliferation and survival, as well as glucose and amino acid uptake and storage. Negatively regulates the TGF-beta-induced signaling by: modulating the association of SMAD3 and SMAD7 with TGF-beta receptor, phosphorylating SMAD2, SMAD3, SMAD4 and SMAD7, preventing the nuclear translocation of SMAD3 and SMAD4 and the translocation of SMAD7 from the nucleus to the cytoplasm in response to TGF-beta. Activates PPARG transcriptional activity and promotes adipocyte differentiation. Activates the NF-kappa-B pathway via phosphorylation of IKKB. The tyrosine phosphorylated form is crucial for the regulation of focal adhesions by angiotensin II. Controls proliferation, survival, and growth of developing pancreatic cells. Participates in the regulation of Ca(2+) entry and Ca(2+)-activated K(+) channels of mast cells. Essential for the motility of vascular endothelial cells (ECs) and is involved in the regulation of their chemotaxis. Plays a critical role in cardiac homeostasis by serving as a dual effector for cell survival and beta-adrenergic response. Plays an important role during thymocyte development by regulating the expression of key nutrient receptors on the surface of pre-T cells and mediating Notch-induced cell growth and proliferative responses. Provides negative feedback inhibition to toll-like receptor-mediated NF-kappa-B activation in macrophages. Isoform 3 is catalytically inactive..
Protein Sequence	MARTTSQLYDAVPIQSSVVLCSCPSPSMVRTQTESSTPPGIPGGSRQGPAMDGTAAEPRPGAGSLQHAQPPPQPRKKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKILEKRHIIKENKVPYVTRERDVMSRLDHPFFVKLYFTFQDDEKLYFGLSYAKNGELLKYIRKIGSFDETCTRFYTAEIVSALEYLHGKGIIHRDLKPENILLNEDMHIQITDFGTAKVLSPESKQARANSFVGTAQYVSPELLTEKSACKSSDLWALGCIIYQLVAGLPPFRAGNEYLIFQKIIKLEYDFPEKFFPKARDLVEKLLVLDATKRLGCEEMEGYGPLKAHPFFESVTWENLHQQTPPKLTAYLPAMSEDDEDCYGNYDNLLSQFGCMQVSSSSSSHSLSASDTGLPQRSGSNIEQYIHDLDSNSFELDLQFSEDEKRLLLEKQAGGNPWHQFVENNLILKMGPVDKRKGLFARRRQLLLTEGPHLYYVDPVNKVLKGEIPWSQELRPEAKNFKTFFVHTPNRTYYLMDPSGNAHKWCRKIQEVWRQRYQSHPDAAVQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MARTTSQLYDA ----CCCCHHHHHHC	22.66	21945579
5	Phosphorylation	---MARTTSQLYDAV ---CCCCHHHHHHCC	14.66	21945579
6	Phosphorylation	--MARTTSQLYDAVP --CCCCHHHHHHCCC	19.99	21945579
9	Phosphorylation	ARTTSQLYDAVPIQS CCCHHHHHHCCCCCC	8.33	21945579
16	Phosphorylation	YDAVPIQSSVVLCSC HHCCCCCCEEEEEEC	26.31	21945579
17	Phosphorylation	DAVPIQSSVVLCSCP HCCCCCCEEEEEECC	10.40	21945579
22	Phosphorylation	QSSVVLCSCPSPSMV CCEEEEEECCCHHHE	25.54	21945579
25	Phosphorylation	VVLCSCPSPSMVRTQ EEEEECCCHHHEEEE	33.65	21945579
27	Phosphorylation	LCSCPSPSMVRTQTE EEECCCHHHEEEECC	33.96	21945579
31	Phosphorylation	PSPSMVRTQTESSTP CCHHHEEEECCCCCC	28.56	29396449
