Reviewed, UniProtKB/Swiss-Prot O15530 (PDPK1_HUMAN)

Names and origin

Protein names

Recommended name:
    3-phosphoinositide-dependent protein kinase 1
      Short name=hPDK1
    EC=2.7.11.1

Gene names

Name:	PDPK1
Synonyms:	PDK1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	556 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Phosphorylates and activates not only PKB/AKT, but also PKA, PKC-zeta, RPS6KA1 and RPS6KB1. May play a general role in signaling processes and in development By similarity. Isoform 3 is catalytically inactive.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	Interacts with TUSC4. Ref.14
Subcellular location	Cytoplasm. Membrane; Peripheral membrane protein. Note: Membrane-associated after cell stimulation leading to its translocation. Tyrosine phosphorylation seems to occur only at the plasma membrane.
Tissue specificity	Appears to be expressed ubiquitously.
Post-translational modification	Phosphorylated on tyrosine and serine/threonine. Phosphorylation on Ser-241 in the activation loop is required for full activity. PDK1 itself can autophosphorylate Ser-241, leading to its own activation. Ref.6 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.19
Sequence similarities	Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PDK1 subfamily. Contains 1 PH domain. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Cytoplasm Membrane
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	actin cytoskeleton organization Traceable author statement. Source: ProtInc activation of protein kinase B activity Ref.2 Inferred from direct assay. Source: UniProtKB cellular response to insulin stimulus Inferred from mutant phenotype. Source: UniProtKB intracellular signaling cascade Inferred from direct assay. Source: MGI negative regulation of protein kinase activity Inferred from direct assay. Source: UniProtKB peptidyl-threonine phosphorylation Ref.2 Inferred from direct assay. Source: UniProtKB positive regulation of establishment of protein localization in plasma membrane Inferred from mutant phenotype. Source: UniProtKB
Cellular component	cytosol Inferred from Experiment. Source: Reactome extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Ref.7 Inferred from direct assay. Source: UniProtKB
Molecular function	3-phosphoinositide-dependent protein kinase activity Ref.2 Inferred from direct assay. Source: UniProtKB ATP binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PTPN12	Q05209	1	EBI-717097,EBI-2266035
PTPN22	Q9Y2R2	1	EBI-717097,EBI-1211241
PTPRB	P23467	1	EBI-717097,EBI-1265766
PTPRC	P08575	1	EBI-717097,EBI-1341
PTPRG	P23470	1	EBI-717097,EBI-2258115
PTPRJ	Q12913	1	EBI-717097,EBI-2264500
PTPRK	Q15262	1	EBI-717097,EBI-474052
PTPRO	Q16827	1	EBI-717097,EBI-723739
SGK1	O00141	1	EBI-717097,EBI-1042854

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O15530-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: O15530-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-50: Missing.

Isoform 3 (identifier: O15530-3)

The sequence of this isoform differs from the canonical sequence as follows:
     238-263: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 556

556

3-phosphoinositide-dependent protein kinase 1

PRO_0000086500

Regions

Domain

82 – 342

261

Protein kinase

Domain

459 – 550

92

PH

Nucleotide binding

88 – 96

9

ATP By similarity

Compositional bias

389 – 398

10

Poly-Ser

Sites

Active site

205

1

Proton acceptor By similarity

Binding site

111

1

ATP By similarity

Amino acid modifications

Modified residue

9

1

Phosphotyrosine Ref.10

Modified residue

25

1

Phosphoserine Ref.8

Modified residue

35

1

Phosphoserine

Modified residue

37

1

Phosphothreonine Ref.15 Ref.17

Modified residue

241

1

Phosphoserine; by autocatalysis Ref.6 Ref.8 Ref.10 Ref.11 Ref.13 Ref.15 Ref.16 Ref.17 Ref.19

Modified residue

245

1

Phosphothreonine Ref.12

Modified residue

304

1

N6-acetyllysine Ref.20

Modified residue

373

1

Phosphotyrosine Ref.10

Modified residue

376

1

Phosphotyrosine Ref.10

Modified residue

393

1

Phosphoserine Ref.8

Modified residue

396

1

Phosphoserine Ref.8

Modified residue

410

1

Phosphoserine Ref.8

Natural variations

Alternative sequence

1 – 50

50

Missing in isoform 2.

