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Q9BZL6

- KPCD2_HUMAN

UniProt

Q9BZL6 - KPCD2_HUMAN

Protein

Serine/threonine-protein kinase D2

Gene

PRKD2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 2 (18 May 2010)
      Previous versions | rss
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    Functioni

    Serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of cell proliferation via MAPK1/3 (ERK1/2) signaling, oxidative stress-induced NF-kappa-B activation, inhibition of HDAC7 transcriptional repression, signaling downstream of T-cell antigen receptor (TCR) and cytokine production, and plays a role in Golgi membrane trafficking, angiogenesis, secretory granule release and cell adhesion. May potentiate mitogenesis induced by the neuropeptide bombesin by mediating an increase in the duration of MAPK1/3 (ERK1/2) signaling, which leads to accumulation of immediate-early gene products including FOS that stimulate cell cycle progression. In response to oxidative stress, is phosphorylated at Tyr-438 by ABL1, which leads to the activation of PRKD2 without increasing its catalytic activity, and mediates activation of NF-kappa-B. In response to the activation of the gastrin receptor CCKBR, is phosphorylated at Ser-244 by CSNK1D and CSNK1E, translocates to the nucleus, phosphorylates HDAC7, leading to nuclear export of HDAC7 and inhibition of HDAC7 transcriptional repression of NR4A1/NUR77. Upon TCR stimulation, is activated independently of ZAP70, translocates from the cytoplasm to the nucleus and is required for interleukin-2 (IL2) promoter up-regulation. During adaptive immune responses, is required in peripheral T-lymphocytes for the production of the effector cytokines IL2 and IFNG after TCR engagement and for optimal induction of antibody responses to antigens. In epithelial cells stimulated with lysophosphatidic acid (LPA), is activated through a PKC-dependent pathway and mediates LPA-stimulated interleukin-8 (IL8) secretion via a NF-kappa-B-dependent pathway. During TCR-induced T-cell activation, interacts with and is activated by the tyrosine kinase LCK, which results in the activation of the NFAT transcription factors. In the trans-Golgi network (TGN), regulates the fission of transport vesicles that are on their way to the plasma membrane and in polarized cells is involved in the transport of proteins from the TGN to the basolateral membrane. Plays an important role in endothelial cell proliferation and migration prior to angiogenesis, partly through modulation of the expression of KDR/VEGFR2 and FGFR1, two key growth factor receptors involved in angiogenesis. In secretory pathway, is required for the release of chromogranin-A (CHGA)-containing secretory granules from the TGN. Downstream of PRKCA, plays important roles in angiotensin-2-induced monocyte adhesion to endothelial cells. Plays a regulatory role in angiogenesis and tumor growth by phosphorylating a downstream mediator CIB1 isoform 2, resulting in vascular endothelial growth factor A (VEGFA) secretion.10 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.By similarity

    Enzyme regulationi

    Activated by DAG and phorbol esters. Phorbol-ester/DAG-type domains bind DAG, mediating translocation to membranes. Autophosphorylation of Ser-710 and phosphorylation of Ser-706 by PKC relieves auto-inhibition by the PH domain.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei580 – 5801ATPPROSITE-ProRule annotation
    Active sitei674 – 6741Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri138 – 18851Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri264 – 31451Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
    BLAST
    Nucleotide bindingi557 – 5659ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. protein kinase activity Source: BHF-UCL
    5. protein kinase C activity Source: UniProtKB-EC
    6. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. cell adhesion Source: UniProtKB-KW
    3. cell death Source: BHF-UCL
    4. cellular response to vascular endothelial growth factor stimulus Source: BHF-UCL
    5. endothelial tube morphogenesis Source: BHF-UCL
    6. intracellular signal transduction Source: BHF-UCL
    7. peptidyl-serine phosphorylation Source: BHF-UCL
    8. positive regulation of angiogenesis Source: UniProtKB
    9. positive regulation of blood vessel endothelial cell migration Source: BHF-UCL
    10. positive regulation of cell adhesion Source: UniProtKB
    11. positive regulation of CREB transcription factor activity Source: BHF-UCL
    12. positive regulation of DNA biosynthetic process Source: UniProtKB
    13. positive regulation of endothelial cell chemotaxis Source: BHF-UCL
    14. positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
    15. positive regulation of endothelial cell migration Source: UniProtKB
    16. positive regulation of endothelial cell proliferation Source: UniProtKB
    17. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
    18. positive regulation of fibroblast growth factor receptor signaling pathway Source: UniProtKB
    19. positive regulation of histone deacetylase activity Source: BHF-UCL
    20. positive regulation of interleukin-2 production Source: UniProtKB
    21. positive regulation of interleukin-8 production Source: UniProtKB
    22. positive regulation of intracellular signal transduction Source: BHF-UCL
    23. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    24. positive regulation of peptidyl-serine phosphorylation Source: BHF-UCL
    25. positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
    26. positive regulation of T cell receptor signaling pathway Source: UniProtKB
    27. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    28. positive regulation of vascular endothelial growth factor receptor signaling pathway Source: UniProtKB
    29. protein autophosphorylation Source: BHF-UCL
    30. protein phosphorylation Source: UniProtKB
    31. T cell receptor signaling pathway Source: BHF-UCL
    32. vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Adaptive immunity, Angiogenesis, Cell adhesion, Immunity