33	Phosphorylation	PSMVRTQTESSTPPG HHHEEEECCCCCCCC	36.90	23911959
35	Phosphorylation	MVRTQTESSTPPGIP HEEEECCCCCCCCCC	42.79	25159151
36	Phosphorylation	VRTQTESSTPPGIPG EEEECCCCCCCCCCC	38.41	25159151
37	Phosphorylation	RTQTESSTPPGIPGG EEECCCCCCCCCCCC	42.66	25159151
45	Phosphorylation	PPGIPGGSRQGPAMD CCCCCCCCCCCCCCC	27.61	29396449
54	Phosphorylation	QGPAMDGTAAEPRPG CCCCCCCCCCCCCCC	20.59	28348404
64	Phosphorylation	EPRPGAGSLQHAQPP CCCCCCCCCCCCCCC	25.07	28348404
83	Ubiquitination	KKRPEDFKFGKILGE CCCCCCCCCCCCCCC	66.58	29967540
88	Ubiquitination	DFKFGKILGEGSFST CCCCCCCCCCCCCHH	6.10	21890473
92	Phosphorylation	GKILGEGSFSTVVLA CCCCCCCCCHHHHHH	16.24	28857561
92	Ubiquitination	GKILGEGSFSTVVLA CCCCCCCCCHHHHHH	16.24	22817900
94	Phosphorylation	ILGEGSFSTVVLARE CCCCCCCHHHHHHHH	23.22	20071362
95	Phosphorylation	LGEGSFSTVVLAREL CCCCCCHHHHHHHHH	16.78	28122231
111	Ubiquitination	TSREYAIKILEKRHI HCHHHHHHHHHHHHC	32.82	29967540
114 (in isoform 4)	Phosphorylation	-	52.06	19664994
118 (in isoform 4)	Phosphorylation	-	5.82	17081983
123	Ubiquitination	RHIIKENKVPYVTRE HHCHHCCCCCEEECC	45.75	29967540
126	Phosphorylation	IKENKVPYVTRERDV HHCCCCCEEECCCHH	19.90	22817900
130	Ubiquitination	KVPYVTRERDVMSRL CCCEEECCCHHHHHC	43.82	32015554
148	Phosphorylation	FFVKLYFTFQDDEKL EEEEEEEEECCCCEE	13.56	19835603
156	Phosphorylation	FQDDEKLYFGLSYAK ECCCCEEEEEEEECC	13.48	25884760
160	Phosphorylation	EKLYFGLSYAKNGEL CEEEEEEEECCCCHH	24.35	19835603
161	Phosphorylation	KLYFGLSYAKNGELL EEEEEEEECCCCHHH	27.00	19835603
170	Phosphorylation	KNGELLKYIRKIGSF CCCHHHHHHHHHCCC	13.11	20068231
176	Phosphorylation	KYIRKIGSFDETCTR HHHHHHCCCCCHHHH	32.76	20068231
177	Ubiquitination	YIRKIGSFDETCTRF HHHHHCCCCCHHHHH	9.20	21890473
177	Acetylation	YIRKIGSFDETCTRF HHHHHCCCCCHHHHH	9.20	19608861
177	Ubiquitination	YIRKIGSFDETCTRF HHHHHCCCCCHHHHH	9.20	21890473
180	Phosphorylation	KIGSFDETCTRFYTA HHCCCCCHHHHHHHH	22.48	20068231
181	Ubiquitination	IGSFDETCTRFYTAE HCCCCCHHHHHHHHH	2.12	22817900
182	Phosphorylation	GSFDETCTRFYTAEI CCCCCHHHHHHHHHH	31.09	20068231
188	Ubiquitination	CTRFYTAEIVSALEY HHHHHHHHHHHHHHH	35.80	29967540
191	Phosphorylation	FYTAEIVSALEYLHG HHHHHHHHHHHHHCC	32.56	20068231
195	Phosphorylation	EIVSALEYLHGKGII HHHHHHHHHCCCCCC	12.59	20068231
196	Ubiquitination	IVSALEYLHGKGIIH HHHHHHHHCCCCCCC	2.91	29967540
210	Ubiquitination	HRDLKPENILLNEDM CCCCCHHHEEECCCC	38.44	29967540
211	Ubiquitination	RDLKPENILLNEDMH CCCCHHHEEECCCCE	4.40	21890473
215	Ubiquitination	PENILLNEDMHIQIT HHHEEECCCCEEEEC	57.59	22817900
231	Phosphorylation	FGTAKVLSPESKQAR CCCEEECCHHHHHHH	29.61	27067055
234	Phosphorylation	AKVLSPESKQARANS EEECCHHHHHHHHHC	33.19	26074081
235	Ubiquitination	KVLSPESKQARANSF EECCHHHHHHHHHCC	46.44	29967540
241	Phosphorylation	SKQARANSFVGTAQY HHHHHHHCCCCCCCC	21.96	19664994
