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O15530

- PDPK1_HUMAN

UniProt

O15530 - PDPK1_HUMAN

Protein

3-phosphoinositide-dependent protein kinase 1

Gene

PDPK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 168 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    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.15 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    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.4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei111 – 1111ATPPROSITE-ProRule annotation
    Active sitei205 – 2051Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi88 – 969ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. 3-phosphoinositide-dependent protein kinase activity Source: BHF-UCL
    2. ATP binding Source: UniProtKB-KW
    3. kinase activity Source: Reactome
    4. phospholipase activator activity Source: BHF-UCL
    5. phospholipase binding Source: BHF-UCL
    6. protein binding Source: IntAct
    7. protein serine/threonine kinase activity Source: BHF-UCL

    GO - Biological processi

    1. actin cytoskeleton organization Source: ProtInc
    2. activation of protein kinase B activity Source: BHF-UCL
    3. blood coagulation Source: Reactome
    4. calcium-mediated signaling Source: BHF-UCL
    5. cell migration Source: BHF-UCL
    6. cellular response to epidermal growth factor stimulus Source: BHF-UCL
    7. cellular response to insulin stimulus Source: BHF-UCL
    8. epidermal growth factor receptor signaling pathway Source: BHF-UCL
    9. extrinsic apoptotic signaling pathway Source: UniProtKB
    10. Fc-epsilon receptor signaling pathway Source: Reactome
    11. fibroblast growth factor receptor signaling pathway Source: Reactome
    12. focal adhesion assembly Source: Ensembl
    13. hyperosmotic response Source: Ensembl
    14. innate immune response Source: Reactome
    15. insulin receptor signaling pathway Source: Reactome
    16. intracellular signal transduction Source: MGI
    17. negative regulation of cardiac muscle cell apoptotic process Source: Ensembl
    18. negative regulation of protein kinase activity Source: BHF-UCL
    19. negative regulation of toll-like receptor signaling pathway Source: Ensembl
    20. negative regulation of transforming growth factor beta receptor signaling pathway Source: UniProtKB
    21. neurotrophin TRK receptor signaling pathway Source: Reactome
    22. peptidyl-threonine phosphorylation Source: BHF-UCL
    23. phosphatidylinositol-mediated signaling Source: Reactome
    24. platelet activation Source: Reactome
    25. positive regulation of establishment of protein localization to plasma membrane Source: BHF-UCL
    26. positive regulation of phospholipase activity Source: BHF-UCL
    27. positive regulation of release of sequestered calcium ion into cytosol Source: BHF-UCL
    28. protein autophosphorylation Source: UniProtKB
    29. protein phosphorylation Source: UniProtKB
    30. regulation of endothelial cell migration Source: Ensembl
    31. regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    32. regulation of mast cell degranulation Source: Ensembl
    33. regulation of transcription, DNA-templated Source: UniProtKB-KW
    34. synaptic transmission Source: Reactome
    35. T cell costimulation Source: Reactome
    36. T cell receptor signaling pathway Source: Reactome
    37. transcription, DNA-templated Source: UniProtKB-KW
    38. type B pancreatic cell development Source: Ensembl

    Keywords - Molecular functioni

    Activator, Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.1. 2681.
    ReactomeiREACT_12555. Downstream TCR signaling.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_15523. Integrin alphaIIb beta3 signaling.
    REACT_163769. Role of LAT2/NTAL/LAB on calcium mobilization.
    REACT_163994. FCERI mediated NF-kB activation.
    REACT_1695. GPVI-mediated activation cascade.
    REACT_19290. G beta:gamma signalling through PI3Kgamma.
    REACT_19358. CD28 dependent PI3K/Akt signaling.
    REACT_19405. CTLA4 inhibitory signaling.
    REACT_20510. RSK activation.
    REACT_75829. PIP3 activates AKT signaling.
    REACT_790. Activation of PKB.
    SignaLinkiO15530.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3-phosphoinositide-dependent protein kinase 1 (EC:2.7.11.1)
    Short name:
    hPDK1
    Gene namesi
    Name:PDPK1
    Synonyms:PDK1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:8816. PDPK1.

    Subcellular locationi

    Cytoplasm. Nucleus. Cell membrane; Peripheral membrane protein. Cell junctionfocal 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.

