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Q8BZ03

- KPCD2_MOUSE

UniProt

Q8BZ03 - KPCD2_MOUSE

Protein

Serine/threonine-protein kinase D2

Gene

Prkd2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      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-439 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.2 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-711 and phosphorylation of Ser-707 by PKC relieves auto-inhibition by the PH domain By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei581 – 5811ATPPROSITE-ProRule annotation
    Active sitei675 – 6751Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri138 – 18851Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri265 – 31551Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
    BLAST
    Nucleotide bindingi558 – 5669ATPPROSITE-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

    GO - Biological processi

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

    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

    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:2141917. Prkd2.

    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. 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.By similarity

    GO - Cellular componenti

    1. Golgi apparatus Source: UniProtKB-SubCell
    2. nucleus Source: Ensembl
    3. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Golgi apparatus, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi707 – 7071S → A: Strong decrease in catalytic activity; when associated with A-711. 1 Publication
    Mutagenesisi711 – 7111S → A: Strong decrease in catalytic activity; when associated with A-707. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 875875Serine/threonine-protein kinase D2PRO_0000260436Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei200 – 2001PhosphoserineBy similarity
    Modified residuei203 – 2031PhosphoserineBy similarity
    Modified residuei206 – 2061PhosphoserineBy similarity
    Modified residuei214 – 2141PhosphoserineBy similarity
    Modified residuei244 – 2441Phosphoserine; by CSNK1D and CSNK1EBy similarity
    Modified residuei439 – 4391Phosphotyrosine; by ABL1By similarity
    Modified residuei519 – 5191PhosphoserineBy similarity
    Modified residuei707 – 7071Phosphoserine; by PKC1 Publication
    Modified residuei711 – 7111Phosphoserine; by autocatalysis1 Publication
    Modified residuei718 – 7181PhosphotyrosineBy similarity
    Modified residuei873 – 8731Phosphoserine; by autocatalysis1 Publication

    Post-translational modificationi

    Phosphorylation of Ser-873 correlates with the activation status of the kinase. Ser-707 is probably phosphorylated by PKC. Phosphorylation at Ser-244 by CSNK1D and CSNK1E promotes nuclear localization and substrate targeting. Phosphorylation at Ser-244, Ser-707 and Ser-711 is required for nuclear localization. Phosphorylated at Tyr-438 by ABL1 in response to oxidative stress By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8BZ03.
    PaxDbiQ8BZ03.
    PRIDEiQ8BZ03.

    PTM databases

    PhosphoSiteiQ8BZ03.

    Expressioni

    Gene expression databases

    BgeeiQ8BZ03.
    CleanExiMM_PRKD2.
    GenevestigatoriQ8BZ03.

    Interactioni

    Subunit structurei

    Interacts (via C-terminus) with LCK.By similarity

    Protein-protein interaction databases

    IntActiQ8BZ03. 1 interaction.
    MINTiMINT-4113563.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BZ03.
    SMRiQ8BZ03. Positions 138-188, 266-358, 396-510, 518-823.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini398 – 510113PHPROSITE-ProRule annotationAdd
    BLAST
    Domaini552 – 808257Protein 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 fingeri265 – 31551Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00750000117523.
    HOGENOMiHOG000015135.
    HOVERGENiHBG003564.
    InParanoidiQ8BZ03.
    KOiK06070.
    OMAiLPQDHEM.
    OrthoDBiEOG75B84N.
    PhylomeDBiQ8BZ03.
    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.