VSP_004894

Alternative sequence

238 – 263

26

Missing in isoform 3.

VSP_004895

Experimental info

Mutagenesis

9

1

Y → F: Slight reduction in pervanadate-stimulated tyrosine phosphorylation. Ref.10

Mutagenesis

25

1

S → A: No effect. Ref.8

Mutagenesis

241

1

S → A: No activation. Ref.8

Mutagenesis

277

1

A → V: 3-fold increase in kinase activity. Ref.9

Mutagenesis

373

1

Y → F: Reduction in basal activity. Ref.10

Mutagenesis

376

1

Y → F: Reduction in basal activity. Ref.10

Mutagenesis

393

1

S → A: No effect. Ref.8

Mutagenesis

396

1

S → A: No effect. Ref.8

Mutagenesis

410

1

S → A: No effect. Ref.8

Mutagenesis

474

1

R → A: No PDGF-dependent translocation to the membrane. Ref.7

Secondary structure

1

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556

Helix Strand Turn

Details...

Helix

79 – 81

3

Beta strand

82 – 90

9

Beta strand

95 – 101

7

Turn

102 – 104

3

Beta strand

107 – 114

8

Helix

115 – 120

6

Helix

124 – 136

13

Beta strand

145 – 150

6

Beta strand

152 – 159

8

Helix

167 – 174

8

Helix

179 – 198

20

Turn

208 – 210

3

Beta strand

211 – 213

3

Beta strand

219 – 221

3

Helix

246 – 248

3

Helix

251 – 255

5

Helix

261 – 277

17

Helix

287 – 295

9

Helix

307 – 314

8

Helix

321 – 323

3

Helix

328 – 330

3

Helix

333 – 337

5

Helix

340 – 342

3

Helix

350 – 352

3

Helix

412 – 415

4

Beta strand

416 – 420

5

Beta strand

423 – 426

4

Helix

432 – 445

14

Helix

449 – 451

3

Turn

452 – 454

3

Beta strand

457 – 467

11

Beta strand

470 – 479

10

Turn

480 – 482

3

Beta strand

483 – 488

6

Turn

489 – 492

4

Beta strand

493 – 498

6

Beta strand

505 – 518

14

Beta strand

521 – 526

6

Helix

532 – 547

16

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: ED8C0306DC4D0653	FASTA	556	63,152
	10 20 30 40 50 60 MARTTSQLYD AVPIQSSVVL CSCPSPSMVR TQTESSTPPG IPGGSRQGPA MDGTAAEPRP 70 80 90 100 110 120 GAGSLQHAQP PPQPRKKRPE DFKFGKILGE GSFSTVVLAR ELATSREYAI KILEKRHIIK 130 140 150 160 170 180 ENKVPYVTRE RDVMSRLDHP FFVKLYFTFQ DDEKLYFGLS YAKNGELLKY IRKIGSFDET 190 200 210 220 230 240 CTRFYTAEIV SALEYLHGKG IIHRDLKPEN ILLNEDMHIQ ITDFGTAKVL SPESKQARAN 250 260 270 280 290 300 SFVGTAQYVS PELLTEKSAC KSSDLWALGC IIYQLVAGLP PFRAGNEYLI FQKIIKLEYD 310 320 330 340 350 360 FPEKFFPKAR DLVEKLLVLD ATKRLGCEEM EGYGPLKAHP FFESVTWENL HQQTPPKLTA 370 380 390 400 410 420 YLPAMSEDDE DCYGNYDNLL SQFGCMQVSS SSSSHSLSAS DTGLPQRSGS NIEQYIHDLD 430 440 450 460 470 480 SNSFELDLQF SEDEKRLLLE KQAGGNPWHQ FVENNLILKM GPVDKRKGLF ARRRQLLLTE 490 500 510 520 530 540 GPHLYYVDPV NKVLKGEIPW SQELRPEAKN FKTFFVHTPN RTYYLMDPSG NAHKWCRKIQ 550 EVWRQRYQSH PDAAVQ
	Isoform 2. Checksum: 22D376B8A13FD3F3	FASTA	506	58,035
