O15530 (PDPK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

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

General annotation (Comments)

Function	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 Ca2+ entry and Ca2+-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. Ref.1 Ref.10 Ref.11 Ref.12 Ref.15 Ref.16 Ref.19 Ref.20 Ref.21 Ref.23 Ref.25 Ref.26 Ref.29 Ref.30 Ref.31
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Homodimerization regulates its activity by maintaining the kinase in an autoinhibitory conformation. NPRL2 down-regulates its activity by interfering with tyrosine phosphorylation at the Tyr-9, Tyr-373 and Tyr-376 residues. The 14-3-3 protein YWHAQ acts as a negative regulator by association with the residues surrounding the Ser-241 residue. STRAP positively regulates its activity by enhancing its autophosphorylation and by stimulating its dissociation from YWHAQ. SMAD2, SMAD3, SMAD4 and SMAD7 also positively regulate its activity by stimulating its dissociation from YWHAQ. Activated by phosphorylation on Tyr-9, Tyr-373 and Tyr-376 by INSR in response to insulin. Ref.18 Ref.26 Ref.32 Ref.40
Subunit structure	Homodimer in its autoinhibited state. Active as monomer. Interacts with NPRL2, PPARG, PAK1, PTK2B, GRB14, PKN1 (via C-terminus), STRAP and IKKB. The Tyr-9 phosphorylated form interacts with SRC, RASA1 and CRK (via their SH2 domains). Interacts with SGK3 in a phosphorylation-dependent manner. The tyrosine-phosphorylated form interacts with PTPN6. The Ser-241 phosphorylated form interacts with YWHAH and YWHAQ. Binds INSR in response to insulin. Interacts (via PH domain) with SMAD3, SMAD4 and SMAD7. Interacts with PKN2; the interaction stimulates PDPK1 autophosphorylation, its PI(3,4,5)P3-dependent kinase activity toward 'Ser-473' of AKT1 but also activates its kinase activity toward PRKCD and PRKCZ. Ref.16 Ref.18 Ref.20 Ref.21 Ref.22 Ref.23 Ref.25 Ref.26 Ref.28 Ref.29 Ref.32 Ref.34 Ref.35 Ref.40
Subcellular location	Cytoplasm. Nucleus. Cell membrane; Peripheral membrane protein. Cell junction › focal adhesion. Note: Tyrosine phosphorylation seems to occur only at the cell membrane. Translocates to the cell membrane following insulin stimulation by a mechanism that involves binding to GRB14 and INSR. SRC and HSP90 promote its localization to the cell membrane. Its nuclear localization is dependent on its association with PTPN6 and its phosphorylation at Ser-396. Restricted to the nucleus in neuronal cells while in non-neuronal cells it is found in the cytoplasm. The Ser-241 phosphorylated form is distributed along the perinuclear region in neuronal cells while in non-neuronal cells it is found in both the nucleus and the cytoplasm. IGF1 transiently increases phosphorylation at Ser-241 of neuronal PDPK1, resulting in its translocation to other cellular compartments. The tyrosine-phosphorylated form colocalizes with PTK2B in focal adhesions after angiotensin II stimulation. Ref.20 Ref.22 Ref.27 Ref.30 Ref.34 Ref.35 Ref.36
Tissue specificity	Appears to be expressed ubiquitously. The Tyr-9 phosphorylated form is markedly increased in diseased tissue compared with normal tissue from lung, liver, colon and breast. Ref.34
Induction	Stimulated by insulin, and the oxidants hydrogen peroxide and peroxovanadate. Ref.18 Ref.26 Ref.32 Ref.40
Domain	The PH domain plays a pivotal role in the localization and nuclear import of PDPK1 and is also essential for its homodimerization.
