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Q9Z2A0

- PDPK1_MOUSE

UniProt

Q9Z2A0 - PDPK1_MOUSE

Protein

3-phosphoinositide-dependent protein kinase 1

Gene

Pdpk1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 2 (18 Oct 2001)
      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.8 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-376 and Tyr-379 residues. The 14-3-3 protein YWHAQ acts as a negative regulator by association with the residues surrounding the Ser-244 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-376 and Tyr-379 by INSR in response to insulin By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei114 – 1141ATPPROSITE-ProRule annotation
    Active sitei208 – 2081Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi91 – 999ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. 3-phosphoinositide-dependent protein kinase activity Source: MGI
    2. ATP binding Source: UniProtKB-KW

    GO - Biological processi

    1. activation of protein kinase B activity Source: Ensembl
    2. cellular response to insulin stimulus Source: Ensembl
    3. extrinsic apoptotic signaling pathway Source: Ensembl
    4. focal adhesion assembly Source: Ensembl
    5. hyperosmotic response Source: MGI
    6. intracellular signal transduction Source: Ensembl
    7. negative regulation of cardiac muscle cell apoptotic process Source: UniProtKB
    8. negative regulation of protein kinase activity Source: Ensembl
    9. negative regulation of toll-like receptor signaling pathway Source: UniProtKB
    10. negative regulation of transforming growth factor beta receptor signaling pathway Source: Ensembl
    11. peptidyl-threonine phosphorylation Source: Ensembl
    12. positive regulation of establishment of protein localization to plasma membrane Source: Ensembl
    13. regulation of endothelial cell migration Source: UniProtKB
    14. regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
    15. regulation of mast cell degranulation Source: UniProtKB
    16. regulation of transcription, DNA-templated Source: UniProtKB-KW
    17. signal transduction Source: MGI
    18. transcription, DNA-templated Source: UniProtKB-KW
    19. type B pancreatic cell development Source: UniProtKB

    Keywords - Molecular functioni

    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. 3474.
    ReactomeiREACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_198245. RSK activation.
    REACT_205561. FCERI mediated NF-kB activation.
    REACT_213364. Role of LAT2/NTAL/LAB on calcium mobilization.
    REACT_220092. GPVI-mediated activation cascade.
    REACT_223974. G beta:gamma signalling through PI3Kgamma.
    REACT_225145. Downstream TCR signaling.
    REACT_226151. CD28 dependent PI3K/Akt signaling.
    REACT_226341. PIP3 activates AKT signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3-phosphoinositide-dependent protein kinase 1 (EC:2.7.11.1)
    Short name:
    mPDK1
    Gene namesi
    Name:Pdpk1
    Synonyms:Pdk1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:1338068. Pdpk1.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus By similarity. Cell membrane 1 Publication; Peripheral membrane protein 1 Publication. Cell junctionfocal adhesion By similarity
    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-244 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 By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. cytoplasmic membrane-bounded vesicle Source: MGI
    3. cytosol Source: Ensembl
    4. focal adhesion Source: UniProtKB-SubCell
    5. nucleus Source: UniProtKB-SubCell
    6. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Mice show severe pancreatic hypoplasia at birth and ensuing hyperglycemia at postnatal stages and die of heart failure by 11 weeks of age.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 5595593-phosphoinositide-dependent protein kinase 1PRO_0000086501Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei9 – 91Phosphotyrosine; by SRC and INSRBy similarity
    Modified residuei25 – 251PhosphoserineBy similarity
    Modified residuei244 – 2441Phosphoserine; alternate1 Publication
    Modified residuei244 – 2441Phosphoserine; by autocatalysis; alternateBy similarity
    Modified residuei307 – 3071N6-acetyllysine1 Publication
    Modified residuei357 – 3571Phosphothreonine; by MELKBy similarity
    Modified residuei376 – 3761Phosphotyrosine; by SRC and INSRBy similarity
    Modified residuei379 – 3791Phosphotyrosine; by SRC and INSRBy similarity
    Modified residuei396 – 3961PhosphoserineBy similarity
    Modified residuei397 – 3971Phosphoserine; by MAP3K5By similarity
    Modified residuei399 – 3991PhosphoserineBy similarity
    Modified residuei401 – 4011Phosphoserine; by MAP3K5By similarity
    Modified residuei413 – 4131PhosphoserineBy similarity
    Modified residuei504 – 5041Phosphoserine; by PKC/PRKCQ1 Publication
    Modified residuei516 – 5161Phosphothreonine; by autocatalysisBy similarity
    Modified residuei532 – 5321Phosphoserine; by PKC/PRKCQ1 Publication

    Post-translational modificationi

    Phosphorylation on Ser-244 in the activation loop is required for full activity. PDPK1 itself can autophosphorylate Ser-244, 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-376 and Tyr-379 by INSR in response to insulin. Palmitate negatively regulates autophosphorylation at Ser-244 and palmitate-induced phosphorylation at Ser-532 and Ser-504 by PKC/PRKCQ negatively regulates its ability to phosphorylate PKB/AKT1. Phosphorylation at Thr-357 by MELK partially inhibits kinase activity, the inhibition is cooperatively enhanced by phosphorylation at Ser-397 and Ser-401 by MAP3K5 By similarity.By similarity
    Monoubiquitinated in the kinase domain, deubiquitinated by USP4.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9Z2A0.
    PaxDbiQ9Z2A0.
    PRIDEiQ9Z2A0.