    GO - Cellular componenti

    1. cell projection Source: BHF-UCL
    2. cytoplasm Source: UniProtKB
    3. cytoplasmic membrane-bounded vesicle Source: Ensembl
    4. cytosol Source: Reactome
    5. focal adhesion Source: UniProtKB-SubCell
    6. nucleoplasm Source: Reactome
    7. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi9 – 91Y → F: Slight reduction in pervanadate-stimulated tyrosine phosphorylation. 1 Publication
    Mutagenesisi25 – 251S → A: No effect. 1 Publication
    Mutagenesisi241 – 2411S → A: No activation. 1 Publication
    Mutagenesisi277 – 2771A → V: 3-fold increase in kinase activity. 1 Publication
    Mutagenesisi354 – 3541T → A: Abolishes phosphorylation by MELK. 1 Publication
    Mutagenesisi373 – 3731Y → F: Reduction in basal activity. 1 Publication
    Mutagenesisi376 – 3761Y → F: Reduction in basal activity. 1 Publication
    Mutagenesisi393 – 3931S → A: No effect. 1 Publication
    Mutagenesisi394 – 3941S → A: Abolishes phosphorylation by MAP3K5; when associated with A-398. 1 Publication
    Mutagenesisi396 – 3961S → A: No effect. 1 Publication
    Mutagenesisi398 – 3981S → A: Abolishes phosphorylation by MAP3K5; when associated with A-394. 1 Publication
    Mutagenesisi410 – 4101S → A: No effect. 1 Publication
    Mutagenesisi474 – 4741R → A: No PDGF-dependent translocation to the membrane. 1 Publication
    Mutagenesisi513 – 5131T → E: Enhanced kinase activity towards PKB. 1 Publication

    Organism-specific databases

    PharmGKBiPA33160.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 5565563-phosphoinositide-dependent protein kinase 1PRO_0000086500Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei9 – 91Phosphotyrosine; by SRC and INSR3 Publications
    Modified residuei25 – 251Phosphoserine1 Publication
    Modified residuei241 – 2411Phosphoserine; by autocatalysis4 Publications
    Modified residuei304 – 3041N6-acetyllysineBy similarity
    Modified residuei354 – 3541Phosphothreonine; by MELK1 Publication
    Modified residuei373 – 3731Phosphotyrosine; by SRC and INSR3 Publications
    Modified residuei376 – 3761Phosphotyrosine; by SRC and INSR3 Publications
    Modified residuei393 – 3931Phosphoserine1 Publication
    Modified residuei394 – 3941Phosphoserine; by MAP3K51 Publication
    Modified residuei396 – 3961Phosphoserine2 Publications
    Modified residuei398 – 3981Phosphoserine; by MAP3K51 Publication
    Modified residuei410 – 4101Phosphoserine1 Publication
    Modified residuei501 – 5011Phosphoserine; by PKC/PRKCQBy similarity
    Modified residuei513 – 5131Phosphothreonine; by autocatalysis1 Publication
    Modified residuei529 – 5291Phosphoserine; by PKC/PRKCQBy similarity

    Post-translational modificationi

    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.By similarity8 Publications
    Autophosphorylated; autophosphorylation is inhibited by the apoptotic C-terminus cleavage product of PKN2.By similarity
    Monoubiquitinated in the kinase domain, deubiquitinated by USP4.

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiO15530.
    PaxDbiO15530.
    PRIDEiO15530.

    PTM databases

    PhosphoSiteiO15530.

    Expressioni

    Tissue specificityi

    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.1 Publication

    Inductioni

    Stimulated by insulin, and the oxidants hydrogen peroxide and peroxovanadate.

    Gene expression databases

    ArrayExpressiO15530.
    BgeeiO15530.
    CleanExiHS_PDK1.
    HS_PDPK1.
    GenevestigatoriO15530.

    Organism-specific databases

    HPAiCAB004272.
    HPA035199.

    Interactioni

    Subunit structurei

    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.14 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AKT1P317493EBI-717097,EBI-296087
    PPP2R2BQ000058EBI-717097,EBI-1052159
    ZDHHC17Q8IUH53EBI-9087775,EBI-524753

    Protein-protein interaction databases

    BioGridi111196. 47 interactions.
    IntActiO15530. 47 interactions.
    MINTiMINT-1371493.
    STRINGi9606.ENSP00000344220.