245	Phosphorylation	RANSFVGTAQYVSPE HHHCCCCCCCCCCHH	12.80	22322096
248	Phosphorylation	SFVGTAQYVSPELLT CCCCCCCCCCHHHHC	10.63	30266825
250	Phosphorylation	VGTAQYVSPELLTEK CCCCCCCCHHHHCCH	14.02	30266825
255	Phosphorylation	YVSPELLTEKSACKS CCCHHHHCCHHCCCC	54.73	23927012
257	Ubiquitination	SPELLTEKSACKSSD CHHHHCCHHCCCCHH	37.81	32015554
277	Ubiquitination	CIIYQLVAGLPPFRA HHHHHHHHCCCCCCC	23.54	21890473
277 (in isoform 2)	Ubiquitination	-	23.54	21890473
278 (in isoform 3)	Ubiquitination	-	31.10	21890473
281	Ubiquitination	QLVAGLPPFRAGNEY HHHHCCCCCCCCCCE	36.08	22817900
288	Phosphorylation	PFRAGNEYLIFQKII CCCCCCCEEEEEEEH	14.75	27642862
296	Acetylation	LIFQKIIKLEYDFPE EEEEEEHHCCCCCCH	38.45	26051181
299	Phosphorylation	QKIIKLEYDFPEKFF EEEHHCCCCCCHHHC	33.06	27642862
304	Acetylation	LEYDFPEKFFPKARD CCCCCCHHHCHHHHH	53.17	23954790
304	Ubiquitination	LEYDFPEKFFPKARD CCCCCCHHHCHHHHH	53.17	22817900
304 (in isoform 1)	Ubiquitination	-	53.17	21890473
306	Ubiquitination	YDFPEKFFPKARDLV CCCCHHHCHHHHHHH	10.06	21890473
308	Ubiquitination	FPEKFFPKARDLVEK CCHHHCHHHHHHHHH	51.39	22817900
310	Ubiquitination	EKFFPKARDLVEKLL HHHCHHHHHHHHHHH	43.87	22817900
314	Ubiquitination	PKARDLVEKLLVLDA HHHHHHHHHHHHHHH	45.33	29967540
315	Ubiquitination	KARDLVEKLLVLDAT HHHHHHHHHHHHHHH	39.37	29967540
323	Ubiquitination	LLVLDATKRLGCEEM HHHHHHHHHHCCHHC	47.55	29967540
333	Phosphorylation	GCEEMEGYGPLKAHP CCHHCCCCCCCCCCC	11.41	27642862
337	Ubiquitination	MEGYGPLKAHPFFES CCCCCCCCCCCCCCC	48.02	29967540
338	Ubiquitination	EGYGPLKAHPFFESV CCCCCCCCCCCCCCC	24.22	21890473
342	Ubiquitination	PLKAHPFFESVTWEN CCCCCCCCCCCCHHH	8.90	22817900
342	Ubiquitination	PLKAHPFFESVTWEN CCCCCCCCCCCCHHH	8.90	21890473
344	Phosphorylation	KAHPFFESVTWENLH CCCCCCCCCCHHHHH	21.49	20873877
346	Phosphorylation	HPFFESVTWENLHQQ CCCCCCCCHHHHHCC	36.02	20873877
354	Phosphorylation	WENLHQQTPPKLTAY HHHHHCCCCCCEEEE	34.68	20873877
366	Phosphorylation	TAYLPAMSEDDEDCY EEEECCCCCCCCCCC	39.72	27251275
368	Ubiquitination	YLPAMSEDDEDCYGN EECCCCCCCCCCCCC	58.24	29967540
373	Phosphorylation	SEDDEDCYGNYDNLL CCCCCCCCCCHHHHH	22.26	20643654
376	Phosphorylation	DEDCYGNYDNLLSQF CCCCCCCHHHHHHHH	11.22	18024423
382	Ubiquitination	NYDNLLSQFGCMQVS CHHHHHHHHCCEEEC	38.43	29967540
389	Phosphorylation	QFGCMQVSSSSSSHS HHCCEEECCCCCCCC	13.96	27251275
390	Phosphorylation	FGCMQVSSSSSSHSL HCCEEECCCCCCCCC	35.07	27251275
391	Phosphorylation	GCMQVSSSSSSHSLS CCEEECCCCCCCCCC	27.08	27251275
392	Phosphorylation	CMQVSSSSSSHSLSA CEEECCCCCCCCCCH	37.50	26657352
393	Phosphorylation	MQVSSSSSSHSLSAS EEECCCCCCCCCCHH	33.74	26657352
394	Phosphorylation	QVSSSSSSHSLSASD EECCCCCCCCCCHHH	21.02	22817900
396	Phosphorylation	SSSSSSHSLSASDTG CCCCCCCCCCHHHCC	26.43	15743829
