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Q15139

- KPCD1_HUMAN

UniProt

Q15139 - KPCD1_HUMAN

Protein

Serine/threonine-protein kinase D1

Gene

PRKD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 2 (14 Oct 2008)
      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 MAPK8/JNK1 and Ras signaling, Golgi membrane integrity and trafficking, cell survival through NF-kappa-B activation, cell migration, cell differentiation by mediating HDAC7 nuclear export, cell proliferation via MAPK1/3 (ERK1/2) signaling, and plays a role in cardiac hypertrophy, VEGFA-induced angiogenesis, genotoxic-induced apoptosis and flagellin-stimulated inflammatory response. Phosphorylates the epidermal growth factor receptor (EGFR) on dual threonine residues, which leads to the suppression of epidermal growth factor (EGF)-induced MAPK8/JNK1 activation and subsequent JUN phosphorylation. Phosphorylates RIN1, inducing RIN1 binding to 14-3-3 proteins YWHAB, YWHAE and YWHAZ and increased competition with RAF1 for binding to GTP-bound form of Ras proteins (NRAS, HRAS and KRAS). Acts downstream of the heterotrimeric G-protein beta/gamma-subunit complex to maintain the structural integrity of the Golgi membranes, and is required for protein transport along the secretory pathway. In the trans-Golgi network (TGN), regulates the fission of transport vesicles that are on their way to the plasma membrane. May act by activating the lipid kinase phosphatidylinositol 4-kinase beta (PI4KB) at the TGN for the local synthesis of phosphorylated inositol lipids, which induces a sequential production of DAG, phosphatidic acid (PA) and lyso-PA (LPA) that are necessary for membrane fission and generation of specific transport carriers to the cell surface. Under oxidative stress, is phosphorylated at Tyr-463 via SRC-ABL1 and contributes to cell survival by activating IKK complex and subsequent nuclear translocation and activation of NFKB1. Involved in cell migration by regulating integrin alpha-5/beta-3 recycling and promoting its recruitment in newly forming focal adhesion. In osteoblast differentiation, mediates the bone morphogenic protein 2 (BMP2)-induced nuclear export of HDAC7, which results in the inhibition of HDAC7 transcriptional repression of RUNX2. In neurons, plays an important role in neuronal polarity by regulating the biogenesis of TGN-derived dendritic vesicles, and is involved in the maintenance of dendritic arborization and Golgi structure in hippocampal cells. May potentiate mitogenesis induced by the neuropeptide bombesin or vasopressin 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. Plays an important role in the proliferative response induced by low calcium in keratinocytes, through sustained activation of MAPK1/3 (ERK1/2) pathway. Downstream of novel PKC signaling, plays a role in cardiac hypertrophy by phosphorylating HDAC5, which in turn triggers XPO1/CRM1-dependent nuclear export of HDAC5, MEF2A transcriptional activation and induction of downstream target genes that promote myocyte hypertrophy and pathological cardiac remodeling. Mediates cardiac troponin I (TNNI3) phosphorylation at the PKA sites, which results in reduced myofilament calcium sensitivity, and accelerated crossbridge cycling kinetics. The PRKD1-HDAC5 pathway is also involved in angiogenesis by mediating VEGFA-induced specific subset of gene expression, cell migration, and tube formation. In response to VEGFA, is necessary and required for HDAC7 phosphorylation which induces HDAC7 nuclear export and endothelial cell proliferation and migration. During apoptosis induced by cytarabine and other genotoxic agents, PRKD1 is cleaved by caspase-3 at Asp-378, resulting in activation of its kinase function and increased sensitivity of cells to the cytotoxic effects of genotoxic agents. In epithelial cells, is required for transducing flagellin-stimulated inflammatory responses by binding and phosphorylating TLR5, which contributes to MAPK14/p38 activation and production of inflammatory cytokines. May play a role in inflammatory response by mediating activation of NF-kappa-B. May be involved in pain transmission by directly modulating TRPV1 receptor.10 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.

