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P28867

- KPCD_MOUSE

UniProt

P28867 - KPCD_MOUSE

Protein

Protein kinase C delta type

Gene

Prkcd

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 3 (27 Mar 2002)
      Previous versions | rss
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    Functioni

    Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays contrasting roles in cell death and cell survival by functioning as a pro-apoptotic protein during DNA damage-induced apoptosis, but acting as an anti-apoptotic protein during cytokine receptor-initiated cell death, is involved in tumor suppression, is required for oxygen radical production by NADPH oxidase and acts as positive or negative regulator in platelet functional responses. Negatively regulates B cell proliferation and also has an important function in self-antigen induced B cell tolerance induction. Upon DNA damage, activates the promoter of the death-promoting transcription factor BCLAF1/Btf to trigger BCLAF1-mediated p53/TP53 gene transcription and apoptosis. In response to oxidative stress, interact with and activate CHUK/IKKA in the nucleus, causing the phosphorylation of p53/TP53. In the case of ER stress or DNA damage-induced apoptosis, can form a complex with the tyrosine-protein kinase ABL1 which trigger apoptosis independently of p53/TP53. In cytosol can trigger apoptosis by activating MAPK11 or MAPK14, inhibiting AKT1 and decreasing the level of X-linked inhibitor of apoptosis protein (XIAP), whereas in nucleus induces apoptosis via the activation of MAPK8 or MAPK9. Upon ionizing radiation treatment, is required for the activation of the apoptosis regulators BAX and BAK, which trigger the mitochondrial cell death pathway. Can phosphorylate MCL1 and target it for degradation which is sufficient to trigger for BAX activation and apoptosis. Is required for the control of cell cycle progression both at G1/S and G2/M phases. Mediates phorbol 12-myristate 13-acetate (PMA)-induced inhibition of cell cycle progression at G1/S phase by up-regulating the CDK inhibitor CDKN1A/p21 and inhibiting the cyclin CCNA2 promoter activity. In response to UV irradiation can phosphorylate CDK1, which is important for the G2/M DNA damage checkpoint activation. Can protect glioma cells from the apoptosis induced by TNFSF10/TRAIL, probably by inducing increased phosphorylation and subsequent activation of AKT1. Can also act as tumor suppressor upon mitogenic stimulation with PMA or TPA. In N-formyl-methionyl-leucyl-phenylalanine (fMLP)-treated cells, is required for NCF1 (p47-phox) phosphorylation and activation of NADPH oxidase activity, and regulates TNF-elicited superoxide anion production in neutrophils, by direct phosphorylation and activation of NCF1 or indirectly through MAPK1/3 (ERK1/2) signaling pathways. May also play a role in the regulation of NADPH oxidase activity in eosinophil after stimulation with IL5, leukotriene B4 or PMA. In collagen-induced platelet aggregation, acts a negative regulator of filopodia formation and actin polymerization by interacting with and negatively regulating VASP phosphorylation. Downstream of PAR1, PAR4 and CD36/GP4 receptors, regulates differentially platelet dense granule secretion; acts as a positive regulator in PAR-mediated granule secretion, whereas it negatively regulates CD36/GP4-mediated granule release. Phosphorylates MUC1 in the C-terminal and regulates the interaction between MUC1 and beta-catenin. The catalytic subunit phosphorylates 14-3-3 proteins (YWHAB, YWHAZ and YWHAH) in a sphingosine-dependent fashion.5 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.
    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