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BRENDAi2.7.11.13. 2681.
    SignaLinkiQ9BZL6.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase D2 (EC:2.7.11.13)
    Alternative name(s):
    nPKC-D2
    Gene namesi
    Name:PRKD2
    Synonyms:PKD2
    ORF Names:HSPC187
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:17293. PRKD2.

    Subcellular locationi

    Cytoplasm. Cell membrane By similarity. Nucleus. Golgi apparatustrans-Golgi network
    Note: Translocation to the cell membrane is required for kinase activation By similarity. Accumulates in the nucleus upon CK1-mediated phosphorylation after activation of G-protein-coupled receptors. Nuclear accumulation is regulated by blocking nuclear export of active PRKD2 rather than by increasing import.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: BHF-UCL
    2. Golgi apparatus Source: UniProtKB-SubCell
    3. nucleus Source: BHF-UCL
    4. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Golgi apparatus, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi244 – 2441S → E: Constitutive kinase activity; when associated with E-706 and E-710. 1 Publication
    Mutagenesisi275 – 2751P → G: Increase in ability to bind phorbol ester, slight increase in ability to bind DAG. 1 Publication
    Mutagenesisi438 – 4381Y → F: Loss of phosphorylation. 1 Publication
    Mutagenesisi695 – 6951D → A: Loss of kinase activity. 1 Publication
    Mutagenesisi706 – 7061S → E: Constitutive kinase activity; when associated with E-710 or with E-244 and E-710. 1 Publication
    Mutagenesisi710 – 7101S → E: Constitutive kinase activity; when associated with E-706 or with E-244 and E-706. 1 Publication

    Organism-specific databases

    PharmGKBiPA134903505.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 878878Serine/threonine-protein kinase D2PRO_0000055716Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei200 – 2001Phosphoserine1 Publication
    Modified residuei203 – 2031Phosphoserine2 Publications
    Modified residuei206 – 2061Phosphoserine2 Publications
    Modified residuei214 – 2141Phosphoserine1 Publication
    Modified residuei244 – 2441Phosphoserine; by CSNK1D and CSNK1E1 Publication
    Modified residuei438 – 4381Phosphotyrosine; by ABL11 Publication
    Modified residuei518 – 5181Phosphoserine1 Publication
    Modified residuei706 – 7061Phosphoserine; by PKC1 Publication
    Modified residuei710 – 7101Phosphoserine4 Publications
    Modified residuei717 – 7171Phosphotyrosine1 Publication
    Modified residuei876 – 8761Phosphoserine; by autocatalysis4 Publications

    Post-translational modificationi

    Phosphorylation of Ser-876 correlates with the activation status of the kinase. Ser-706 is probably phosphorylated by PKC. Phosphorylation at Ser-244 by CSNK1D and CSNK1E promotes nuclear localization and substrate targeting. Phosphorylation at Ser-244, Ser-706 and Ser-710 is required for nuclear localization. Phosphorylated at Tyr-438 by ABL1 in response to oxidative stress.8 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9BZL6.
    PaxDbiQ9BZL6.
    PRIDEiQ9BZL6.