    Enzyme regulationi

    Activated by DAG and phorbol esters. Phorbol-ester/DAG-type domain 1 binds DAG with high affinity and appears to play the dominant role in mediating translocation to the cell membrane and trans-Golgi network. Phorbol-ester/DAG-type domain 2 binds phorbol ester with higher affinity. Autophosphorylation of Ser-742 and phosphorylation of Ser-738 by PKC relieves auto-inhibition by the PH domain. Phosphorylation on Tyr-463 by the SRC-ABL1 pathway in response to oxidative stress, is also required for activation. Activated by DAPK1 under oxidative stress.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei612 – 6121ATP
    Active sitei706 – 7061Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri146 – 19651Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri270 – 32051Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
    BLAST
    Nucleotide bindingi589 – 5979ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. identical protein binding Source: IntAct
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: UniProtKB
    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. apoptotic process Source: UniProtKB-KW
    3. cell proliferation Source: ProtInc
    4. cellular response to oxidative stress Source: UniProtKB
    5. cellular response to vascular endothelial growth factor stimulus Source: UniProtKB
    6. Golgi organization Source: UniProtKB
    7. Golgi vesicle transport Source: UniProtKB
    8. inflammatory response Source: UniProtKB-KW
    9. innate immune response Source: UniProtKB-KW
    10. integrin-mediated signaling pathway Source: BHF-UCL
    11. intracellular signal transduction Source: BHF-UCL
    12. negative regulation of cell death Source: UniProtKB
    13. negative regulation of endocytosis Source: BHF-UCL
    14. peptidyl-serine phosphorylation Source: BHF-UCL
    15. positive regulation of angiogenesis Source: UniProtKB
    16. positive regulation of blood vessel endothelial cell migration Source: BHF-UCL
    17. positive regulation of CREB transcription factor activity Source: BHF-UCL
    18. positive regulation of endothelial cell chemotaxis Source: BHF-UCL
    19. positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
    20. positive regulation of endothelial cell migration Source: UniProtKB
    21. positive regulation of endothelial cell proliferation Source: BHF-UCL
    22. positive regulation of histone deacetylase activity Source: BHF-UCL
    23. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    24. positive regulation of neuron projection development Source: UniProtKB
    25. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    26. positive regulation of osteoblast differentiation Source: UniProtKB
    27. positive regulation of peptidyl-serine phosphorylation Source: BHF-UCL
    28. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    29. protein autophosphorylation Source: BHF-UCL
    30. regulation of integrin-mediated signaling pathway Source: BHF-UCL
    31. regulation of keratinocyte proliferation Source: UniProtKB
    32. signal transduction Source: ProtInc
    33. small molecule metabolic process Source: Reactome
    34. sphingolipid biosynthetic process Source: Reactome
    35. sphingolipid metabolic process Source: Reactome
    36. vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Angiogenesis, Apoptosis, Differentiation, Immunity, Inflammatory response, Innate immunity, Neurogenesis

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BRENDAi2.7.11.13. 2681.
    ReactomeiREACT_115810. Sphingolipid de novo biosynthesis.
    SignaLinkiQ15139.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase D1 (EC:2.7.11.13)
    Alternative name(s):
    Protein kinase C mu type
    Protein kinase D
    nPKC-D1
    nPKC-mu
    Gene namesi
    Name:PRKD1
    Synonyms:PKD, PKD1, PRKCM
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:9407. PRKD1.

    Subcellular locationi

    Cytoplasm 1 Publication. Cell membrane 1 Publication. Golgi apparatustrans-Golgi network By similarity
    Note: Translocation to the cell membrane is required for kinase activation.