	10 20 30 40 50 60 MDGTAAEPRP GAGSLQHAQP PPQPRKKRPE DFKFGKILGE GSFSTVVLAR ELATSREYAI 70 80 90 100 110 120 KILEKRHIIK ENKVPYVTRE RDVMSRLDHP FFVKLYFTFQ DDEKLYFGLS YAKNGELLKY 130 140 150 160 170 180 IRKIGSFDET CTRFYTAEIV SALEYLHGKG IIHRDLKPEN ILLNEDMHIQ ITDFGTAKVL 190 200 210 220 230 240 SPESKQARAN SFVGTAQYVS PELLTEKSAC KSSDLWALGC IIYQLVAGLP PFRAGNEYLI 250 260 270 280 290 300 FQKIIKLEYD FPEKFFPKAR DLVEKLLVLD ATKRLGCEEM EGYGPLKAHP FFESVTWENL 310 320 330 340 350 360 HQQTPPKLTA YLPAMSEDDE DCYGNYDNLL SQFGCMQVSS SSSSHSLSAS DTGLPQRSGS 370 380 390 400 410 420 NIEQYIHDLD SNSFELDLQF SEDEKRLLLE KQAGGNPWHQ FVENNLILKM GPVDKRKGLF 430 440 450 460 470 480 ARRRQLLLTE GPHLYYVDPV NKVLKGEIPW SQELRPEAKN FKTFFVHTPN RTYYLMDPSG 490 500 NAHKWCRKIQ EVWRQRYQSH PDAAVQ
	Isoform 3. Checksum: CEAF882CBD3EB1F2	FASTA	530	60,396
	10 20 30 40 50 60 MARTTSQLYD AVPIQSSVVL CSCPSPSMVR TQTESSTPPG IPGGSRQGPA MDGTAAEPRP 70 80 90 100 110 120 GAGSLQHAQP PPQPRKKRPE DFKFGKILGE GSFSTVVLAR ELATSREYAI KILEKRHIIK 130 140 150 160 170 180 ENKVPYVTRE RDVMSRLDHP FFVKLYFTFQ DDEKLYFGLS YAKNGELLKY IRKIGSFDET 190 200 210 220 230 240 CTRFYTAEIV SALEYLHGKG IIHRDLKPEN ILLNEDMHIQ ITDFGTAKVL SPESKQADLW 250 260 270 280 290 300 ALGCIIYQLV AGLPPFRAGN EYLIFQKIIK LEYDFPEKFF PKARDLVEKL LVLDATKRLG 310 320 330 340 350 360 CEEMEGYGPL KAHPFFESVT WENLHQQTPP KLTAYLPAMS EDDEDCYGNY DNLLSQFGCM 370 380 390 400 410 420 QVSSSSSSHS LSASDTGLPQ RSGSNIEQYI HDLDSNSFEL DLQFSEDEKR LLLEKQAGGN 430 440 450 460 470 480 PWHQFVENNL ILKMGPVDKR KGLFARRRQL LLTEGPHLYY VDPVNKVLKG EIPWSQELRP 490 500 510 520 530 EAKNFKTFFV HTPNRTYYLM DPSGNAHKWC RKIQEVWRQR YQSHPDAAVQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase B alpha." Alessi D.R., James S.R., Downes C.P., Holmes A.B., Gaffney P.R.J., Reese C.B., Cohen P. Curr. Biol. 7:261-269(1997) [PubMed: 9094314] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"3-phosphoinositide-dependent protein kinase-1 (PDK1): structural and functional homology with the Drosophila DSTPK61 kinase." Alessi D.R., Deak M., Casamayor A., Caudwell F.B., Morrice N.A., Norman D.G., Gaffney P.R.J., Reese C.B., MacDougall C.N., Harbison D., Ashworth A., Bownes M. Curr. Biol. 7:776-789(1997) [PubMed: 9368760] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"Protein kinase B kinases that mediate phosphatidylinositol 3,4,5-trisphosphate-dependent activation of protein kinase B." Stephens L.R., Anderson K.E., Stokoe D., Erdjument-Bromage H., Painter G.F., Holmes A.B., Gaffney P.R.J., Reese C.B., McCormick F., Tempst P., Coadwell W.J., Hawkins P.T. Science 279:710-714(1998) [PubMed: 9445477] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3). Tissue: Myeloid.
[4]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Kidney.
[6]	Bienvenut W.V., Waridel P., Quadroni M. Submitted (MAR-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 60-75; 87-100; 184-199; 239-257 AND 284-293, PHOSPHORYLATION AT SER-241, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[7]	"Translocation of PDK-1 to the plasma membrane is important in allowing PDK-1 to activate protein kinase B." Anderson K.E., Coadwell W.J., Stephens L.R., Hawkins P.T. Curr. Biol. 8:684-691(1998) [PubMed: 9637919] [Abstract] Cited for: MUTAGENESIS OF ARG-474, ALTERNATIVE SPLICING.