    PTM databases

    PhosphoSiteiQ9BZL6.

    Expressioni

    Tissue specificityi

    Widely expressed.

    Gene expression databases

    ArrayExpressiQ9BZL6.
    BgeeiQ9BZL6.
    CleanExiHS_PKD2.
    HS_PRKD2.
    GenevestigatoriQ9BZL6.

    Organism-specific databases

    HPAiHPA021490.

    Interactioni

    Subunit structurei

    Interacts (via C-terminus) with LCK. Interacts (via N-terminal AP-rich region) with CIB1 isoform 2.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HDAC7Q8WUI46EBI-1384325,EBI-1048378

    Protein-protein interaction databases

    BioGridi117384. 20 interactions.
    IntActiQ9BZL6. 27 interactions.
    MINTiMINT-1179710.
    STRINGi9606.ENSP00000291281.

    Structurei

    Secondary structure

    1
    878
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi399 – 4068
    Beta strandi409 – 4113
    Beta strandi415 – 4217
    Beta strandi423 – 43311
    Beta strandi438 – 4425
    Turni443 – 4453
    Beta strandi448 – 4525
    Beta strandi456 – 4583
    Beta strandi465 – 4706
    Beta strandi486 – 4883
    Helixi495 – 50713

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2COANMR-A398-509[»]
    3BGMX-ray1.60C526-534[»]
    ProteinModelPortaliQ9BZL6.
    SMRiQ9BZL6. Positions 138-188, 237-357, 395-509, 537-846.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9BZL6.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini397 – 509113PHPROSITE-ProRule annotationAdd
    BLAST
    Domaini551 – 807257Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 PH domain.PROSITE-ProRule annotation
    Contains 2 phorbol-ester/DAG-type zinc fingers.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri138 – 18851Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri264 – 31451Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000015135.
    HOVERGENiHBG003564.
    InParanoidiQ9BZL6.
    KOiK06070.
    OrthoDBiEOG75B84N.
    PhylomeDBiQ9BZL6.
    TreeFamiTF314320.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    InterProiIPR020454. DAG/PE-bd.
    IPR011009. Kinase-like_dom.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR015727. Protein_Kinase_C_mu-related.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PANTHERiPTHR22968. PTHR22968. 1 hit.
    PfamiPF00130. C1_1. 2 hits.
    PF00169. PH. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000552. PKC_mu_nu_D2. 1 hit.
    PRINTSiPR00008. DAGPEDOMAIN.
    SMARTiSM00109. C1. 2 hits.
    SM00233. PH. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS50003. PH_DOMAIN. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    PS00479. ZF_DAG_PE_1. 2 hits.
    PS50081. ZF_DAG_PE_2. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9BZL6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATAPSYPAG LPGSPGPGSP PPPGGLELQS PPPLLPQIPA PGSGVSFHIQ    50
    IGLTREFVLL PAASELAHVK QLACSIVDQK FPECGFYGLY DKILLFKHDP 100
    TSANLLQLVR SSGDIQEGDL VEVVLSASAT FEDFQIRPHA LTVHSYRAPA 150
    FCDHCGEMLF GLVRQGLKCD GCGLNYHKRC AFSIPNNCSG ARKRRLSSTS 200
    LASGHSVRLG TSESLPCTAE ELSRSTTELL PRRPPSSSSS SSASSYTGRP 250
    IELDKMLLSK VKVPHTFLIH SYTRPTVCQA CKKLLKGLFR QGLQCKDCKF 300
    NCHKRCATRV PNDCLGEALI NGDVPMEEAT DFSEADKSAL MDESEDSGVI 350
    PGSHSENALH ASEEEEGEGG KAQSSLGYIP LMRVVQSVRH TTRKSSTTLR 400
    EGWVVHYSNK DTLRKRHYWR LDCKCITLFQ NNTTNRYYKE IPLSEILTVE 450
    SAQNFSLVPP GTNPHCFEIV TANATYFVGE MPGGTPGGPS GQGAEAARGW 500
    ETAIRQALMP VILQDAPSAP GHAPHRQASL SISVSNSQIQ ENVDIATVYQ 550
    IFPDEVLGSG QFGVVYGGKH RKTGRDVAVK VIDKLRFPTK QESQLRNEVA 600
    ILQSLRHPGI VNLECMFETP EKVFVVMEKL HGDMLEMILS SEKGRLPERL 650
    TKFLITQILV ALRHLHFKNI VHCDLKPENV LLASADPFPQ VKLCDFGFAR 700
    IIGEKSFRRS VVGTPAYLAP EVLLNQGYNR SLDMWSVGVI MYVSLSGTFP 750
    FNEDEDINDQ IQNAAFMYPA SPWSHISAGA IDLINNLLQV KMRKRYSVDK 800
    SLSHPWLQEY QTWLDLRELE GKMGERYITH ESDDVRWEQF AAEHPLPGSG 850
    LPTDRDLGGA CPPQDHDMQG LAERISVL 878
    Length:878
    Mass (Da):96,750
    Last modified:May 18, 2010 - v2
    Checksum:i8BAB45FB5B1718E7
    GO