    GO - Cellular componenti

    1. cell-cell junction Source: Ensembl
    2. cell cortex Source: Ensembl
    3. cytoplasm Source: HPA
    4. cytosol Source: UniProtKB
    5. integral component of plasma membrane Source: ProtInc
    6. nucleus Source: Ensembl
    7. plasma membrane Source: HPA
    8. trans-Golgi network Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Golgi apparatus, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi157 – 1571P → G: Increase in ability to bind phorbol ester, loss of ability to bind DAG. 1 Publication
    Mutagenesisi281 – 2811P → G: No effect on ability to bind phorbol ester, slight increase in ability to bind DAG. 1 Publication
    Mutagenesisi432 – 4321Y → E: Decreased phosphorylation level when coexpressed with SRC in HeLa cells. Unchanged phosphorylation level when coexpressed with ABL. 1 Publication
    Mutagenesisi432 – 4321Y → F: Decreased phosphorylation level when coexpressed with SRC in HeLa cells. Unchanged phosphorylation level when coexpressed with ABL. Unaltered kinase activity. Decreased kinase activity; when associated with F-463 and F-502. 1 Publication
    Mutagenesisi463 – 4631Y → E: Constitutive activation and constitutive phosphorylation of S-738 and S-742. 1 Publication
    Mutagenesisi463 – 4631Y → F: Decreased phosphorylation level when coexpressed with either SRC or ABL in HeLa cells. Decreased kinase activity. 1 Publication
    Mutagenesisi502 – 5021Y → E: Loss of activation. 1 Publication
    Mutagenesisi502 – 5021Y → F: Decreased phosphorylation level when coexpressed with SRC in HeLa cells. Unchanged phosphorylation level when coexpressed with ABL. Unaltered kinase activity. Decreased kinase activity; when associated with F-432 and F-502. 1 Publication
    Mutagenesisi612 – 6121K → W: Loss of kinase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA33771.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 912912Serine/threonine-protein kinase D1PRO_0000055714Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei95 – 951Phosphotyrosine2 Publications
    Modified residuei205 – 2051Phosphoserine3 Publications
    Modified residuei208 – 2081Phosphoserine2 Publications
    Modified residuei345 – 3451Phosphoserine2 Publications
    Modified residuei397 – 3971Phosphoserine; by MAPK132 Publications
    Modified residuei401 – 4011Phosphoserine; by MAPK132 Publications
    Modified residuei432 – 4321Phosphotyrosine2 Publications
    Modified residuei448 – 4481Phosphoserine2 Publications
    Modified residuei463 – 4631Phosphotyrosine; by ABL3 Publications
    Modified residuei473 – 4731Phosphoserine2 Publications
    Modified residuei502 – 5021Phosphotyrosine2 Publications
    Modified residuei738 – 7381Phosphoserine; by PKC/PRKCD2 Publications
    Modified residuei742 – 7421Phosphoserine; by autocatalysis and PKC/PRKCD2 Publications
    Modified residuei910 – 9101Phosphoserine; by autocatalysis1 Publication

    Post-translational modificationi

    Phosphorylated at Ser-397 and Ser-401 by MAPK13 during regulation of insulin secretion in pancreatic beta cells. Phosphorylated by DAPK1. Phosphorylated by ABL at Tyr-463, which primes the kinase in response to oxidative stress, and promotes a second step activating phosphorylation at Ser-738/Ser-742 by PKRD.7 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ15139.
    PaxDbiQ15139.
    PRIDEiQ15139.

    PTM databases

    PhosphoSiteiQ15139.

    Expressioni

    Gene expression databases

    ArrayExpressiQ15139.
    BgeeiQ15139.
    CleanExiHS_PKD1.
    HS_PRKD1.
    GenevestigatoriQ15139.

    Organism-specific databases

    HPAiCAB018367.
    HPA029834.

    Interactioni

    Subunit structurei

    Interacts (via N-terminus) with ADAP1/CENTA1. Interacts with MAPK13 and SRC. Interacts with DAPK1 in an oxidative stress-regulated manner.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-1181072,EBI-1181072
    C1QBPQ070219EBI-1181072,EBI-347528
    CDH1P128307EBI-1181072,EBI-727477
    HSP90AB1P082382EBI-1181072,EBI-352572
    MAPK13O152646EBI-1181072,EBI-2116951
    MT2AP027957EBI-1181072,EBI-996616

    Protein-protein interaction databases

    BioGridi111573. 26 interactions.
    DIPiDIP-38481N.
    IntActiQ15139. 6 interactions.
    MINTiMINT-88491.
    STRINGi9606.ENSP00000333568.

    Structurei

    3D structure databases

    ProteinModelPortaliQ15139.
    SMRiQ15139. Positions 147-196, 271-320, 420-541, 550-867.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini422 – 541120PHPROSITE-ProRule annotationAdd
    BLAST
    Domaini583 – 839257Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi17 – 2610Poly-Ala
    Compositional biasi200 – 2034Poly-Arg

    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 fingeri146 – 19651Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri270 – 32051Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG003564.
    InParanoidiQ15139.
    KOiK06070.
    OrthoDBiEOG75B84N.
    PhylomeDBiQ15139.
    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.