    Q8BZ03-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAAPSHPAG LPGSPGPGSP PPPGGLDLQS PPPLLPQIPA PGSGVSFHIQ    50
    IGLTREFVLL PAASELAHVK QLACSIVDQK FPECGFYGLY DKILLFKHDP 100
    TSANLLQLVR SAADIQEGDL VEVVLSASAT FEDFQIRPHA LTVHSYRAPA 150
    FCDHCGEMLF GLVRQGLKCD GCGLNYHKRC AFSIPNNCSG ARKRRLSSTS 200
    LASGHSVRLG SSESLPCTAE ELSRSTTDLL PRRPPSSSSS SSSSSFYTGR 250
    PIELDKMLMS KVKVPHTFLI HSYTRPTVCQ ACKKLLKGLF RQGLQCKDCK 300
    FNCHKRCATR VPNDCLGEAL INGDVPMEEA ADYSEADKSS ISDELEDSGV 350
    IPGSHSESAL HASEEEEGEG HKAQSSLGYI PLMRVVQSVR HTTRKSSTTL 400
    REGWVVHYSN KDTLRKRHYW RLDCKCITLF QNNTTNRYYK EIPLSEILAV 450
    EPAQNFSLVP PGTNPHCFEI ITANVTYFVG ETPGGAPGGP SGQGTEAVRG 500
    WETAIRQALM PVILQDAPSA PGHTPHRQAS LSISVSNSQI QENVDIATVY 550
    QIFPDEVLGS GQFGVVYGGK HRKTGRDVAV KVIDKLRFPT KQESQLRNEV 600
    AILQSLRHPG IVNLECMFET PEKVFVVMEK LHGDMLEMIL SSEKGRLPER 650
    LTKFLITQIL VALRHLHFKN IVHCDLKPEN VLLASADPFP QVKLCDFGFA 700
    RIIGEKSFRR SVVGTPAYLA PEVLLNQGYN RSLDMWSVGV IMYVSLSGTF 750
    PFNEDEDIND QIQNAAFMYP ASPWSHISSG AIDLINNLLQ VKMRKRYSVD 800
    KSLSHPWLQE YQTWLDLREL EGKMGERYIT HESDDARWDQ FVAERHGTPA 850
    EGDLGGACLP QDHEMQGLAE RISIL 875
    Length:875
    Mass (Da):96,542
    Last modified:March 1, 2003 - v1
    Checksum:iC7173546FA1E6DB1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti213 – 2131E → G in BAE42012. (PubMed:16141072)Curated
    Sequence conflicti220 – 2201E → G in BAE41652. (PubMed:16141072)Curated
    Sequence conflicti310 – 3101R → H in BAE32326. (PubMed:16141072)Curated
    Sequence conflicti310 – 3101R → H in BAE41652. (PubMed:16141072)Curated
    Sequence conflicti630 – 6301K → N in BAE42012. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK037030 mRNA. Translation: BAC29677.1.
    AK154029 mRNA. Translation: BAE32326.1.
    AK170236 mRNA. Translation: BAE41652.1.
    AK170761 mRNA. Translation: BAE42012.1.
    BC095949 mRNA. Translation: AAH95949.1.
    BC096444 mRNA. Translation: AAH96444.1.
    CCDSiCCDS20855.1.
    RefSeqiNP_001239387.1. NM_001252458.1.
    NP_849231.1. NM_178900.4.
    UniGeneiMm.1881.
    Mm.488710.

    Genome annotation databases

    EnsembliENSMUST00000086104; ENSMUSP00000083273; ENSMUSG00000041187.
    ENSMUST00000168093; ENSMUSP00000131192; ENSMUSG00000041187.
    GeneIDi101540.
    KEGGimmu:101540.
    UCSCiuc009fig.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK037030 mRNA. Translation: BAC29677.1 .
    AK154029 mRNA. Translation: BAE32326.1 .
    AK170236 mRNA. Translation: BAE41652.1 .
    AK170761 mRNA. Translation: BAE42012.1 .
    BC095949 mRNA. Translation: AAH95949.1 .
    BC096444 mRNA. Translation: AAH96444.1 .
    CCDSi CCDS20855.1.
    RefSeqi NP_001239387.1. NM_001252458.1.
    NP_849231.1. NM_178900.4.
    UniGenei Mm.1881.
    Mm.488710.

    3D structure databases

    ProteinModelPortali Q8BZ03.
    SMRi Q8BZ03. Positions 138-188, 266-358, 396-510, 518-823.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q8BZ03. 1 interaction.
    MINTi MINT-4113563.

    PTM databases

    PhosphoSitei Q8BZ03.

    Proteomic databases

    MaxQBi Q8BZ03.
    PaxDbi Q8BZ03.
    PRIDEi Q8BZ03.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000086104 ; ENSMUSP00000083273 ; ENSMUSG00000041187 .
    ENSMUST00000168093 ; ENSMUSP00000131192 ; ENSMUSG00000041187 .
    GeneIDi 101540.
    KEGGi mmu:101540.
    UCSCi uc009fig.2. mouse.

    Organism-specific databases

    CTDi 25865.
    MGIi MGI:2141917. Prkd2.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00750000117523.
    HOGENOMi HOG000015135.
    HOVERGENi HBG003564.
    InParanoidi Q8BZ03.
    KOi K06070.
    OMAi LPQDHEM.
    OrthoDBi EOG75B84N.
    PhylomeDBi Q8BZ03.
    TreeFami TF314320.

    Miscellaneous databases

    NextBioi 355000.
    PROi Q8BZ03.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8BZ03.
    CleanExi MM_PRKD2.
    Genevestigatori Q8BZ03.

    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. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
      Tissue: Thymus and Vagina.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: FVB/N.
      Tissue: Colon and Mammary tumor.
    3. "Protein kinase D2 potentiates MEK/ERK/RSK signaling, c-Fos accumulation and DNA synthesis induced by bombesin in Swiss 3T3 cells."
      Sinnett-Smith J., Zhukova E., Rey O., Rozengurt E.
      J. Cell. Physiol. 211:781-790(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL PROLIFERATION.
    4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    5. "Unique functions for protein kinase D1 and protein kinase D2 in mammalian cells."
      Matthews S.A., Navarro M.N., Sinclair L.V., Emslie E., Feijoo-Carnero C., Cantrell D.A.
      Biochem. J. 432:153-163(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN T-CELLS, PHOSPHORYLATION AT SER-707; SER-711 AND SER-873, MUTAGENESIS OF SER-707 AND SER-711.

    Entry informationi

    Entry nameiKPCD2_MOUSE
    AccessioniPrimary (citable) accession number: Q8BZ03
    Secondary accession number(s): Q3TCE5, Q3TDF0, Q3U4V4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2006
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 115 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3