    Sequence cautioni

    The sequence AAF36107.1 differs from that shown. Reason: Frameshift at positions 604, 606, 738, 744, 755, 758, 833 and 854.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti790 – 7901V → L in AAF36107. (PubMed:11042152)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti324 – 3241V → M.1 Publication
    Corresponds to variant rs45455991 [ dbSNP | Ensembl ].
    VAR_042330
    Natural varianti496 – 4961A → V.1 Publication
    Corresponds to variant rs55716765 [ dbSNP | Ensembl ].
    VAR_042331
    Natural varianti604 – 6041S → G.1 Publication
    Corresponds to variant rs34325043 [ dbSNP | Ensembl ].
    VAR_042332
    Natural varianti773 – 7731W → R.1 Publication
    Corresponds to variant rs55933311 [ dbSNP | Ensembl ].
    VAR_042333
    Natural varianti835 – 8351V → A.3 Publications
    Corresponds to variant rs314665 [ dbSNP | Ensembl ].
    VAR_061531
    Natural varianti848 – 8481G → E in a lung adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_042334
    Natural varianti870 – 8701G → E in a gastric adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_042335

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF309082 mRNA. Translation: AAK01149.1.
    AC008635 Genomic DNA. No translation available.
    AC093503 Genomic DNA. No translation available.
    AL050147 mRNA. Translation: CAB43292.1.
    AF151021 mRNA. Translation: AAF36107.1. Frameshift.
    CCDSiCCDS12689.1.
    PIRiT08777.
    RefSeqiNP_001073349.1. NM_001079880.1.
    NP_001073350.1. NM_001079881.1.
    NP_001073351.1. NM_001079882.1.
    NP_057541.2. NM_016457.4.
    UniGeneiHs.466987.

    Genome annotation databases

    EnsembliENST00000291281; ENSP00000291281; ENSG00000105287.
    ENST00000433867; ENSP00000393978; ENSG00000105287.
    GeneIDi25865.
    KEGGihsa:25865.
    UCSCiuc002pfh.3. human.

    Polymorphism databases

    DMDMi296434570.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF309082 mRNA. Translation: AAK01149.1 .
    AC008635 Genomic DNA. No translation available.
    AC093503 Genomic DNA. No translation available.
    AL050147 mRNA. Translation: CAB43292.1 .
    AF151021 mRNA. Translation: AAF36107.1 . Frameshift.
    CCDSi CCDS12689.1.
    PIRi T08777.
    RefSeqi NP_001073349.1. NM_001079880.1.
    NP_001073350.1. NM_001079881.1.
    NP_001073351.1. NM_001079882.1.
    NP_057541.2. NM_016457.4.
    UniGenei Hs.466987.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2COA NMR - A 398-509 [» ]
    3BGM X-ray 1.60 C 526-534 [» ]
    ProteinModelPortali Q9BZL6.
    SMRi Q9BZL6. Positions 138-188, 237-357, 395-509, 537-846.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117384. 20 interactions.
    IntActi Q9BZL6. 27 interactions.
    MINTi MINT-1179710.
    STRINGi 9606.ENSP00000291281.