[8]	"Phosphorylation of Ser-241 is essential for the activity of 3-phosphoinositide-dependent protein kinase-1: identification of five sites of phosphorylation in vivo." Casamayor A., Morrice N.A., Alessi D.R. Biochem. J. 342:287-292(1999) [PubMed: 10455013] [Abstract] Cited for: PHOSPHORYLATION AT SER-25; SER-241; SER-393; SER-396 AND SER-410, MUTAGENESIS OF SER-25; SER-241; SER-393; SER-396 AND SER-410.
[9]	"A PDK1 homolog is necessary and sufficient to transduce AGE-1 PI3 kinase signals that regulate diapause in Caenorhabditis elegans." Paradis S., Ailion M., Toker A., Thomas J.H., Ruvkun G. Genes Dev. 13:1438-1452(1999) [PubMed: 10364160] [Abstract] Cited for: MUTAGENESIS OF ALA-277.
[10]	"Identification of tyrosine phosphorylation sites on 3-phosphoinositide-dependent protein kinase-1 (PDK1) and their role in regulating kinase activity." Park J., Hill M.M., Hess D., Brazil D.P., Hofsteenge J., Hemmings B.A. J. Biol. Chem. 276:37459-37471(2001) [PubMed: 11481331] [Abstract] Cited for: PHOSPHORYLATION AT TYR-9; SER-241; TYR-373 AND TYR-376, MUTAGENESIS OF TYR-9; TYR-373 AND TYR-376.
[11]	"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) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, MASS SPECTROMETRY. Tissue: Epithelium.
[12]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-245, MASS SPECTROMETRY. Tissue: Epithelium.
[13]	"Phosphoproteomic analysis of the human pituitary." Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F. Pituitary 9:109-120(2006) [PubMed: 16807684] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, MASS SPECTROMETRY. Tissue: Pituitary.
[14]	"TUSC4/NPRL2, a novel PDK1-interacting protein, inhibits PDK1 tyrosine phosphorylation and its downstream signaling." Kurata A., Katayama R., Watanabe T., Tsuruo T., Fujita N. Cancer Sci. 99:1827-1834(2008) [PubMed: 18616680] [Abstract] Cited for: INTERACTION WITH TUSC4.
[15]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the 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) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-37 AND SER-241, MASS SPECTROMETRY.
[16]	"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) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, MASS SPECTROMETRY.
[17]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-37 AND SER-241, MASS SPECTROMETRY.
[18]	"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) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35 AND SER-241, MASS SPECTROMETRY.
[19]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, MASS SPECTROMETRY. Tissue: T-cell.
[20]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-304, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF017995 mRNA. Translation: AAC51825.1.
Y15056 mRNA. Translation: CAA75341.1.
CR536517 mRNA. Translation: CAG38755.1.
BC012103 mRNA. Translation: AAH12103.1.

