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Q9WTQ1

- KPCD1_RAT

UniProt

Q9WTQ1 - KPCD1_RAT

Protein

Serine/threonine-protein kinase D1

Gene

Prkd1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 2 (20 May 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-469 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.4 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 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-748 and phosphorylation of Ser-744 by PKC relieves auto-inhibition by the PH domain. Phosphorylation on Tyr-469 by the SRC-ABL1 pathway in response to oxidative stress, is also required for activation. Activated by DAPK1 under oxidative stress By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei618 – 6181ATPPROSITE-ProRule annotation
    Active sitei712 – 7121Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri144 – 19451Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri276 – 32651Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
    BLAST
    Nucleotide bindingi595 – 6039ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. apoptotic process Source: UniProtKB-KW
    3. cellular response to oxidative stress Source: UniProtKB
    4. cellular response to vascular endothelial growth factor stimulus Source: UniProtKB
    5. Golgi organization Source: UniProtKB
    6. Golgi vesicle transport Source: UniProtKB
    7. inflammatory response Source: UniProtKB-KW
    8. innate immune response Source: UniProtKB-KW
    9. intracellular signal transduction Source: RGD
    10. negative regulation of cell death Source: UniProtKB
    11. peptidyl-serine phosphorylation Source: Ensembl
    12. positive regulation of angiogenesis Source: UniProtKB
    13. positive regulation of blood vessel endothelial cell migration Source: Ensembl
    14. positive regulation of CREB transcription factor activity Source: Ensembl
    15. positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway Source: Ensembl
    16. positive regulation of endothelial cell migration Source: UniProtKB
    17. positive regulation of endothelial cell proliferation Source: Ensembl
    18. positive regulation of histone deacetylase activity Source: Ensembl
    19. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    20. positive regulation of neuron projection development Source: UniProtKB
    21. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    22. positive regulation of osteoblast differentiation Source: UniProtKB
    23. positive regulation of peptidyl-serine phosphorylation Source: Ensembl
    24. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    25. regulation of keratinocyte proliferation Source: UniProtKB

    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

    ReactomeiREACT_196736. Sphingolipid de novo biosynthesis.

    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:Pkcm, Pkd, Prkcm
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 6

    Organism-specific databases

    RGDi620964. Prkd1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cell-cell junction Source: Ensembl
    2. cell cortex Source: Ensembl
    3. cytosol Source: UniProtKB
    4. nucleus Source: Ensembl
    5. plasma membrane Source: UniProtKB
    6. trans-Golgi network Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Golgi apparatus, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 918918Serine/threonine-protein kinase D1PRO_0000333881Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei93 – 931PhosphotyrosineBy similarity
    Modified residuei203 – 2031PhosphoserineBy similarity
    Modified residuei206 – 2061PhosphoserineBy similarity
    Modified residuei351 – 3511PhosphoserineBy similarity
    Modified residuei403 – 4031Phosphoserine; by MAPK13By similarity
    Modified residuei407 – 4071Phosphoserine; by MAPK13By similarity
    Modified residuei438 – 4381PhosphotyrosineBy similarity
    Modified residuei454 – 4541PhosphoserineBy similarity
    Modified residuei469 – 4691Phosphotyrosine; by ABLBy similarity
    Modified residuei508 – 5081PhosphotyrosineBy similarity
    Modified residuei744 – 7441Phosphoserine; by PKC/PRKCDBy similarity
    Modified residuei748 – 7481Phosphoserine; by autocatalysis and PKC/PRKCDBy similarity
    Modified residuei916 – 9161Phosphoserine; by autocatalysis1 Publication

    Post-translational modificationi

    Phosphorylated at Ser-403 and Ser-407 by MAPK13 during regulation of insulin secretion in pancreatic beta cells. Phosphorylated by DAPK1. Phosphorylated by ABL at Tyr-469, which primes the kinase in response to oxidative stress, and promotes a second step activating phosphorylation at Ser-744/Ser-748 by PKRD By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9WTQ1.

    PTM databases

    PhosphoSiteiQ9WTQ1.