Post-translational modification	Phosphorylation on Ser-241 in the activation loop is required for full activity. PDPK1 itself can autophosphorylate Ser-241, leading to its own activation. Autophosphorylation is inhibited by the apoptotic C-terminus cleavage product of PKN2 By similarity. Tyr-9 phosphorylation is critical for stabilization of both PDPK1 and the PDPK1/SRC complex via HSP90-mediated protection of PDPK1 degradation. Angiotensin II stimulates the tyrosine phosphorylation of PDPK1 in vascular smooth muscle in a calcium- and SRC-dependent manner. Phosphorylated on Tyr-9, Tyr-373 and Tyr-376 by INSR in response to insulin. 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. 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. Ref.8 Ref.13 Ref.17 Ref.20 Ref.27 Ref.28 Ref.38 Autophosphorylated; autophosphorylation is inhibited by the apoptotic C-terminus cleavage product of PKN2 By similarity. Ref.8 Ref.13 Ref.17 Ref.20 Ref.27 Ref.28 Ref.38 Monoubiquitinated in the kinase domain, deubiquitinated by USP4.
Sequence similarities	Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PDPK1 subfamily. Contains 1 PH domain. Contains 1 protein kinase domain.
Sequence caution	The sequence BAD93072.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cell junction Cell membrane Cytoplasm Membrane Nucleus
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Activator Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	T cell costimulation Traceable author statement. Source: Reactome T cell receptor signaling pathway Traceable author statement. Source: Reactome actin cytoskeleton organization Traceable author statement PubMed 10792047. Source: ProtInc activation of protein kinase B activity Inferred from direct assay Ref.2. Source: BHF-UCL epidermal growth factor receptor signaling pathway Traceable author statement. Source: Reactome fibroblast growth factor receptor signaling pathway Traceable author statement. Source: Reactome focal adhesion assembly Inferred from electronic annotation. Source: Compara hyperosmotic response Inferred from electronic annotation. Source: Compara insulin receptor signaling pathway Traceable author statement. Source: Reactome negative regulation of cardiac muscle cell apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of protein kinase activity Inferred from direct assay PubMed 9373175. Source: BHF-UCL negative regulation of toll-like receptor signaling pathway Inferred from electronic annotation. Source: Compara negative regulation of transforming growth factor beta receptor signaling pathway Inferred from direct assay Ref.29. Source: UniProtKB nerve growth factor receptor signaling pathway Traceable author statement. Source: Reactome peptidyl-threonine phosphorylation Inferred from direct assay Ref.2. Source: BHF-UCL phosphatidylinositol-mediated signaling Traceable author statement. Source: Reactome platelet activation Traceable author statement. Source: Reactome positive regulation of establishment of protein localization to plasma membrane Inferred from mutant phenotype PubMed 10567711. Source: BHF-UCL protein autophosphorylation Traceable author statement Ref.24. Source: UniProtKB regulation of I-kappaB kinase/NF-kappaB cascade Inferred from mutant phenotype Ref.25. Source: UniProtKB regulation of apoptotic process Inferred from mutant phenotype Ref.25. Source: UniProtKB regulation of endothelial cell migration Inferred from electronic annotation. Source: Compara regulation of mast cell degranulation Inferred from electronic annotation. Source: Compara regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW synaptic transmission Traceable author statement. Source: Reactome transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW type B pancreatic cell development Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasmic membrane-bounded vesicle Inferred from electronic annotation. Source: Compara cytosol Traceable author statement. Source: Reactome focal adhesion Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Traceable author statement. Source: Reactome plasma membrane Inferred from direct assay Ref.9. Source: UniProtKB
Molecular_function	3-phosphoinositide-dependent protein kinase activity Inferred from direct assay Ref.2. Source: BHF-UCL ATP binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PPP2R2B	Q00005	8	EBI-717097,EBI-1052159