    Chemistry

    BindingDBi Q9BZL6.
    ChEMBLi CHEMBL4900.
    GuidetoPHARMACOLOGYi 2173.

    PTM databases

    PhosphoSitei Q9BZL6.

    Polymorphism databases

    DMDMi 296434570.

    Proteomic databases

    MaxQBi Q9BZL6.
    PaxDbi Q9BZL6.
    PRIDEi Q9BZL6.

    Protocols and materials databases

    DNASUi 25865.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000291281 ; ENSP00000291281 ; ENSG00000105287 .
    ENST00000433867 ; ENSP00000393978 ; ENSG00000105287 .
    GeneIDi 25865.
    KEGGi hsa:25865.
    UCSCi uc002pfh.3. human.

    Organism-specific databases

    CTDi 25865.
    GeneCardsi GC19M047177.
    HGNCi HGNC:17293. PRKD2.
    HPAi HPA021490.
    MIMi 607074. gene.
    neXtProti NX_Q9BZL6.
    PharmGKBi PA134903505.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000015135.
    HOVERGENi HBG003564.
    InParanoidi Q9BZL6.
    KOi K06070.
    OrthoDBi EOG75B84N.
    PhylomeDBi Q9BZL6.
    TreeFami TF314320.

    Enzyme and pathway databases

    BRENDAi 2.7.11.13. 2681.
    SignaLinki Q9BZL6.