    Enzyme regulationi

    Novel PKCs (PRKCD, PRKCE, PRKCH and PRKCQ) are calcium-insensitive, but activated by diacylglycerol (DAG) and phosphatidylserine. Three specific sites; Thr-505 (activation loop of the kinase domain), Ser-643 (turn motif) and Ser-662 (hydrophobic region), need to be phosphorylated for its full activation. Activated by caspase-3 (CASP3) cleavage during apoptosis. After cleavage, the pseudosubstrate motif in the regulatory subunit is released from the substrate recognition site of the catalytic subunit, which enables PRKCD to become constitutively activated. The catalytic subunit which displays properties of a sphingosine-dependent protein kinase is activated by D-erythro-sphingosine (Sph) or N,N-dimethyl-D-erythrosphingosine (DMS) or N,N,N-trimethyl-D-erythrosphingosine (TMS), but not by ceramide or Sph-1-P and is strongly inhibited by phosphatidylserine By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei48 – 481Interaction with phosphotyrosine-containing peptideBy similarity
    Sitei62 – 621Interaction with phosphotyrosine-containing peptideBy similarity
    Sitei67 – 671Interaction with phosphotyrosine-containing peptideBy similarity
    Sitei123 – 1231Interaction with phosphotyrosine-containing peptideBy similarity
    Sitei327 – 3282Cleavage; by caspase-3By similarity
    Binding sitei376 – 3761ATPPROSITE-ProRule annotation
    Active sitei471 – 4711Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri158 – 20851Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri230 – 28051Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
    BLAST
    Nucleotide bindingi353 – 3619ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. enzyme activator activity Source: Ensembl
    3. insulin receptor substrate binding Source: BHF-UCL
    4. metal ion binding Source: UniProtKB-KW
    5. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
    6. protein kinase C activity Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. B cell proliferation Source: MGI
    3. cell cycle Source: UniProtKB-KW
    4. cellular senescence Source: Ensembl
    5. defense response to bacterium Source: UniProtKB
    6. immunoglobulin mediated immune response Source: MGI
    7. interleukin-10 production Source: MGI
    8. interleukin-12 production Source: MGI
    9. intracellular signal transduction Source: InterPro
    10. negative regulation of actin filament polymerization Source: UniProtKB
    11. negative regulation of filopodium assembly Source: UniProtKB
    12. negative regulation of glial cell apoptotic process Source: UniProtKB
    13. negative regulation of insulin receptor signaling pathway Source: BHF-UCL
    14. negative regulation of MAP kinase activity Source: Ensembl
    15. negative regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
    16. negative regulation of platelet aggregation Source: UniProtKB
    17. neutrophil activation Source: Ensembl
    18. peptidyl-threonine phosphorylation Source: Ensembl
    19. positive regulation of apoptotic signaling pathway Source: MGI
    20. positive regulation of ceramide biosynthetic process Source: Ensembl
    21. positive regulation of glucosylceramide catabolic process Source: Ensembl
    22. positive regulation of phospholipid scramblase activity Source: Ensembl
    23. positive regulation of protein dephosphorylation Source: Ensembl
    24. positive regulation of response to DNA damage stimulus Source: Ensembl
    25. positive regulation of sphingomyelin catabolic process Source: Ensembl
    26. positive regulation of superoxide anion generation Source: UniProtKB
    27. termination of signal transduction Source: Ensembl

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Apoptosis, Cell cycle

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BRENDAi2.7.11.13. 3474.
    ReactomeiREACT_188269. DAG and IP3 signaling.
    REACT_198660. Interferon gamma signaling.
    REACT_198691. HuR stabilizes mRNA.
    REACT_210240. Role of phospholipids in phagocytosis.
    REACT_215587. Calmodulin induced events.
    REACT_219232. Effects of PIP2 hydrolysis.
    REACT_224460. Apoptotic cleavage of cellular proteins.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein kinase C delta type (EC:2.7.11.13)
    Alternative name(s):
    Tyrosine-protein kinase PRKCD (EC:2.7.10.2)
    nPKC-delta
    Cleaved into the following 2 chains:
    Alternative name(s):
    Sphingosine-dependent protein kinase-1
    Short name:
    SDK1
    Gene namesi
    Name:Prkcd
    Synonyms:Pkcd
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 14

    Organism-specific databases

    MGIiMGI:97598. Prkcd.

    Subcellular locationi

    Cytoplasm By similarity. Cytoplasmperinuclear region By similarity. Nucleus By similarity. Endoplasmic reticulum By similarity. Mitochondrion By similarity. Membrane By similarity; Peripheral membrane protein By similarity

    GO - Cellular componenti

    1. cell-cell junction Source: MGI
    2. cytoplasm Source: MGI
    3. endoplasmic reticulum Source: UniProtKB
    4. membrane Source: UniProtKB-SubCell
    5. mitochondrion Source: UniProtKB-SubCell
    6. nuclear matrix Source: MGI
    7. nucleus Source: MGI
    8. perinuclear region of cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Membrane, Mitochondrion, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Mice are viable up to 1 year despite detection of auto-immune disease in these animals. They exhibit glomerulonephritis, splenomegaly and lymphadenopathy associated with B-cell expansion and defective B-cell tolerance to self-antigen.1 Publication