Alternative products

This entry describes 5 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.

Isoform 4 (identifier: O15530-4)

The sequence of this isoform differs from the canonical sequence as follows:
     110-237: IKILEKRHII...KVLSPESKQA → T

Isoform 5 (identifier: O15530-5)

The sequence of this isoform differs from the canonical sequence as follows:
     448-556: WHQFVENNLI...YQSHPDAAVQ → CLTGRII

Note: No experimental confirmation available.

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; by SRC and INSR Ref.17 Ref.20 Ref.28

Modified residue

25

1

Phosphoserine Ref.13

Modified residue

241

1

Phosphoserine; by autocatalysis Ref.8 Ref.13 Ref.17

Modified residue

354

1

Phosphothreonine; by MELK Ref.38

Modified residue

373

1

Phosphotyrosine; by SRC and INSR Ref.17 Ref.20 Ref.28

Modified residue

376

1

Phosphotyrosine; by SRC and INSR Ref.17 Ref.20 Ref.28

Modified residue

393

1

Phosphoserine Ref.13

Modified residue

394

1

Phosphoserine; by MAP3K5 Ref.38

Modified residue

396

1

Phosphoserine Ref.13 Ref.27

Modified residue

398

1

Phosphoserine; by MAP3K5 Ref.38

Modified residue

410

1

Phosphoserine Ref.13

Modified residue

501

1

Phosphoserine; by PKC/PRKCQ By similarity

Modified residue

513

1

Phosphothreonine; by autocatalysis

Modified residue

529

1

Phosphoserine; by PKC/PRKCQ By similarity

Natural variations

Alternative sequence

1 – 50

50

Missing in isoform 2.

VSP_004894

Alternative sequence

110 – 237

128

IKILE…ESKQA → T in isoform 4.

VSP_041902

Alternative sequence

238 – 263

26

Missing in isoform 3.

VSP_004895

Alternative sequence

448 – 556

109

WHQFV…DAAVQ → CLTGRII in isoform 5.

VSP_044796

Experimental info

Mutagenesis

9

1

Y → F: Slight reduction in pervanadate-stimulated tyrosine phosphorylation. Ref.17

Mutagenesis

25

1

S → A: No effect. Ref.13

Mutagenesis

241

1

S → A: No activation. Ref.13

Mutagenesis

277

1

A → V: 3-fold increase in kinase activity. Ref.14

Mutagenesis

354

1

T → A: Abolishes phosphorylation by MELK. Ref.38

Mutagenesis

373

1

Y → F: Reduction in basal activity. Ref.17

Mutagenesis

376

1

Y → F: Reduction in basal activity. Ref.17

Mutagenesis

393

1

S → A: No effect. Ref.13

Mutagenesis

394

1

S → A: Abolishes phosphorylation by MAP3K5; when associated with A-398. Ref.38

Mutagenesis

396

1

S → A: No effect. Ref.13

Mutagenesis

398

1

S → A: Abolishes phosphorylation by MAP3K5; when associated with A-394. Ref.38

Mutagenesis

410

1

S → A: No effect. Ref.13

Mutagenesis

474

1

R → A: No PDGF-dependent translocation to the membrane. Ref.9

Mutagenesis

513

1

T → E: Enhanced kinase activity towards PKB. Ref.40

Secondary structure

1

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556

Helix Strand Turn

Details...