    PTM databases

    PhosphoSiteiQ9Z2A0.

    Expressioni

    Tissue specificityi

    Highly expressed in heart, brain, liver and testis, also expressed in embryonic cells.

    Gene expression databases

    ArrayExpressiQ9Z2A0.
    BgeeiQ9Z2A0.
    CleanExiMM_PDK1.
    MM_PDPK1.
    GenevestigatoriQ9Z2A0.

    Interactioni

    Subunit structurei

    Homodimer in its autoinhibited state. Active as monomer. Interacts with NPRL2, PAK1, PTK2B, GRB14, 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-244 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 By similarity. Interacts with PKN1 (via C-terminus) and PPARG.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi202099. 1 interaction.
    IntActiQ9Z2A0. 21 interactions.
    MINTiMINT-4106940.
    STRINGi10090.ENSMUSP00000099991.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Z2A0.
    SMRiQ9Z2A0. Positions 45-552.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini85 – 345261Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini462 – 55392PHAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi392 – 40110Poly-Ser

    Domaini

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

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00550000074819.
    HOGENOMiHOG000233026.
    HOVERGENiHBG098357.
    InParanoidiA6H6U3.
    KOiK06276.
    OMAiSEDMHIQ.
    OrthoDBiEOG7R56S4.
    PhylomeDBiQ9Z2A0.
    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]

    Sequencei

    Sequence statusi: Complete.

    Q9Z2A0-1 [UniParc]FASTAAdd to Basket

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    MARTTSQLYD AVPIQSSVVL CSCPSPSMVR SQTEPGSSPG IPSGVSRQGS    50
    TMDGTTAEAR PSTNPLQQHP AQLPPQPRKK RPEDFKFGKI LGEGSFSTVV 100
    LARELATSRE YAIKILEKRH IIKENKVPYV TRERDVMSRL DHPFFVKLYF 150
    TFQDDEKLYF GLSYAKNGEL LKYIRKIGSF DETCTRFYTA EIVSALEYLH 200
    GKGIIHRDLK PENILLNEDM HIQITDFGTA KVLSPESKQA RANSFVGTAQ 250
    YVSPELLTEK SACKSSDLWA LGCIIYQLVA GLPPFRAGNE YLIFQKIIKL 300
    EYHFPEKFFP KARDLVEKLL VLDATKRLGC EEMEGYGPLK AHPFFETITW 350
    ENLHQQTPPK LTAYLPAMSE DDEDCYGNYD NLLSQFGFMQ VSSSSSSHSL 400
    STVETSLPQR SGSNIEQYIH DLDTNSFELD LQFSEDEKRL LLEKQAGGNP 450
    WHQFVENNLI LKMGPVDKRK GLFARRRQLL LTEGPHLYYV DPVNKVLKGE 500
    IPWSQELRPE AKNFKTFFVH TPNRTYYLMD PSGNAHKWCR KIQEVWRQQY 550
    QSNPDAAVQ 559
    Length:559
    Mass (Da):63,759
    Last modified:October 18, 2001 - v2
    Checksum:iF2A617A27460FAC9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti84 – 841D → N in AAC67544. (PubMed:10075713)Curated
    Sequence conflicti248 – 2481T → P in AAC96115. 1 PublicationCurated
    Sequence conflicti285 – 2851F → S in AAC96115. 1 PublicationCurated
    Sequence conflicti546 – 5461W → R in AAC96115. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF086625 mRNA. Translation: AAC67544.1.
    AF126294 mRNA. Translation: AAD38505.1.
    AF079535 mRNA. Translation: AAC96115.1.
    BC146001 mRNA. Translation: AAI46002.1.
    BC146003 mRNA. Translation: AAI46004.1.
    CCDSiCCDS28474.1.
    RefSeqiNP_035192.2. NM_011062.4.
    UniGeneiMm.10504.

    Genome annotation databases

    EnsembliENSMUST00000102927; ENSMUSP00000099991; ENSMUSG00000024122.
    GeneIDi18607.
    KEGGimmu:18607.
    UCSCiuc008auk.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF086625 mRNA. Translation: AAC67544.1 .
    AF126294 mRNA. Translation: AAD38505.1 .
    AF079535 mRNA. Translation: AAC96115.1 .
    BC146001 mRNA. Translation: AAI46002.1 .
    BC146003 mRNA. Translation: AAI46004.1 .
    CCDSi CCDS28474.1.
    RefSeqi NP_035192.2. NM_011062.4.
    UniGenei Mm.10504.

    3D structure databases

    ProteinModelPortali Q9Z2A0.
    SMRi Q9Z2A0. Positions 45-552.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202099. 1 interaction.
    IntActi Q9Z2A0. 21 interactions.
    MINTi MINT-4106940.
    STRINGi 10090.ENSMUSP00000099991.