    Keywords - Diseasei

    Tumor suppressor

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 674674Protein kinase C delta typePRO_0000055695Add
    BLAST
    Chaini1 – 327327Protein kinase C delta type regulatory subunitBy similarityPRO_0000421669Add
    BLAST
    Chaini328 – 674347Protein kinase C delta type catalytic subunitBy similarityPRO_0000421670Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei43 – 431Phosphothreonine1 Publication
    Modified residuei64 – 641PhosphotyrosineBy similarity
    Modified residuei130 – 1301PhosphoserineBy similarity
    Modified residuei155 – 1551PhosphotyrosineBy similarity
    Modified residuei218 – 2181PhosphothreonineBy similarity
    Modified residuei299 – 2991Phosphoserine; by autocatalysisBy similarity
    Modified residuei311 – 3111Phosphotyrosine; alternate4 Publications
    Modified residuei311 – 3111Phosphotyrosine; by SRC; alternate4 Publications
    Modified residuei332 – 3321Phosphotyrosine; by SRCBy similarity
    Modified residuei372 – 3721PhosphotyrosineBy similarity
    Modified residuei505 – 5051Phosphothreonine; by autocatalysis2 Publications
    Modified residuei565 – 5651PhosphotyrosineBy similarity
    Modified residuei643 – 6431PhosphoserineCurated
    Modified residuei652 – 6521PhosphoserineBy similarity
    Modified residuei662 – 6621Phosphoserine1 Publication

    Post-translational modificationi

    Autophosphorylated and/or phosphorylated at Thr-505, within the activation loop; phosphorylation at Thr-505 is not a prerequisite for enzymatic activity. Autophosphorylated at Ser-299. Upon TNFSF10/TRAIL treatment, phosphorylated at Tyr-155; phosphorylation is required for its translocation to the endoplasmic reticulum and cleavage by caspase-3. Phosphorylated at Tyr-311, Tyr-332 and Tyr-565; phosphorylation of Tyr-311 and Tyr-565 following thrombin stimulation potentiates its kinase activity. Phosphorylated by protein kinase PDPK1; phosphorylation is inhibited by the apoptotic C-terminal cleavage product of PKN2 By similarity.By similarity
    Proteolytically cleaved into a catalytic subunit and a regulatory subunit by caspase-3 during apoptosis which results in kinase activation.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP28867.
    PaxDbiP28867.
    PRIDEiP28867.

    PTM databases

    PhosphoSiteiP28867.

    Expressioni

    Tissue specificityi

    Isoform 1 is highly expressed in developing pro- and pre-B-cells and moderately in mature T-cells. Isoform 2 is highly expressed in testis and ovary and at a lower level in thymocytes, brain and kidney.

    Gene expression databases

    ArrayExpressiP28867.
    BgeeiP28867.
    CleanExiMM_PRKCD.
    GenevestigatoriP28867.

    Interactioni

    Subunit structurei

    Interacts with PDPK1 (via N-terminal region), RAD9A, CDCP1, MUC1 and VASP.By similarity

    Protein-protein interaction databases

    BioGridi202197. 7 interactions.
    DIPiDIP-1169N.
    IntActiP28867. 3 interactions.
    MINTiMINT-97906.

    Structurei

    Secondary structure

    1
    674
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi233 – 2364
    Turni245 – 2473
    Beta strandi253 – 2564
    Beta strandi258 – 2614
    Turni262 – 2643
    Helixi270 – 2734
    Beta strandi278 – 2803

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1PTQX-ray1.95A231-280[»]
    1PTRX-ray2.20A231-280[»]
    3UEJX-ray1.30A/B231-280[»]
    3UEYX-ray1.30A/B231-280[»]
    3UFFX-ray1.30A/B231-280[»]
    3UGDX-ray1.45A/B231-280[»]
    3UGIX-ray1.36A/B231-280[»]
    3UGLX-ray1.36A/B231-280[»]
    ProteinModelPortaliP28867.
    SMRiP28867. Positions 1-123, 149-666.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP28867.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 9090C2Add
    BLAST
    Domaini347 – 601255Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini602 – 67372AGC-kinase C-terminalAdd
    BLAST

    Domaini

    The C1 domain, containing the phorbol ester/DAG-type region 1 (C1A) and 2 (C1B), is the diacylglycerol sensor.
    The C2 domain is a non-calcium binding domain. It binds proteins containing phosphotyrosine in a sequence-specific manner By similarity.By similarity

    Sequence similaritiesi

    Contains 1 AGC-kinase C-terminal domain.Curated
    Contains 1 C2 domain.Curated
    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 fingeri158 – 20851Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri230 – 28051Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00750000117339.
    HOGENOMiHOG000233022.
    HOVERGENiHBG108317.
    KOiK06068.
    OMAiGEDEAKF.
    OrthoDBiEOG77M8QM.
    PhylomeDBiP28867.
    TreeFamiTF102004.