Helix

79 – 81

3

Beta strand

82 – 91

10

Beta strand

94 – 101

8

Turn

102 – 104

3

Beta strand

107 – 114

8

Helix

115 – 120

6

Helix

124 – 134

11

Beta strand

145 – 150

6

Beta strand

152 – 159

8

Beta strand

163 – 166

4

Helix

167 – 174

8

Helix

179 – 198

20

Helix

208 – 210

3

Beta strand

211 – 213

3

Beta strand

219 – 221

3

Helix

224 – 226

3

Turn

232 – 235

4

Beta strand

238 – 240

3

Helix

246 – 248

3

Helix

251 – 256

6

Helix

261 – 277

17

Helix

287 – 296

10

Beta strand

303 – 305

3

Helix

307 – 316

10

Helix

321 – 323

3

Helix

328 – 330

3

Helix

333 – 337

5

Helix

340 – 342

3

Helix

347 – 349

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 [UniParc]. 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 [UniParc]. 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
	Isoform 4 [UniParc]. Checksum: 860C8A8C06161CE1	FASTA	429	48,201
	10 20 30 40 50 60 MARTTSQLYD AVPIQSSVVL CSCPSPSMVR TQTESSTPPG IPGGSRQGPA MDGTAAEPRP 70 80 90 100 110 120 GAGSLQHAQP PPQPRKKRPE DFKFGKILGE GSFSTVVLAR ELATSREYAT RANSFVGTAQ 130 140 150 160 170 180 YVSPELLTEK SACKSSDLWA LGCIIYQLVA GLPPFRAGNE YLIFQKIIKL EYDFPEKFFP 190 200 210 220 230 240 KARDLVEKLL VLDATKRLGC EEMEGYGPLK AHPFFESVTW ENLHQQTPPK LTAYLPAMSE 250 260 270 280 290 300 DDEDCYGNYD NLLSQFGCMQ VSSSSSSHSL SASDTGLPQR SGSNIEQYIH DLDSNSFELD 310 320 330 340 350 360 LQFSEDEKRL LLEKQAGGNP WHQFVENNLI LKMGPVDKRK GLFARRRQLL LTEGPHLYYV 370 380 390 400 410 420 DPVNKVLKGE IPWSQELRPE AKNFKTFFVH TPNRTYYLMD PSGNAHKWCR KIQEVWRQRY QSHPDAAVQ
	Isoform 5 [UniParc]. Checksum: 8D812DCC8CED2998	FASTA	454	50,838
	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 SNSFELDLQF SEDEKRLLLE KQAGGNPCLT GRII