398	Phosphorylation	SSSSHSLSASDTGLP CCCCCCCCHHHCCCC	28.83	22817900
408	Phosphorylation	DTGLPQRSGSNIEQY HCCCCCCCCCCHHHH	41.13	24719451
410	Phosphorylation	GLPQRSGSNIEQYIH CCCCCCCCCHHHHHH	35.56	26074081
415	Phosphorylation	SGSNIEQYIHDLDSN CCCCHHHHHHCCCCC	6.34	19690332
441	Ubiquitination	EKRLLLEKQAGGNPW HHHHHHHHHCCCCCC	45.47	29967540
485	Phosphorylation	LTEGPHLYYVDPVNK HCCCCEEEEECCCCH	9.82	11481331
486	Phosphorylation	TEGPHLYYVDPVNKV CCCCEEEEECCCCHH	12.53	-
495	Ubiquitination	DPVNKVLKGEIPWSQ CCCCHHHCCCCCCCC	58.44	29967540
495	Malonylation	DPVNKVLKGEIPWSQ CCCCHHHCCCCCCCC	58.44	26320211
501	Phosphorylation	LKGEIPWSQELRPEA HCCCCCCCCCCCCCC	14.39	19664994
509	Ubiquitination	QELRPEAKNFKTFFV CCCCCCCCCCCEEEE	62.34	29967540
513	Phosphorylation	PEAKNFKTFFVHTPN CCCCCCCEEEEECCC	20.40	21082442
529	Phosphorylation	TYYLMDPSGNAHKWC EEEEECCCCCHHHHH	40.18	21082442
534	Acetylation	DPSGNAHKWCRKIQE CCCCCHHHHHHHHHH	45.65	7704099

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
9	Y	Phosphorylation	Kinase	INSR	P06213	Uniprot
9	Y	Phosphorylation	Kinase	RET	P07949	PSP
9	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
9	Y	Phosphorylation	Kinase	SRC	P12931	Uniprot
25	S	Phosphorylation	Kinase	PDPK1	O15530	PhosphoELM
25	S	Phosphorylation	Kinase	PDK1	Q15118	GPS
64	S	Phosphorylation	Kinase	PKCT	Q04759	PSP
241	S	Phosphorylation	Kinase	PDPK1	O15530	PhosphoELM
241	S	Phosphorylation	Kinase	PDK1	Q15118	GPS
241	S	Phosphorylation	Kinase	PKCT	Q04759	PSP
354	T	Phosphorylation	Kinase	CDK1	P06493	PSP
354	T	Phosphorylation	Kinase	MELK	Q61846	PSP
354	T	Phosphorylation	Kinase	MELK	Q14680	Uniprot
373	Y	Phosphorylation	Kinase	SRC	P12931	Uniprot
373	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
373	Y	Phosphorylation	Kinase	INSR	P06213	Uniprot
373	Y	Phosphorylation	Kinase	IGF1R	P08069	PSP
376	Y	Phosphorylation	Kinase	SRC	P12931	Uniprot
376	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
376	Y	Phosphorylation	Kinase	IGF1R	P08069	PSP
376	Y	Phosphorylation	Kinase	INSR	P06213	Uniprot
393	S	Phosphorylation	Kinase	PDPK1	O15530	PhosphoELM
393	S	Phosphorylation	Kinase	PDK1	Q15118	GPS
394	S	Phosphorylation	Kinase	ASK1	Q99683	PSP
396	S	Phosphorylation	Kinase	PDPK1	O15530	PhosphoELM
396	S	Phosphorylation	Kinase	PDK1	Q15118	GPS
398	S	Phosphorylation	Kinase	ASK1	Q99683	PSP
410	S	Phosphorylation	Kinase	PDPK1	O15530	PhosphoELM
410	S	Phosphorylation	Kinase	PDK1	Q15118	GPS
501	S	Phosphorylation	Kinase	PRKCQ	Q04759	Uniprot
513	T	Phosphorylation	Kinase	PDPK1	O15530	PhosphoELM
513	T	Phosphorylation	Kinase	PDK1	Q15118	GPS
529	S	Phosphorylation	Kinase	PRKCQ	Q04759	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
241	S	Phosphorylation
PDPK1 itself can autophosphorylate Ser-241, leading to its own activation.