    Expressioni

    Gene expression databases

    GenevestigatoriQ9WTQ1.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi250093. 1 interaction.
    IntActiQ9WTQ1. 1 interaction.
    STRINGi10116.ENSRNOP00000005596.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9WTQ1.
    SMRiQ9WTQ1. Positions 425-552.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini428 – 547120PHPROSITE-ProRule annotationAdd
    BLAST
    Domaini589 – 845257Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi16 – 2611Poly-AlaAdd
    BLAST
    Compositional biasi198 – 2014Poly-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 fingeri144 – 19451Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri276 – 32651Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00750000117523.
    HOGENOMiHOG000015135.
    HOVERGENiHBG003564.
    InParanoidiQ9WTQ1.
    KOiK06070.
    OMAiMAECQND.
    OrthoDBiEOG75B84N.
    PhylomeDBiQ9WTQ1.

    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.

    Q9WTQ1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSAPPLLRPP SPLLPAAAAV AAAAAALVPG SGPAPFPAPG AAPAGGISFH    50
    LQIGLSREPV LLLQDSSGDY SLAHVREMAC SIVDQKFPEC GFYGLYDKIL 100
    LFRHDPASEN ILQLVKIASD IQEGDLIEVV LSASATFEDF QIRPHALFVH 150
    SYRAPAFCDH CGEMLWGLVR QGLKCEGCGL NYHKRCAFKI PNNCSGVRRR 200
    RLSNVSLTGL GTVRTASAEF STSAPDEPLL SPVSPGFEQK SPSESFIGRE 250
    KRSNSQSYVG RPIQLDKLLM SKVKVPHTFV IHSYTRPTVC QFCKKLLKGL 300
    FRQGLQCKDC RFNCHKRCAP KVPNNCLGEV TINGELLSPG AESDVVMEEG 350
    SDDNDSERNS GLMDDMDEAM VQDTEMALAE GQSDGAEMQD PDADQEDSNR 400
    TISPSTSNNI PLMRVVQSVK HTKRRSSTVM KEGWMVHYTS KDTLRKRHYW 450
    RLDSKSITLF QNDTGSRYYK EIPLSEILCL EPAKPSALIP TGANPHCFEI 500
    TTANVVYYVG ENVVNPSSPP PNNSVPPSGI GTDVARMWEV AIQHALMPVI 550
    PKGSSVGSGT NSHKDISVSI SVSNSQIQEN VDISTVYQIF PDEVLGSGQF 600
    GIVYGGKHRK TGRDVAIKII DKLRFPTKQE SQLRNEVAIL QNLHHPGVVN 650
    LECMFETPER VFVVMEKLHG DMLEMILSSE KGRLPEHITK FLITQILVAL 700
    RHLHFKNIVH CDLKPENVLL ASADPFPQVK LCDFGFARII GEKSFRRSVV 750
    GTPAYLAPEV LRNKGYNRSL DMWSVGVIIY VSLSGTFPFN EDEDIHDQIQ 800
    NAAFMYPPNP WKEISHEAID LINNLLQVKM RKRYSVDKTL SHPWLQDYQT 850
    WLDLRELECR IGERYITHES DDSRWEQYAG EQGLQYPAHL INLSASHGDS 900
    PEAEEREMKA LSERVSIL 918
    Length:918
    Mass (Da):102,043
    Last modified:May 20, 2008 - v2
    Checksum:i93E46AF6C0242B86
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti718 – 7181V → G in BAA78373. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AABR03048549 Genomic DNA. No translation available.
    AABR03048623 Genomic DNA. No translation available.
    AABR03048825 Genomic DNA. No translation available.
    AABR03049215 Genomic DNA. No translation available.
    AABR03049278 Genomic DNA. No translation available.
    AABR03050321 Genomic DNA. No translation available.
    AABR03052344 Genomic DNA. No translation available.
    AB020616 mRNA. Translation: BAA78373.1.
    RefSeqiNP_001263644.1. NM_001276715.1.
    UniGeneiRn.144619.
    Rn.234516.