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN PHOSPHORYLATION OF PKB/AKT1.
[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] [Europe PMC] [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] [Europe PMC] [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]	"Homo sapiens protein coding cDNA." Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). Tissue: Brain.
[6]	"The sequence and analysis of duplication-rich human chromosome 16." Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A. Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4). Tissue: Brain, Kidney and Uterus.
[8]	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.
[9]	"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] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF ARG-474, ALTERNATIVE SPLICING.
[10]	"Regulation of protein kinase C zeta by PI 3-kinase and PDK-1." Chou M.M., Hou W., Johnson J., Graham L.K., Lee M.H., Chen C.S., Newton A.C., Schaffhausen B.S., Toker A. Curr. Biol. 8:1069-1077(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF PRKCZ.
[11]	"Phosphorylation and activation of cAMP-dependent protein kinase by phosphoinositide-dependent protein kinase." Cheng X., Ma Y., Moore M., Hemmings B.A., Taylor S.S. Proc. Natl. Acad. Sci. U.S.A. 95:9849-9854(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF PRKACA.
[12]	"Phosphorylation and activation of p70s6k by PDK1." Pullen N., Dennis P.B., Andjelkovic M., Dufner A., Kozma S.C., Hemmings B.A., Thomas G. Science 279:707-710(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF RPS6KB1.
[13]	"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] [Europe PMC] [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.
[14]	"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] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF ALA-277.
[15]	"90-kDa ribosomal S6 kinase is phosphorylated and activated by 3-phosphoinositide-dependent protein kinase-1." Jensen C.J., Buch M.-B., Krag T.O., Hemmings B.A., Gammeltoft S., Froedin M. J. Biol. Chem. 274:27168-27176(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF RPS6KA3.
[16]	"p21-activated kinase (PAK1) is phosphorylated and activated by 3-phosphoinositide-dependent kinase-1 (PDK1)." King C.C., Gardiner E.M., Zenke F.T., Bohl B.P., Newton A.C., Hemmings B.A., Bokoch G.M. J. Biol. Chem. 275:41201-41209(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF PAK1, INTERACTION WITH PAK1.
[17]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-9; SER-241; TYR-373 AND TYR-376, MUTAGENESIS OF TYR-9; TYR-373 AND TYR-376.
[18]	"Regulation of kinase activity of 3-phosphoinositide-dependent protein kinase-1 by binding to 14-3-3." Sato S., Fujita N., Tsuruo T. J. Biol. Chem. 277:39360-39367(2002) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION, INTERACTION WITH YWHAH AND YWHAQ.
[19]	"Multiple phosphoinositide 3-kinase-dependent steps in activation of protein kinase B." Scheid M.P., Marignani P.A., Woodgett J.R. Mol. Cell. Biol. 22:6247-6260(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF PKB/AKT1.
[20]	"Pyk2- and Src-dependent tyrosine phosphorylation of PDK1 regulates focal 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) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION AT TYR-9; TYR-373 AND TYR-376 BY SRC, INTERACTION WITH PTK2B, SUBCELLULAR LOCATION.
[21]	"Peroxisomal targeting as a tool for assaying protein-protein interactions in the living cell: cytokine-independent survival kinase (CISK) binds PDK-1 in vivo in a phosphorylation-dependent manner." Nilsen T., Slagsvold T., Skjerpen C.S., Brech A., Stenmark H., Olsnes S. J. Biol. Chem. 279:4794-4801(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF SGK3, INTERACTION WITH SGK3.
[22]	"The adaptor protein Grb14 regulates the localization of 3-phosphoinositide-dependent kinase-1." King C.C., Newton A.C. J. Biol. Chem. 279:37518-37527(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH GRB14.
[23]	"PDK1 acquires PDK2 activity in the presence of a synthetic peptide derived from the carboxyl terminus of PRK2." Balendran A., Casamayor A., Deak M., Paterson A., Gaffney P., Currie R., Downes C.P., Alessi D.R. Curr. Biol. 9:393-404(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF AKT1, INTERACTION WITH PKN2.
[24]	"PDK1, the master regulator of AGC kinase signal transduction." Mora A., Komander D., van Aalten D.M., Alessi D.R. Semin. Cell Dev. Biol. 15:161-170(2004) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION.