    Miscellaneous databases

    ChiTaRSi PRKD2. human.
    EvolutionaryTracei Q9BZL6.
    GeneWikii PRKD2.
    GenomeRNAii 25865.
    NextBioi 47239.
    PROi Q9BZL6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BZL6.
    Bgeei Q9BZL6.
    CleanExi HS_PKD2.
    HS_PRKD2.
    Genevestigatori Q9BZL6.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    InterProi IPR020454. DAG/PE-bd.
    IPR011009. Kinase-like_dom.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR015727. Protein_Kinase_C_mu-related.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    PANTHERi PTHR22968. PTHR22968. 1 hit.
    Pfami PF00130. C1_1. 2 hits.
    PF00169. PH. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000552. PKC_mu_nu_D2. 1 hit.
    PRINTSi PR00008. DAGPEDOMAIN.
    SMARTi SM00109. C1. 2 hits.
    SM00233. PH. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS50003. PH_DOMAIN. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    PS00479. ZF_DAG_PE_1. 2 hits.
    PS50081. ZF_DAG_PE_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and characterization of the human protein kinase D2. A novel member of the protein kinase d family of serine threonine kinases."
      Sturany S., Van Lint J., Mueller F., Wilda M., Hameister H., Hoecker M., Brey A., Gern U., Vandenheede J., Gress T., Adler G., Seufferlein T.
      J. Biol. Chem. 276:3310-3318(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT SER-876, VARIANT ALA-835.
      Tissue: Pancreas.
    2. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 337-878, VARIANT ALA-835.
      Tissue: Uterus.
    4. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
      Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
      , Gu J., Chen S.-J., Chen Z.
      Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 574-878, VARIANT ALA-835.
      Tissue: Umbilical cord blood.
    5. "Mechanism of activation of protein kinase D2(PKD2) by the CCK(B)/gastrin receptor."
      Sturany S., Van Lint J., Gilchrist A., Vandenheede J.R., Adler G., Seufferlein T.
      J. Biol. Chem. 277:29431-29436(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, PHOSPHORYLATION AT SER-706; SER-710 AND SER-876.
    6. "Protein kinase D2 mediates activation of nuclear factor kappaB by Bcr-Abl in Bcr-Abl+ human myeloid leukemia cells."
      Mihailovic T., Marx M., Auer A., Van Lint J., Schmid M., Weber C., Seufferlein T.
      Cancer Res. 64:8939-8944(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NF-KAPPA-B ACTIVATION, PHOSPHORYLATION AT TYR-438, MUTAGENESIS OF TYR-438.
    7. "Protein kinase D regulates basolateral membrane protein exit from trans-Golgi network."
      Yeaman C., Ayala M.I., Wright J.R., Bard F., Bossard C., Ang A., Maeda Y., Seufferlein T., Mellman I., Nelson W.J., Malhotra V.
      Nat. Cell Biol. 6:106-112(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TRAFFICKING.
    8. "Protein kinase D2 contributes to either IL-2 promoter regulation or induction of cell death upon TCR stimulation depending on its activity in Jurkat cells."
      Irie A., Harada K., Tsukamoto H., Kim J.R., Araki N., Nishimura Y.
      Int. Immunol. 18:1737-1747(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ADAPTIVE IMMUNE RESPONSE.
    9. "Protein kinase D2 mediates lysophosphatidic acid-induced interleukin 8 production in nontransformed human colonic epithelial cells through NF-kappaB."
      Chiu T.T., Leung W.Y., Moyer M.P., Strieter R.M., Rozengurt E.
      Am. J. Physiol. 292:C767-C777(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Phosphorylation at Ser244 by CK1 determines nuclear localization and substrate targeting of PKD2."
      von Blume J., Knippschild U., Dequiedt F., Giamas G., Beck A., Auer A., Van Lint J., Adler G., Seufferlein T.
      EMBO J. 26:4619-4633(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF HDAC7, ENZYME REGULATION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-244.
    11. "Angiotensin II directly triggers endothelial exocytosis via protein kinase C-dependent protein kinase D2 activation."
      Ge X., Low B., Liang M., Fu J.
      J. Pharmacol. Sci. 105:168-176(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL ADHESION.
    12. "Selective binding of phorbol esters and diacylglycerol by individual C1 domains of the PKD family."
      Chen J., Deng F., Li J., Wang Q.J.
      Biochem. J. 411:333-342(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHORBOL-ESTER BINDING, MUTAGENESIS OF PRO-275.
    13. "Protein kinase D2 regulates chromogranin A secretion in human BON neuroendocrine tumour cells."
      von Wichert G., Edenfeld T., von Blume J., Krisp H., Krndija D., Schmid H., Oswald F., Lother U., Walther P., Adler G., Seufferlein T.
      Cell. Signal. 20:925-934(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN SECRETORY PATHWAY, SUBCELLULAR LOCATION.
    14. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-710 AND SER-876, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200; SER-203; SER-206; SER-214 AND SER-710, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "PKD2 interacts with Lck and regulates NFAT activity in T cells."
      Li Q., Sun X., Wu J., Lin Z., Luo Y.
      BMB Rep. 42:35-40(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH LCK.
    18. "Identification of protein kinase D2 as a pivotal regulator of endothelial cell proliferation, migration, and angiogenesis."
      Hao Q., Wang L., Zhao Z.J., Tang H.
      J. Biol. Chem. 284:799-806(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ANGIOGENESIS.
    19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206; SER-518; SER-710; TYR-717 AND SER-876, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "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.
    21. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "A novel splice variant of calcium and integrin-binding protein 1 mediates protein kinase D2-stimulated tumour growth by regulating angiogenesis."
      Armacki M., Joodi G., Nimmagadda S.C., de Kimpe L., Pusapati G.V., Vandoninck S., Van Lint J., Illing A., Seufferlein T.
      Oncogene 33:1167-1180(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CIB1 ISOFORM 2, MUTAGENESIS OF SER-244; ASP-695; SER-706 AND SER-710.
    25. "Solution structure of the PH domain of protein kinase C, D2 type from human."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 395-509.
    26. "Phosphorylation-dependent interaction between antigenic peptides and MHC class I: a molecular basis for the presentation of transformed self."
      Mohammed F., Cobbold M., Zarling A.L., Salim M., Barrett-Wilt G.A., Shabanowitz J., Hunt D.F., Engelhard V.H., Willcox B.E.
      Nat. Immunol. 9:1236-1243(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 526-534.
    27. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] MET-324; VAL-496; GLY-604; ARG-773; GLU-848 AND GLU-870.

    Entry informationi

    Entry nameiKPCD2_HUMAN
    AccessioniPrimary (citable) accession number: Q9BZL6
    Secondary accession number(s): Q8TB08, Q9P0T6, Q9Y3X8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 27, 2002
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 152 of the entry and version 2 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, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3