    Genome annotation databases

    EnsembliENSRNOT00000068077; ENSRNOP00000063159; ENSRNOG00000004165.
    GeneIDi85421.
    KEGGirno:85421.
    UCSCiRGD:620964. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AABR03048549 Genomic DNA. No translation available.
    AABR03048623 Genomic DNA. No translation available.
    AABR03048825 Genomic DNA. No translation available.
    AABR03049215 Genomic DNA. No translation available.
    AABR03049278 Genomic DNA. No translation available.
    AABR03050321 Genomic DNA. No translation available.
    AABR03052344 Genomic DNA. No translation available.
    AB020616 mRNA. Translation: BAA78373.1 .
    RefSeqi NP_001263644.1. NM_001276715.1.
    UniGenei Rn.144619.
    Rn.234516.

    3D structure databases

    ProteinModelPortali Q9WTQ1.
    SMRi Q9WTQ1. Positions 425-552.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 250093. 1 interaction.
    IntActi Q9WTQ1. 1 interaction.
    STRINGi 10116.ENSRNOP00000005596.

    PTM databases

    PhosphoSitei Q9WTQ1.

    Proteomic databases

    PaxDbi Q9WTQ1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000068077 ; ENSRNOP00000063159 ; ENSRNOG00000004165 .
    GeneIDi 85421.
    KEGGi rno:85421.
    UCSCi RGD:620964. rat.

    Organism-specific databases

    CTDi 5587.
    RGDi 620964. Prkd1.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00750000117523.
    HOGENOMi HOG000015135.
    HOVERGENi HBG003564.
    InParanoidi Q9WTQ1.
    KOi K06070.
    OMAi MAECQND.
    OrthoDBi EOG75B84N.
    PhylomeDBi Q9WTQ1.

    Enzyme and pathway databases

    Reactomei REACT_196736. Sphingolipid de novo biosynthesis.

    Miscellaneous databases

    NextBioi 617508.

    Gene expression databases

    Genevestigatori Q9WTQ1.

    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. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
      Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
      , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
      Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Brown Norway.
    2. "Rat PKC mu mRNA partial cds."
      Minami H., Owada Y., Kondo H.
      Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 718-864.
      Strain: Wistar.
      Tissue: Brain.
    3. "Gbetagamma-mediated regulation of Golgi organization is through the direct activation of protein kinase D."
      Jamora C., Yamanouye N., Van Lint J., Laudenslager J., Vandenheede J.R., Faulkner D.J., Malhotra V.
      Cell 98:59-68(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN GOLGI REGULATION.
    4. "Protein kinase D is a novel mediator of cardiac troponin I phosphorylation and regulates myofilament function."
      Haworth R.S., Cuello F., Herron T.J., Franzen G., Kentish J.C., Gautel M., Avkiran M.
      Circ. Res. 95:1091-1099(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CARDIOMYOCYTE.
    5. "Hepatocyte resistance to oxidative stress is dependent on protein kinase C-mediated down-regulation of c-Jun/AP-1."
      Wang Y., Schattenberg J.M., Rigoli R.M., Storz P., Czaja M.J.
      J. Biol. Chem. 279:31089-31097(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-744; SER-748 AND SER-916.
    6. "Protein kinases C and D mediate agonist-dependent cardiac hypertrophy through nuclear export of histone deacetylase 5."
      Vega R.B., Harrison B.C., Meadows E., Roberts C.R., Papst P.J., Olson E.N., McKinsey T.A.
      Mol. Cell. Biol. 24:8374-8385(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CARDIAC HYPERTROPHY.
    7. "Protein kinase d regulates trafficking of dendritic membrane proteins in developing neurons."
      Bisbal M., Conde C., Donoso M., Bollati F., Sesma J., Quiroga S., Diaz Anel A., Malhotra V., Marzolo M.P., Caceres A.
      J. Neurosci. 28:9297-9308(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NEURONAL POLARITY.

    Entry informationi

    Entry nameiKPCD1_RAT
    AccessioniPrimary (citable) accession number: Q9WTQ1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: May 20, 2008
    Last modified: October 1, 2014
    This is version 89 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3