    Structurei

    Secondary structure

    1
    556
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi79 – 813
    Beta strandi82 – 9110
    Beta strandi94 – 1018
    Turni102 – 1043
    Beta strandi107 – 1148
    Helixi115 – 1206
    Helixi124 – 13411
    Beta strandi145 – 1506
    Beta strandi152 – 1598
    Beta strandi163 – 1664
    Helixi167 – 1748
    Helixi179 – 19820
    Helixi208 – 2103
    Beta strandi211 – 2133
    Beta strandi219 – 2213
    Helixi224 – 2263
    Turni232 – 2354
    Beta strandi238 – 2403
    Helixi246 – 2483
    Helixi251 – 2566
    Helixi261 – 27717
    Helixi287 – 29610
    Beta strandi303 – 3053
    Helixi307 – 31610
    Helixi321 – 3233
    Helixi328 – 3303
    Helixi333 – 3375
    Helixi340 – 3423
    Helixi347 – 3493
    Helixi350 – 3523
    Helixi412 – 4154
    Beta strandi416 – 4205
    Beta strandi423 – 4264
    Helixi432 – 44514
    Helixi449 – 4513
    Turni452 – 4543
    Beta strandi457 – 46711
    Beta strandi470 – 47910
    Turni480 – 4823
    Beta strandi483 – 4886
    Turni489 – 4924
    Beta strandi493 – 4986
    Beta strandi505 – 51814
    Beta strandi521 – 5266
    Helixi532 – 54716

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1H1WX-ray2.00A71-359[»]
    1OKYX-ray2.30A51-360[»]
    1OKZX-ray2.51A51-360[»]
    1UU3X-ray1.70A51-360[»]
    1UU7X-ray1.90A51-360[»]
    1UU8X-ray2.50A51-360[»]
    1UU9X-ray1.95A72-357[»]
    1UVRX-ray2.81A71-359[»]
    1W1DX-ray1.50A409-556[»]
    1W1GX-ray1.45A409-556[»]
    1W1HX-ray1.45A/B/C/D409-556[»]
    1Z5MX-ray2.17A74-359[»]
    2BIYX-ray1.95A51-360[»]
    2PE0X-ray2.35A74-359[»]
    2PE1X-ray2.14A74-359[»]
    2PE2X-ray2.13A74-359[»]
    2R7BX-ray2.70A48-359[»]
    2VKIX-ray1.80A409-556[»]
    2XCHX-ray2.00A51-359[»]
    2XCKX-ray2.30A51-359[»]
    3H9OX-ray2.30A51-359[»]
    3HRCX-ray1.91A50-359[»]
    3HRFX-ray1.90A50-359[»]
    3IONX-ray2.40A48-359[»]
    3IOPX-ray2.20A48-359[»]
    3NAXX-ray1.75A66-362[»]
    3NAYX-ray2.60A/B66-362[»]
    3NUNX-ray2.20A67-358[»]
    3NUSX-ray2.75A73-358[»]
    3NUUX-ray1.98A73-358[»]
    3NUYX-ray2.10A73-358[»]
    3ORXX-ray2.20A/B/C/D/E/F/G/H51-359[»]
    3ORZX-ray2.00A/B/C/D51-359[»]
    3OTUX-ray2.10A51-359[»]
    3PWYX-ray3.50A51-359[»]
    3QC4X-ray1.80A/B51-359[»]
    3QCQX-ray2.50A48-359[»]
    3QCSX-ray2.49A48-359[»]
    3QCXX-ray2.30A48-359[»]
    3QCYX-ray2.20A48-359[»]
    3QD0X-ray1.99A48-359[»]
    3QD3X-ray2.00A48-359[»]
    3QD4X-ray2.30A48-359[»]
    3RCJX-ray1.70A50-359[»]
    3RWPX-ray1.92A51-359[»]
    3RWQX-ray2.55A51-359[»]
    3SC1X-ray2.70A50-359[»]
    4A06X-ray2.00A50-359[»]
    4A07X-ray1.85A50-359[»]
    4AW0X-ray1.43A51-359[»]
    4AW1X-ray1.68A51-359[»]
    4CT1X-ray1.85A50-359[»]
    4CT2X-ray1.25A50-359[»]
    ProteinModelPortaliO15530.
    SMRiO15530. Positions 75-556.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO15530.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini82 – 342261Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini459 – 55092PHAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi389 – 39810Poly-Ser

    Domaini

    The PH domain plays a pivotal role in the localization and nuclear import of PDPK1 and is also essential for its homodimerization.