    PTM databases

    PhosphoSitei Q9Z2A0.

    Proteomic databases

    MaxQBi Q9Z2A0.
    PaxDbi Q9Z2A0.
    PRIDEi Q9Z2A0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000102927 ; ENSMUSP00000099991 ; ENSMUSG00000024122 .
    GeneIDi 18607.
    KEGGi mmu:18607.
    UCSCi uc008auk.2. mouse.

    Organism-specific databases

    CTDi 5170.
    MGIi MGI:1338068. Pdpk1.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00550000074819.
    HOGENOMi HOG000233026.
    HOVERGENi HBG098357.
    InParanoidi A6H6U3.
    KOi K06276.
    OMAi SEDMHIQ.
    OrthoDBi EOG7R56S4.
    PhylomeDBi Q9Z2A0.
    TreeFami TF105423.

    Enzyme and pathway databases

    BRENDAi 2.7.11.1. 3474.
    Reactomei REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_198245. RSK activation.
    REACT_205561. FCERI mediated NF-kB activation.
    REACT_213364. Role of LAT2/NTAL/LAB on calcium mobilization.
    REACT_220092. GPVI-mediated activation cascade.
    REACT_223974. G beta:gamma signalling through PI3Kgamma.
    REACT_225145. Downstream TCR signaling.
    REACT_226151. CD28 dependent PI3K/Akt signaling.
    REACT_226341. PIP3 activates AKT signaling.

    Miscellaneous databases

    ChiTaRSi PDPK1. mouse.
    NextBioi 294526.
    PROi Q9Z2A0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Z2A0.
    Bgeei Q9Z2A0.
    CleanExi MM_PDK1.
    MM_PDPK1.
    Genevestigatori Q9Z2A0.

    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. "Primary structure, tissue distribution, and expression of mouse phosphoinositide-dependent protein kinase-1, a protein kinase that phosphorylates and activates protein kinase C zeta."
      Dong L.Q., Zhang R.-B., Langlais P., He H., Clark M., Zhu L., Liu F.
      J. Biol. Chem. 274:8117-8122(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "Mouse phosphoinositide-dependent protein kinase 1 (mPDK1)."
      Park J., Hemmings B.A.
      Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    3. Xu P., Taylor S.
      Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6.
    4. "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].
      Tissue: Brain.
    5. "Phosphorylation of protein kinase N by phosphoinositide-dependent protein kinase-1 mediates insulin signals to the actin cytoskeleton."
      Dong L.Q., Landa L.R., Wick M.J., Zhu L., Mukai H., Ono Y., Liu F.
      Proc. Natl. Acad. Sci. U.S.A. 97:5089-5094(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF PKN1 AND PKN2, INTERACTION WITH PKN1 AND PKN2.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic brain.
    7. "3-phosphoinositide-dependent protein kinase-1 activates the peroxisome proliferator-activated receptor-gamma and promotes adipocyte differentiation."
      Yin Y., Yuan H., Wang C., Pattabiraman N., Rao M., Pestell R.G., Glazer R.I.
      Mol. Endocrinol. 20:268-278(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PPARG.
    8. "Notch-induced T cell development requires phosphoinositide-dependent kinase 1."
      Kelly A.P., Finlay D.K., Hinton H.J., Clarke R.G., Fiorini E., Radtke F., Cantrell D.A.
      EMBO J. 26:3441-3450(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "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.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    11. "Pdk1 activity controls proliferation, survival, and growth of developing pancreatic cells."
      Westmoreland J.J., Wang Q., Bouzaffour M., Baker S.J., Sosa-Pineda B.
      Dev. Biol. 334:285-298(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    12. "Protein kinase C theta (PKCtheta)-dependent phosphorylation of PDK1 at Ser504 and Ser532 contributes to palmitate-induced insulin resistance."
      Wang C., Liu M., Riojas R.A., Xin X., Gao Z., Zeng R., Wu J., Dong L.Q., Liu F.
      J. Biol. Chem. 284:2038-2044(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-504 AND SER-532 BY PKC/PRKCQ.
    13. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    14. "Phosphoinositide-dependent kinase PDK1 in the regulation of Ca2+ entry into mast cells."
      Shumilina E., Zemtsova I.M., Heise N., Schmid E., Eichenmueller M., Tyan L., Rexhepaj R., Lang F.
      Cell. Physiol. Biochem. 26:699-706(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "Phosphoinositide-dependent kinase 1 provides negative feedback inhibition to Toll-like receptor-mediated NF-kappaB activation in macrophages."
      Chaurasia B., Mauer J., Koch L., Goldau J., Kock A.S., Bruening J.C.
      Mol. Cell. Biol. 30:4354-4366(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-307, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiPDPK1_MOUSE
    AccessioniPrimary (citable) accession number: Q9Z2A0
    Secondary accession number(s): A6H6U3, Q9R1D8, Q9R215
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 18, 2001
    Last sequence update: October 18, 2001
    Last modified: October 1, 2014
    This is version 131 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3