241	S	Phosphorylation
Palmitate negatively regulates autophosphorylation at Ser-241 and palmitate-induced phosphorylation at Ser-529 and Ser-501 by PKC/PRKCQ negatively regulates its ability to phosphorylate PKB/AKT1.
241	S	Phosphorylation
Phosphorylation on Ser-241 in the activation loop is required for full activity.
354	T	Phosphorylation	22544756
Phosphorylation at Thr-354 by MELK partially inhibits kinase activity, the inhibition is cooperatively enhanced by phosphorylation at Ser-394 and Ser-398 by MAP3K5.
394	S	Phosphorylation	22544756
Phosphorylation at Thr-354 by MELK partially inhibits kinase activity, the inhibition is cooperatively enhanced by phosphorylation at Ser-394 and Ser-398 by MAP3K5.
398	S	Phosphorylation	22544756
Phosphorylation at Thr-354 by MELK partially inhibits kinase activity, the inhibition is cooperatively enhanced by phosphorylation at Ser-394 and Ser-398 by MAP3K5.
501	S	Phosphorylation	11481331
Palmitate negatively regulates autophosphorylation at Ser-241 and palmitate-induced phosphorylation at Ser-529 and Ser-501 by PKC/PRKCQ negatively regulates its ability to phosphorylate PKB/AKT1.
529	S	Phosphorylation	11481331
Palmitate negatively regulates autophosphorylation at Ser-241 and palmitate-induced phosphorylation at Ser-529 and Ser-501 by PKC/PRKCQ negatively regulates its ability to phosphorylate PKB/AKT1.

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KPCZ_HUMAN	PRKCZ	physical	10764742
KPCI_HUMAN	PRKCI	physical	10764742
NHRF2_HUMAN	SLC9A3R2	physical	12387817
KPCD_HUMAN	PRKCD	physical	11781095
KPCZ_HUMAN	PRKCZ	physical	11781095
PKN2_HUMAN	PKN2	physical	11781095
PDPK1_HUMAN	PDPK1	physical	10856237
AKT1_HUMAN	AKT1	physical	11825911
KPCB_HUMAN	PRKCB	physical	11376011
KPCZ_HUMAN	PRKCZ	physical	9748166
PKN2_HUMAN	PKN2	physical	10764742
PKN1_HUMAN	PKN1	physical	10764742
1433T_HUMAN	YWHAQ	physical	12177059
1433F_HUMAN	YWHAH	physical	12177059
KAPCA_HUMAN	PRKACA	physical	10698939
ILK_HUMAN	ILK	physical	11313365
SGK1_HUMAN	SGK1	physical	10357815
MK08_HUMAN	MAPK8	physical	10357815
KPCZ_HUMAN	PRKCZ	physical	10357815
SND1_HUMAN	SND1	physical	20562859
G3BP1_HUMAN	G3BP1	physical	20562859
TBL2_HUMAN	TBL2	physical	20562859
PA2G4_HUMAN	PA2G4	physical	20562859
KPCT_HUMAN	PRKCQ	physical	15802604
CAR11_HUMAN	CARD11	physical	15802604
PEA15_HUMAN	PEA15	physical	21900206
PGFS_HUMAN	FAM213B	physical	21900206
CAR11_HUMAN	CARD11	physical	21900206
PDIP2_HUMAN	POLDIP2	physical	21900206
GIT1_HUMAN	GIT1	physical	21900206
ZN133_HUMAN	ZNF133	physical	21900206
XPO7_HUMAN	XPO7	physical	21900206
MTMR5_HUMAN	SBF1	physical	21900206
PNO1_HUMAN	PNO1	physical	21900206
DDIT4_HUMAN	DDIT4	physical	21900206
SNF5_HUMAN	SMARCB1	physical	21900206
SOCS3_HUMAN	SOCS3	physical	21900206
WDCP_HUMAN	C2orf44	physical	21900206
KTBL1_HUMAN	KATNBL1	physical	21900206
XRCC6_HUMAN	XRCC6	physical	21900206
TELT_HUMAN	TCAP	physical	21900206
BLMH_HUMAN	BLMH	physical	21900206
PHAX_HUMAN	PHAX	physical	21900206
NIPA_HUMAN	ZC3HC1	physical	21900206
LC7L2_HUMAN	LUC7L2	physical	21900206
SGK1_HUMAN	SGK1	physical	17916563
STRAP_HUMAN	STRAP	physical	17916563
A4_HUMAN	APP	physical	21832049
AKT1_HUMAN	AKT1	physical	22569334
PDPK1_HUMAN	PDPK1	physical	25384981
TBL2_HUMAN	TBL2	physical	26186194
KAIN_HUMAN	SERPINA4	physical	26186194
CBPA4_HUMAN	CPA4	physical	26186194
F199X_HUMAN	FAM199X	physical	26186194
M3K7_HUMAN	MAP3K7	physical	26432169
HSP7C_HUMAN	HSPA8	physical	28514442
KAIN_HUMAN	SERPINA4	physical	28514442