    Sequence similaritiesi

    Contains 1 PH domain.Curated
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000233026.
    HOVERGENiHBG098357.
    InParanoidiO15530.
    KOiK06276.
    OMAiSEDMHIQ.
    OrthoDBiEOG7R56S4.
    PhylomeDBiO15530.
    TreeFamiTF105423.

    Family and domain databases

    Gene3Di2.30.29.30. 2 hits.
    InterProiIPR011009. Kinase-like_dom.
    IPR011993. PH_like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O15530-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MARTTSQLYD AVPIQSSVVL CSCPSPSMVR TQTESSTPPG IPGGSRQGPA    50
    MDGTAAEPRP GAGSLQHAQP PPQPRKKRPE DFKFGKILGE GSFSTVVLAR 100
    ELATSREYAI KILEKRHIIK ENKVPYVTRE RDVMSRLDHP FFVKLYFTFQ 150
    DDEKLYFGLS YAKNGELLKY IRKIGSFDET CTRFYTAEIV SALEYLHGKG 200
    IIHRDLKPEN ILLNEDMHIQ ITDFGTAKVL SPESKQARAN SFVGTAQYVS 250
    PELLTEKSAC KSSDLWALGC IIYQLVAGLP PFRAGNEYLI FQKIIKLEYD 300
    FPEKFFPKAR DLVEKLLVLD ATKRLGCEEM EGYGPLKAHP FFESVTWENL 350
    HQQTPPKLTA YLPAMSEDDE DCYGNYDNLL SQFGCMQVSS SSSSHSLSAS 400
    DTGLPQRSGS NIEQYIHDLD SNSFELDLQF SEDEKRLLLE KQAGGNPWHQ 450
    FVENNLILKM GPVDKRKGLF ARRRQLLLTE GPHLYYVDPV NKVLKGEIPW 500
    SQELRPEAKN FKTFFVHTPN RTYYLMDPSG NAHKWCRKIQ EVWRQRYQSH 550
    PDAAVQ 556
    Length:556
    Mass (Da):63,152
    Last modified:January 1, 1998 - v1
    Checksum:iED8C0306DC4D0653
    GO
    Isoform 2 (identifier: O15530-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:506
    Mass (Da):58,035
    Checksum:i22D376B8A13FD3F3
    GO
    Isoform 3 (identifier: O15530-3) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:530
    Mass (Da):60,396
    Checksum:iCEAF882CBD3EB1F2
    GO
    Isoform 4 (identifier: O15530-4) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:429
    Mass (Da):48,201
    Checksum:i860C8A8C06161CE1
    GO
    Isoform 5 (identifier: O15530-5) [UniParc]FASTAAdd to Basket

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

    Note: No experimental confirmation available.

    Show »
    Length:454
    Mass (Da):50,838
    Checksum:i8D812DCC8CED2998
    GO

    Sequence cautioni

    The sequence BAD93072.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5050Missing in isoform 2. CuratedVSP_004894Add
    BLAST
    Alternative sequencei110 – 237128IKILE…ESKQA → T in isoform 4. 1 PublicationVSP_041902Add
    BLAST
    Alternative sequencei238 – 26326Missing in isoform 3. 1 PublicationVSP_004895Add
    BLAST
    Alternative sequencei448 – 556109WHQFV…DAAVQ → CLTGRII in isoform 5. 1 PublicationVSP_044796Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS10472.1. [O15530-1]
    CCDS10473.1. [O15530-4]
    CCDS58411.1. [O15530-5]
    RefSeqiNP_001248745.1. NM_001261816.1. [O15530-5]
    NP_002604.1. NM_002613.4. [O15530-1]
    NP_112558.2. NM_031268.5. [O15530-4]
    UniGeneiHs.459691.