[25]	"3-Phosphoinositide-dependent protein kinase-1-mediated IkappaB kinase beta (IkkB) phosphorylation activates NF-kappaB signaling." Tanaka H., Fujita N., Tsuruo T. J. Biol. Chem. 280:40965-40973(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF IKKB, INTERACTION WITH IKKB.
[26]	"Regulation of transforming growth factor-beta signaling and PDK1 kinase activity by physical interaction between PDK1 and serine-threonine kinase receptor-associated protein." Seong H.A., Jung H., Choi H.S., Kim K.T., Ha H. J. Biol. Chem. 280:42897-42908(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ENZYME REGULATION, INTERACTION WITH STRAP.
[27]	"Phosphoinositide-dependent phosphorylation of PDK1 regulates nuclear translocation." Scheid M.P., Parsons M., Woodgett J.R. Mol. Cell. Biol. 25:2347-2363(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-396, SUBCELLULAR LOCATION.
[28]	"Tyrosine phosphorylation of phosphoinositide-dependent kinase 1 by the 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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-9; TYR-373 AND TYR-376 BY INSR, INTERACTION WITH INSR.
[29]	"3-Phosphoinositide-dependent PDK1 negatively regulates transforming growth factor-beta-induced signaling in a kinase-dependent manner through physical interaction with Smad proteins." Seong H.A., Jung H., Kim K.T., Ha H. J. Biol. Chem. 282:12272-12289(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SMAD2; SMAD3; SMAD4 AND SMAD7.
[30]	"Essential role of PDK1 in regulating endothelial cell migration." Primo L., di Blasio L., Roca C., Droetto S., Piva R., Schaffhausen B., Bussolino F. J. Cell Biol. 176:1035-1047(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[31]	"The C-terminus of PRK2/PKNgamma is required for optimal activation by RhoA in a GTP-dependent manner." Lim W.G., Chen X., Liu J.P., Tan B.J., Zhou S., Smith A., Lees N., Hou L., Gu F., Yu X.Y., Du Y., Smith D., Verma C., Liu K., Duan W. Arch. Biochem. Biophys. 479:170-178(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF PKN2.
[32]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NPRL2, ENZYME REGULATION.
[33]	"Dissecting the role of the 3-phosphoinositide-dependent protein kinase-1 (PDK1) signalling pathways." Bayascas J.R. Cell Cycle 7:2978-2982(2008) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION.
[34]	"Regulation of 3-phosphoinositide-dependent protein kinase-1 (PDK1) by Src involves tyrosine phosphorylation of PDK1 and Src homology 2 domain binding." Yang K.J., Shin S., Piao L., Shin E., Li Y., Park K.A., Byun H.S., Won M., Hong J., Kweon G.R., Hur G.M., Seok J.H., Chun T., Brazil D.P., Hemmings B.A., Park J. J. Biol. Chem. 283:1480-1491(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SRC; RASA1 AND CRK, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[35]	"The nuclear localization of 3'-phosphoinositide-dependent kinase-1 is dependent on its association with the protein tyrosine phosphatase SHP-1." Sephton C.F., Zhang D., Lehmann T.M., Pennington P.R., Scheid M.P., Mousseau D.D. Cell. Signal. 21:1634-1644(2009) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PTPN6.
[36]	"IGF-I regulated phosphorylation and translocation of PDK-1 in neurons." Alajajian B.B., Fletcher L., Isgor E., Jimenez D.F., Digicaylioglu M. NeuroReport 20:579-583(2009) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[37]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[38]	"PDK1 phosphorylation at Thr354 by murine protein serine/threonine kinase 38 contributes to the negative regulation of PDK1 activity." Seong H.A., Jung H., Manoharan R., Ha H. J. Biol. Chem. 287:20811-20822(2012) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-354 BY MELK, PHOSPHORYLATION AT SER-394 AND SER-398 BY MAP3K5, MUTAGENESIS OF THR-354; SER-394 AND SER-398.
[39]	"Ubiquitin-specific protease 4 inhibits mono-ubiquitination of the master growth factor signaling kinase PDK1." Uras I.Z., List T., Nijman S.M. PLoS ONE 7:E31003-E31003(2012) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION, DEUBIQUITINATION BY USP4.
[40]	"Regulation of 3-phosphoinositide-dependent protein kinase 1 activity by homodimerization in live cells." Masters T.A., Calleja V., Armoogum D.A., Marsh R.J., Applebee C.J., Laguerre M., Bain A.J., Larijani B. Sci. Signal. 3:RA78-RA78(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 409-556, SUBUNIT, ENZYME REGULATION, MUTAGENESIS OF THR-513.
+	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.
AB209835 mRNA. Translation: BAD93072.1. Different initiation.
AC093525 Genomic DNA. No translation available.
AC141586 Genomic DNA. No translation available.
BC006339 mRNA. Translation: AAH06339.2.
BC012103 mRNA. Translation: AAH12103.1.
BC033494 mRNA. Translation: AAH33494.1.