    Q15139-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSAPPVLRPP SPLLPVAAAA AAAAAALVPG SGPGPAPFLA PVAAPVGGIS    50
    FHLQIGLSRE PVLLLQDSSG DYSLAHVREM ACSIVDQKFP ECGFYGMYDK 100
    ILLFRHDPTS ENILQLVKAA SDIQEGDLIE VVLSASATFE DFQIRPHALF 150
    VHSYRAPAFC DHCGEMLWGL VRQGLKCEGC GLNYHKRCAF KIPNNCSGVR 200
    RRRLSNVSLT GVSTIRTSSA ELSTSAPDEP LLQKSPSESF IGREKRSNSQ 250
    SYIGRPIHLD KILMSKVKVP HTFVIHSYTR PTVCQYCKKL LKGLFRQGLQ 300
    CKDCRFNCHK RCAPKVPNNC LGEVTINGDL LSPGAESDVV MEEGSDDNDS 350
    ERNSGLMDDM EEAMVQDAEM AMAECQNDSG EMQDPDPDHE DANRTISPST 400
    SNNIPLMRVV QSVKHTKRKS STVMKEGWMV HYTSKDTLRK RHYWRLDSKC 450
    ITLFQNDTGS RYYKEIPLSE ILSLEPVKTS ALIPNGANPH CFEITTANVV 500
    YYVGENVVNP SSPSPNNSVL TSGVGADVAR MWEIAIQHAL MPVIPKGSSV 550
    GTGTNLHRDI SVSISVSNCQ IQENVDISTV YQIFPDEVLG SGQFGIVYGG 600
    KHRKTGRDVA IKIIDKLRFP TKQESQLRNE VAILQNLHHP GVVNLECMFE 650
    TPERVFVVME KLHGDMLEMI LSSEKGRLPE HITKFLITQI LVALRHLHFK 700
    NIVHCDLKPE NVLLASADPF PQVKLCDFGF ARIIGEKSFR RSVVGTPAYL 750
    APEVLRNKGY NRSLDMWSVG VIIYVSLSGT FPFNEDEDIH DQIQNAAFMY 800
    PPNPWKEISH EAIDLINNLL QVKMRKRYSV DKTLSHPWLQ DYQTWLDLRE 850
    LECKIGERYI THESDDLRWE KYAGEQGLQY PTHLINPSAS HSDTPETEET 900
    EMKALGERVS IL 912
    Length:912
    Mass (Da):101,704
    Last modified:October 14, 2008 - v2
    Checksum:i0BC9414C335D2DBB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti135 – 1351A → R in CAA53384. (PubMed:8119958)Curated
    Sequence conflicti877 – 8771G → R in CAA53384. (PubMed:8119958)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti152 – 1521H → Y in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035468
    Natural varianti225 – 2251S → P.1 Publication
    VAR_042324
    Natural varianti478 – 4781K → Q.1 Publication
    Corresponds to variant rs55852813 [ dbSNP | Ensembl ].
    VAR_042325
    Natural varianti585 – 5851P → S in a metastatic melanoma sample; somatic mutation. 1 Publication
    VAR_042326
    Natural varianti677 – 6771R → M in a lung bronchoalveolar carcinoma sample; somatic mutation. 1 Publication
    VAR_042327
    Natural varianti679 – 6791P → L.1 Publication
    Corresponds to variant rs34588699 [ dbSNP | Ensembl ].
    VAR_042328
    Natural varianti825 – 8251R → K.
    Corresponds to variant rs11161065 [ dbSNP | Ensembl ].
    VAR_046988
    Natural varianti857 – 8571E → K in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035469
    Natural varianti891 – 8911H → R.1 Publication
    Corresponds to variant rs45582934 [ dbSNP | Ensembl ].
    VAR_042329

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X75756 mRNA. Translation: CAA53384.1.
    AK314170 mRNA. Translation: BAG36853.1.
    AL135858 Genomic DNA. No translation available.
    CH471078 Genomic DNA. Translation: EAW65971.1.
    CCDSiCCDS9637.1.
    PIRiA53215.
    RefSeqiNP_002733.2. NM_002742.2.
    UniGeneiHs.508999.

    Genome annotation databases

    EnsembliENST00000331968; ENSP00000333568; ENSG00000184304.
    GeneIDi5587.
    KEGGihsa:5587.
    UCSCiuc001wqh.3. human.