    Genome annotation databases

    EnsembliENST00000268673; ENSP00000268673; ENSG00000140992. [O15530-4]
    ENST00000342085; ENSP00000344220; ENSG00000140992. [O15530-1]
    ENST00000441549; ENSP00000395357; ENSG00000140992. [O15530-5]
    GeneIDi5170.
    KEGGihsa:5170.
    UCSCiuc002cqs.4. human. [O15530-1]
    uc002cqt.4. human. [O15530-4]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS10472.1. [O15530-1 ]
    CCDS10473.1. [O15530-4 ]
    CCDS58411.1. [O15530-5 ]
    RefSeqi NP_001248745.1. NM_001261816.1. [O15530-5 ]
    NP_002604.1. NM_002613.4. [O15530-1 ]
    NP_112558.2. NM_031268.5. [O15530-4 ]
    UniGenei Hs.459691.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 51-359 [» ]
    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 51-359 [» ]
    4AW1 X-ray 1.68 A 51-359 [» ]
    4CT1 X-ray 1.85 A 50-359 [» ]
    4CT2 X-ray 1.25 A 50-359 [» ]
    ProteinModelPortali O15530.
    SMRi O15530. Positions 75-556.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111196. 47 interactions.
    IntActi O15530. 47 interactions.
    MINTi MINT-1371493.
    STRINGi 9606.ENSP00000344220.

    Chemistry

    BindingDBi O15530.
    ChEMBLi CHEMBL2534.
    DrugBanki DB00482. Celecoxib.
    GuidetoPHARMACOLOGYi 1519.

    PTM databases

    PhosphoSitei O15530.

    Proteomic databases

    MaxQBi O15530.
    PaxDbi O15530.
    PRIDEi O15530.

    Protocols and materials databases

    DNASUi 5170.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000268673 ; ENSP00000268673 ; ENSG00000140992 . [O15530-4 ]
    ENST00000342085 ; ENSP00000344220 ; ENSG00000140992 . [O15530-1 ]
    ENST00000441549 ; ENSP00000395357 ; ENSG00000140992 . [O15530-5 ]
    GeneIDi 5170.
    KEGGi hsa:5170.
    UCSCi uc002cqs.4. human. [O15530-1 ]
    uc002cqt.4. human. [O15530-4 ]

    Organism-specific databases

    CTDi 5170.
    GeneCardsi GC16P002587.
    H-InvDB HIX0038570.
    HIX0038793.
    HGNCi HGNC:8816. PDPK1.
    HPAi CAB004272.
    HPA035199.
    MIMi 605213. gene.
    neXtProti NX_O15530.
    PharmGKBi PA33160.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233026.
    HOVERGENi HBG098357.
    InParanoidi O15530.
    KOi K06276.
    OMAi SEDMHIQ.
    OrthoDBi EOG7R56S4.
    PhylomeDBi O15530.
    TreeFami TF105423.

    Enzyme and pathway databases

    BRENDAi 2.7.11.1. 2681.
    Reactomei REACT_12555. Downstream TCR signaling.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_15523. Integrin alphaIIb beta3 signaling.
    REACT_163769. Role of LAT2/NTAL/LAB on calcium mobilization.
    REACT_163994. FCERI mediated NF-kB activation.
    REACT_1695. GPVI-mediated activation cascade.
    REACT_19290. G beta:gamma signalling through PI3Kgamma.
    REACT_19358. CD28 dependent PI3K/Akt signaling.
    REACT_19405. CTLA4 inhibitory signaling.
    REACT_20510. RSK activation.
    REACT_75829. PIP3 activates AKT signaling.
    REACT_790. Activation of PKB.
    SignaLinki O15530.

    Miscellaneous databases

    ChiTaRSi PDPK1. human.
    EvolutionaryTracei O15530.
    GeneWikii Phosphoinositide-dependent_kinase-1.
    GenomeRNAii 5170.
    NextBioi 20004.
    PROi O15530.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O15530.
    Bgeei O15530.
    CleanExi HS_PDK1.
    HS_PDPK1.
    Genevestigatori O15530.

    Family and domain databases

    Gene3Di 2.30.29.30. 2 hits.
    InterProi IPR011009. Kinase-like_dom.
    IPR011993. PH_like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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, IDENTIFICATION BY 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. 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. 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. "Role of the PH domain in regulating in vitro autophosphorylation events required for reconstitution of PDK1 catalytic activity."
      Gao X., Harris T.K.
      Bioorg. Chem. 34:200-223(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-241 AND THR-513.
    30. "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.
    31. "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.
    32. "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.
    33. "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.
    34. "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.
    35. "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.
    36. "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.
    37. "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.
    38. "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.
    39. "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.
    40. "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.
    41. "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.

    Entry informationi

    Entry nameiPDPK1_HUMAN
    AccessioniPrimary (citable) accession number: O15530
    Secondary accession number(s): H0Y4Z0
    , Q59EH6, Q6FI20, Q8IV52, Q9BRD5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 18, 2001
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 168 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3