F199X_HUMAN	FAM199X	physical	28514442
SCRN2_HUMAN	SCRN2	physical	28514442
CBPA4_HUMAN	CPA4	physical	28514442
TBL2_HUMAN	TBL2	physical	28514442
AKT2_HUMAN	AKT2	physical	27563096
AKT1_HUMAN	AKT1	physical	27563096
AKT1_MOUSE	Akt1	physical	19662498

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00482	Celecoxib

Regulatory Network of PDPK1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-304, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"PDK1 phosphorylation at Thr354 by murine protein serine/threoninekinase 38 contributes to the negative regulation of PDK1 activity."; Seong H.A., Jung H., Manoharan R., Ha H.; J. Biol. Chem. 0:0-0(2012). Cited for: PHOSPHORYLATION AT THR-354 BY MELK, PHOSPHORYLATION AT SER-394 ANDSER-398 BY MAP3K5, AND MUTAGENESIS OF THR-354; SER-394 AND SER-398.	22544756 [Abstract]
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35 AND SER-241, AND MASSSPECTROMETRY.	19369195 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-37 AND SER-241, AND MASSSPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-37 AND SER-241, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Phosphoproteomic analysis of the human pituitary."; Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.; Pituitary 9:109-120(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND MASSSPECTROMETRY.	16807684 [Abstract]
"Phosphoinositide-dependent phosphorylation of PDK1 regulates nucleartranslocation."; Scheid M.P., Parsons M., Woodgett J.R.; Mol. Cell. Biol. 25:2347-2363(2005). Cited for: PHOSPHORYLATION AT SER-396, AND SUBCELLULAR LOCATION.	15743829 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND MASSSPECTROMETRY.	15302935 [Abstract]
"Identification of tyrosine phosphorylation sites on 3-phosphoinositide-dependent protein kinase-1 (PDK1) and their role inregulating kinase activity."; Park J., Hill M.M., Hess D., Brazil D.P., Hofsteenge J.,Hemmings B.A.; J. Biol. Chem. 276:37459-37471(2001). Cited for: PHOSPHORYLATION AT TYR-9; SER-241; TYR-373 AND TYR-376, ANDMUTAGENESIS OF TYR-9; TYR-373 AND TYR-376.	11481331 [Abstract]
"Phosphorylation of Ser-241 is essential for the activity of 3-phosphoinositide-dependent protein kinase-1: identification of fivesites of phosphorylation in vivo."; Casamayor A., Morrice N.A., Alessi D.R.; Biochem. J. 342:287-292(1999). Cited for: PHOSPHORYLATION AT SER-25; SER-241; SER-393; SER-396 AND SER-410, ANDMUTAGENESIS OF SER-25; SER-241; SER-393; SER-396 AND SER-410.	10455013 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-245, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Tyrosine phosphorylation of phosphoinositide-dependent kinase 1 bythe insulin receptor is necessary for insulin metabolic signaling."; Fiory F., Alberobello A.T., Miele C., Oriente F., Esposito I.,Corbo V., Ruvo M., Tizzano B., Rasmussen T.E., Gammeltoft S.,Formisano P., Beguinot F.; Mol. Cell. Biol. 25:10803-10814(2005). Cited for: PHOSPHORYLATION AT TYR-9; TYR-373 AND TYR-376 BY INSR, AND INTERACTIONWITH INSR.	16314505 [Abstract]
"Pyk2- and Src-dependent tyrosine phosphorylation of PDK1 regulatesfocal adhesions."; Taniyama Y., Weber D.S., Rocic P., Hilenski L., Akers M.L., Park J.,Hemmings B.A., Alexander R.W., Griendling K.K.; Mol. Cell. Biol. 23:8019-8029(2003). Cited for: FUNCTION, PHOSPHORYLATION AT TYR-9; TYR-373 AND TYR-376 BY SRC,INTERACTION WITH PTK2B, AND SUBCELLULAR LOCATION.	14585963 [Abstract]

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