    Polymorphism databases

    DMDMi209572639.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X75756 mRNA. Translation: CAA53384.1 .
    AK314170 mRNA. Translation: BAG36853.1 .
    AL135858 Genomic DNA. No translation available.
    CH471078 Genomic DNA. Translation: EAW65971.1 .
    CCDSi CCDS9637.1.
    PIRi A53215.
    RefSeqi NP_002733.2. NM_002742.2.
    UniGenei Hs.508999.

    3D structure databases

    ProteinModelPortali Q15139.
    SMRi Q15139. Positions 147-196, 271-320, 420-541, 550-867.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111573. 26 interactions.
    DIPi DIP-38481N.
    IntActi Q15139. 6 interactions.
    MINTi MINT-88491.
    STRINGi 9606.ENSP00000333568.

    Chemistry

    BindingDBi Q15139.
    ChEMBLi CHEMBL2096620.
    GuidetoPHARMACOLOGYi 1489.

    PTM databases

    PhosphoSitei Q15139.

    Polymorphism databases

    DMDMi 209572639.

    Proteomic databases

    MaxQBi Q15139.
    PaxDbi Q15139.
    PRIDEi Q15139.

    Protocols and materials databases

    DNASUi 5587.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000331968 ; ENSP00000333568 ; ENSG00000184304 .
    GeneIDi 5587.
    KEGGi hsa:5587.
    UCSCi uc001wqh.3. human.

    Organism-specific databases

    CTDi 5587.
    GeneCardsi GC14M030045.
    H-InvDB HIX0037727.
    HGNCi HGNC:9407. PRKD1.
    HPAi CAB018367.
    HPA029834.
    MIMi 605435. gene.
    neXtProti NX_Q15139.
    PharmGKBi PA33771.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG003564.
    InParanoidi Q15139.
    KOi K06070.
    OrthoDBi EOG75B84N.
    PhylomeDBi Q15139.
    TreeFami TF314320.

    Enzyme and pathway databases

    BRENDAi 2.7.11.13. 2681.
    Reactomei REACT_115810. Sphingolipid de novo biosynthesis.
    SignaLinki Q15139.

    Miscellaneous databases

    GeneWikii Protein_kinase_D1.
    GenomeRNAii 5587.
    NextBioi 21670.
    PROi Q15139.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15139.
    Bgeei Q15139.
    CleanExi HS_PKD1.
    HS_PRKD1.
    Genevestigatori Q15139.