IPI

IPI00002538.
IPI00216646.
IPI00216647.
IPI00867720.

RefSeq

NP_001248745.1. NM_001261816.1.
NP_002604.1. NM_002613.4.
NP_112558.2. NM_031268.5.

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	[»]
2XCH	X-ray	2.00	A	51-359	[»]
2XCK	X-ray	2.30	A	51-359	[»]
3H9O	X-ray	2.30	A	51-359	[»]
3HRC	X-ray	1.91	A	50-359	[»]
3HRF	X-ray	1.90	A	50-359	[»]
3ION	X-ray	2.40	A	48-359	[»]
3IOP	X-ray	2.20	A	48-359	[»]
3NAX	X-ray	1.75	A	66-362	[»]
3NAY	X-ray	2.60	A/B	66-362	[»]
3NUN	X-ray	2.20	A	67-358	[»]
3NUS	X-ray	2.75	A	73-358	[»]
3NUU	X-ray	1.98	A	73-358	[»]
3NUY	X-ray	2.10	A	73-358	[»]
3ORX	X-ray	2.20	A/B/C/D/E/F/G/H	51-359	[»]
3ORZ	X-ray	2.00	A/B/C/D	51-359	[»]
3OTU	X-ray	2.10	A	51-359	[»]
3PWY	X-ray	3.50	A	51-359	[»]
3QC4	X-ray	1.80	A/B	51-359	[»]
3QCQ	X-ray	2.50	A	48-359	[»]
3QCS	X-ray	2.49	A	48-359	[»]
3QCX	X-ray	2.30	A	48-359	[»]
3QCY	X-ray	2.20	A	48-359	[»]
3QD0	X-ray	1.99	A	48-359	[»]
3QD3	X-ray	2.00	A	48-359	[»]
3QD4	X-ray	2.30	A	48-359	[»]
3RCJ	X-ray	1.70	A	50-359	[»]
3RWP	X-ray	1.92	A	51-359	[»]
3RWQ	X-ray	2.55	A	50-359	[»]
3SC1	X-ray	2.70	A	50-359	[»]
4A06	X-ray	2.00	A	50-359	[»]
4A07	X-ray	1.85	A	50-359	[»]
4AW0	X-ray	1.43	A	50-359	[»]
4AW1	X-ray	1.68	A	50-359	[»]

ProteinModelPortal

O15530.

ModBase

Search...

Protein-protein interaction databases

IntAct

O15530. 19 interactions.

MINT

MINT-203926.

STRING

9606.ENSP00000344220.

PTM databases

PhosphoSite

O15530.

Proteomic databases

PaxDb

O15530.

PRIDE

O15530.

Protocols and materials databases

DNASU

5170.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000268673; ENSP00000268673; ENSG00000140992.
ENST00000342085; ENSP00000344220; ENSG00000140992.
ENST00000441549; ENSP00000395357; ENSG00000140992.

GeneID

5170.

KEGG

hsa:5170.

UCSC

uc002cqs.3. human.

Organism-specific databases

CTD

5170.

GeneCards

GC16P002587.

H-InvDB

HIX0038570.
HIX0038793.

HGNC

HGNC:8816. PDPK1.

HPA

CAB004272.

MIM

605213. gene.

neXtProt

NX_O15530.

PharmGKB

PA33160.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000233026.

HOVERGEN

HBG098357.

InParanoid

O15530.

KO

K06276.

OMA

HLQTPPK.

OrthoDB

EOG4ZPDVM.

PhylomeDB

O15530.

Enzyme and pathway databases

BRENDA

2.7.11.1. 2681.

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_111102. Signal Transduction.
REACT_116125. Disease.
REACT_13685. Neuronal System.
REACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

O15530.

Bgee

O15530.

CleanEx

HS_PDK1.
HS_PDPK1.

Genevestigator

O15530.

GermOnline

ENSG00000140992. Homo sapiens.

Family and domain databases

Gene3D

2.30.29.30. 2 hits.

InterPro

IPR011009. Kinase-like_dom.
IPR011993. PH_like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]

Pfam

PF00069. Pkinase. 1 hit.
[Graphical view]

SMART

SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

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

Search...

Other

BindingDB

O15530.

ChEMBL

CHEMBL2534.

ChiTaRS

PDPK1. human.

DrugBank

DB00482. Celecoxib.

EvolutionaryTrace

O15530.

GenomeRNAi

5170.

NextBio

20004.

SOURCE

Search...

Entry information

Entry name

PDPK1_HUMAN

Accession

Primary (citable) accession number: O15530
Secondary accession number(s): H0Y4Z0 , Q59EH6, Q6FI20, Q8IV52, Q9BRD5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 18, 2001
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 152 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.