IPI

IPI00002538.
IPI00216646.
IPI00216647.

RefSeq

NP_002604.1.
NP_112558.2.

UniGene

Hs.459691

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1H1W	X-ray	2.00	A	71-359	[»]
1OKY	X-ray	2.30	A	51-360	[»]
1OKZ	X-ray	2.51	A	51-360	[»]
1UU3	X-ray	1.70	A	51-360	[»]
1UU7	X-ray	1.90	A	51-360	[»]
1UU8	X-ray	2.50	A	51-360	[»]
1UU9	X-ray	1.95	A	72-357	[»]
1UVR	X-ray	2.81	A	71-359	[»]
1W1D	X-ray	1.50	A	409-556	[»]
1W1G	X-ray	1.45	A	409-556	[»]
1W1H	X-ray	1.45	A/B/C/D	409-556	[»]
1Z5M	X-ray	2.17	A	74-359	[»]
2BIY	X-ray	1.95	A	51-360	[»]
2PE0	X-ray	2.35	A	74-359	[»]
2PE1	X-ray	2.14	A	74-359	[»]
2PE2	X-ray	2.13	A	74-359	[»]
2R7B	X-ray	2.70	A	48-359	[»]
2VKI	X-ray	1.80	A	409-556	[»]
3H9O	X-ray	2.30	A	51-359	[»]
3HRC	X-ray	1.91	A	51-359	[»]
3HRF	X-ray	1.90	A	51-359	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

O15530. 16 interactions.

STRING

O15530.

PTM databases

PhosphoSite

O15530.

Proteomic databases

PRIDE

O15530.

Genome annotation databases

Ensembl

ENST00000342085; ENSP00000344220; ENSG00000140992; Homo sapiens. [Genome view]

GeneID

5170.

KEGG

hsa:5170.

UCSC

uc002cqs.1. human.

Organism-specific databases

CTD

5170.

GeneCards

GC16P002527.

H-InvDB

HIX0012730.
HIX0027031.
HIX0038570.
HIX0038793.

HGNC

HGNC:8816. PDPK1.

HPA

CAB004272.

MIM

605213. gene.

PharmGKB

PA33160.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG14283.

HOGENOM

HBG755340.

HOVERGEN

O15530.

InParanoid

O15530.

OMA

ESITWEL.

OrthoDB

EOG9Z390V.

PhylomeDB

O15530.

Enzyme and pathway databases

BRENDA

2.7.11.1. 247.

Pathway_Interaction_DB

bcr_5pathway. BCR signaling pathway.
pi3kcipathway. Class I PI3K signaling events.
pi3kciaktpathway. Class I PI3K signaling events mediated by Akt.
fgf_pathway. FGF signaling pathway.
igf1_pathway. IGF1 pathway.
insulin_pathway. Insulin Pathway.
mtor_4pathway. mTOR signaling pathway.
met_pathway. Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met).
kitpathway. Signaling events mediated by Stem cell factor receptor (c-Kit).
vegfr1_2_pathway. Signaling events mediated by VEGFR1 and VEGFR2.
tcrpathway. TCR signaling in naive CD4+ T cells.
cd8tcrpathway. TCR signaling in naive CD8+ T cells.
tgfbrpathway. TGF-beta receptor signaling.
pi3kplctrkpathway. Trk receptor signaling mediated by PI3K and PLC-gamma.
vegfr1_pathway. VEGFR1 specific signals.

Reactome

REACT_11061. Signalling by NGF.
REACT_13685. Synaptic Transmission.
REACT_14797. Signaling by GPCR.
REACT_498. Signaling by Insulin receptor.
REACT_604. Hemostasis.
REACT_6900. Signaling in Immune system.

Gene expression databases

ArrayExpress

O15530.

Bgee

O15530.

CleanEx

HS_PDK1.
HS_PDPK1.

Genevestigator

O15530.

GermOnline

ENSG00000140992. Homo sapiens.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR011993. PH_type.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_prot_kinase-like_dom.
IPR015746. Ser/Thr_kinase_PInositide-dep.
IPR008271. Ser/Thr_prot_kinase_AS.
IPR002290. Ser/Thr_prot_kinase_dom.
[Graphical view]

Gene3D

G3DSA:2.30.29.30. PH_type. 1 hit.

PANTHER

PTHR22985:SF93. PK1_3-phosphoinositide. 1 hit.

Pfam

PF00069. Pkinase. 1 hit.
[Graphical view]

SMART

SM00220. S_TKc. 1 hit.
[Graphical view]

PROSITE

PS50003. PH_DOMAIN. False negative.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

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Other Resources

DrugBank

DB00482. Celecoxib.

NextBio

20004.

SOURCE

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Entry information

Entry name

PDPK1_HUMAN

Accession

Primary (citable) accession number: O15530
Secondary accession number(s): Q6FI20

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 18, 2001
Last sequence update:	January 1, 1998
Last modified:	February 9, 2010
This is version 115 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.