    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. "PKCmu is a novel, atypical member of the protein kinase C family."
      Johannes F.-J., Prestle J., Eis S., Oberhagemann P., Pfizenmaier K.
      J. Biol. Chem. 269:6140-6148(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Placenta.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Testis.
    3. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Cell-type specific phosphorylation of threonines T654 and T669 by PKD defines the signal capacity of the EGF receptor."
      Bagowski C.P., Stein-Gerlach M., Choidas A., Ullrich A.
      EMBO J. 18:5567-5576(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN EGFR PHOSPHORYLATION.
    6. "Proteolytic cleavage and activation of protein kinase C [micro] by caspase-3 in the apoptotic response of cells to 1-beta -D-arabinofuranosylcytosine and other genotoxic agents."
      Endo K., Oki E., Biedermann V., Kojima H., Yoshida K., Johannes F.J., Kufe D., Datta R.
      J. Biol. Chem. 275:18476-18481(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN APOPTOSIS.
    7. "Centaurin-alpha(1) associates with and is phosphorylated by isoforms of protein kinase C."
      Zemlickova E., Dubois T., Kerai P., Clokie S., Cronshaw A.D., Wakefield R.I.D., Johannes F.-J., Aitken A.
      Biochem. Biophys. Res. Commun. 307:459-465(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ADAP1.
    8. "Protein kinase D mediates a stress-induced NF-kappaB activation and survival pathway."
      Storz P., Toker A.
      EMBO J. 22:109-120(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL SURVIVAL.
    9. "Tyrosine phosphorylation of protein kinase D in the pleckstrin homology domain leads to activation."
      Storz P., Doppler H., Johannes F.J., Toker A.
      J. Biol. Chem. 278:17969-17976(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT TYR-432; TYR-463 AND TYR-502, MUTAGENESIS OF TYR-432; TYR-463; TYR-502 AND LYS-612.
    10. "Interaction between protein kinase Cmu and the vanilloid receptor type 1."
      Wang Y., Kedei N., Wang M., Wang Q.J., Huppler A.R., Toth A., Tran R., Blumberg P.M.
      J. Biol. Chem. 279:53674-53682(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF TRPV1.
    11. "Protein kinase Cdelta selectively regulates protein kinase D-dependent activation of NF-kappaB in oxidative stress signaling."
      Storz P., Doppler H., Toker A.
      Mol. Cell. Biol. 24:2614-2626(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-463; SER-738 AND SER-742.
    12. "DAP kinase regulates JNK signaling by binding and activating protein kinase D under oxidative stress."
      Eisenberg-Lerner A., Kimchi A.
      Cell Death Differ. 14:1908-1915(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY DAPK1, INTERACTION WITH DAPK1, PHOSPHORYLATION AT SER-910, ENZYME REGULATION.
    13. "A novel tyrosine phosphorylation site in protein kinase D contributes to oxidative stress-mediated activation."
      Doppler H., Storz P.
      J. Biol. Chem. 282:31873-31881(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-95.
    14. "Protein kinase D interaction with TLR5 is required for inflammatory signaling in response to bacterial flagellin."
      Ivison S.M., Graham N.R., Bernales C.Q., Kifayet A., Ng N., Shobab L.A., Steiner T.S.
      J. Immunol. 178:5735-5743(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN INNATE IMMUNITY.
    15. "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: ENZYME REGULATION, PHORBOL-ESTER BINDING, SUBCELLULAR LOCATION, MUTAGENESIS OF PRO-157 AND PRO-281.
    16. "Protein kinase D-dependent phosphorylation and nuclear export of histone deacetylase 5 mediates vascular endothelial growth factor-induced gene expression and angiogenesis."
      Ha C.H., Wang W., Jhun B.S., Wong C., Hausser A., Pfizenmaier K., McKinsey T.A., Olson E.N., Jin Z.G.
      J. Biol. Chem. 283:14590-14599(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF HDAC5, FUNCTION IN ANGIOGENESIS.
    17. "Control of endothelial cell proliferation and migration by VEGF signaling to histone deacetylase 7."
      Wang S., Li X., Parra M., Verdin E., Bassel-Duby R., Olson E.N.
      Proc. Natl. Acad. Sci. U.S.A. 105:7738-7743(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF HDAC7.
    18. "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].
    19. Cited for: PHOSPHORYLATION AT SER-397 AND SER-401, INTERACTION WITH MAPK13, FUNCTION.
    20. "Protein kinase D controls the integrity of Golgi apparatus and the maintenance of dendritic arborization in hippocampal neurons."
      Czoendoer K., Ellwanger K., Fuchs Y.F., Lutz S., Gulyas M., Mansuy I.M., Hausser A., Pfizenmaier K., Schlett K.
      Mol. Biol. Cell 20:2108-2120(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ANGIOGENESIS.
    21. Cited for: REVIEW ON FUNCTION IN TRAFFICKING.
    22. Cited for: REVIEW ON FUNCTION.
    23. "Protein kinase d in the cardiovascular system: emerging roles in health and disease."
      Avkiran M., Rowland A.J., Cuello F., Haworth R.S.
      Circ. Res. 102:157-163(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    24. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205; SER-345; SER-448 AND SER-473, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "Protein kinase D1, a new molecular player in VEGF signaling and angiogenesis."
      Ha C.H., Jin Z.G.
      Mol. Cells 28:1-5(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION IN ANGIOGENESIS.
    26. "Protein kinase D signaling: multiple biological functions in health and disease."
      Rozengurt E.
      Physiology (Bethesda) 26:23-33(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    27. "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-205 AND SER-208, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. Cited for: VARIANTS [LARGE SCALE ANALYSIS] TYR-152 AND LYS-857.
    29. "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] PRO-225; GLN-478; SER-585; MET-677; LEU-679 AND ARG-891.

    Entry informationi

    Entry nameiKPCD1_HUMAN
    AccessioniPrimary (citable) accession number: Q15139
    Secondary accession number(s): A6NL64, B2RAF6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: October 14, 2008
    Last modified: October 1, 2014
    This is version 150 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: 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. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3