    Family and domain databases

    Gene3Di2.60.40.150. 1 hit.
    InterProiIPR000961. AGC-kinase_C.
    IPR000008. C2_dom.
    IPR020454. DAG/PE-bd.
    IPR011009. Kinase-like_dom.
    IPR027436. PKC_delta.
    IPR017892. Pkinase_C.
    IPR014376. Prot_kin_PKC_delta.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00130. C1_1. 2 hits.
    PF00069. Pkinase. 1 hit.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000551. PKC_delta. 1 hit.
    PIRSF501104. Protein_kin_C_delta. 1 hit.
    PRINTSiPR00008. DAGPEDOMAIN.
    SMARTiSM00109. C1. 2 hits.
    SM00239. C2. 1 hit.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49562. SSF49562. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS51285. AGC_KINASE_CTER. 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]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P28867-1) [UniParc]FASTAAdd to Basket

    Also known as: PKC-delta-I

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAPFLRISFN SYELGSLQVE DEASQPFCAV KMKEALSTER GKTLVQKKPT    50
    MYPEWKTTFD AHIYEGRVIQ IVLMRAAEDP VSEVTVGVSV LAERCKKNNG 100
    KAEFWLDLQP QAKVLMCVQY FLEDGDCKQS MRSEEEAKFP TMNRRGAIKQ 150
    AKIHYIKNHE FIATFFGQPT FCSVCKEFVW GLNKQGYKCR QCNAAIHKKC 200
    IDKIIGRCTG TATNSRDTIF QKERFNIDMP HRFKVYNYMS PTFCDHCGSL 250
    LWGLVKQGLK CEDCGMNVHH KCREKVANLC GINQKLLAEA LNQVTQRSSR 300
    KLDTTESVGI YQGFEKKPEV SGSDILDNNG TYGKIWEGST RCTLENFTFQ 350
    KVLGKGSFGK VLLAELKGKD KYFAIKCLKK DVVLIDDDVE CTMVEKRVLA 400
    LAWESPFLTH LICTFQTKDH LFFVMEFLNG GDLMFHIQDK GRFELYRATF 450
    YAAEIICGLQ FLHSKGIIYR DLKLDNVMLD RDGHIKIADF GMCKENIFGE 500
    GRASTFCGTP DYIAPEILQG LKYSFSVDWW SFGVLLYEML IGQSPFHGDD 550
    EDELFESIRV DTPHYPRWIT KESKDIMEKL FERDPDKRLG VTGNIRIHPF 600
    FKTINWSLLE KRKVEPPFKP KVKSPSDYSN FDPEFLNEKP QLSFSDKNLI 650
    DSMDQEAFHG FSFVNPKFEQ FLDI 674
    Length:674
    Mass (Da):77,547
    Last modified:March 27, 2002 - v3
    Checksum:i6E9F753348F03D59
    GO
    Isoform 2 (identifier: P28867-2) [UniParc]FASTAAdd to Basket

    Also known as: PKC-delta-II

    The sequence of this isoform differs from the canonical sequence as follows:
         326-326: L → LGEAGSHISLKLSFPSRAKEKDSSETC

    Show »
    Length:700
    Mass (Da):80,294
    Checksum:iCFB6D8A58220C962
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti214 – 2141N → I in BAA36408. (PubMed:11558579)Curated
    Sequence conflicti226 – 2261N → S in BAA36408. (PubMed:11558579)Curated
    Sequence conflicti319 – 3191E → D in AAA73056. (PubMed:1868068)Curated
    Sequence conflicti330 – 3301G → W in AAA73056. (PubMed:1868068)Curated
    Sequence conflicti337 – 3371E → V in AAA73056. (PubMed:1868068)Curated
    Sequence conflicti501 – 5011G → D in AAA73056. (PubMed:1868068)Curated
    Sequence conflicti503 – 5031A → P in AAA73056. (PubMed:1868068)Curated
    Sequence conflicti513 – 5131I → S in AAA73056. (PubMed:1868068)Curated
    Sequence conflicti518 – 5203LQG → PARA in BAA36408. (PubMed:11558579)Curated
    Sequence conflicti538 – 5381E → R in BAA36408. (PubMed:11558579)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei326 – 3261L → LGEAGSHISLKLSFPSRAKE KDSSETC in isoform 2. 1 PublicationVSP_004741

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M69042 mRNA. Translation: AAA73056.1.
    X60304 mRNA. Translation: CAA42845.1.
    AF274044 Genomic DNA. Translation: AAF79208.1.
    AF251036 mRNA. Translation: AAF64316.1.
    AB011812 mRNA. Translation: BAA36408.1.
    CCDSiCCDS26895.1. [P28867-1]
    PIRiA40281. KIMSCD.
    RefSeqiNP_035233.1. NM_011103.3. [P28867-1]
    XP_006518758.1. XM_006518695.1. [P28867-2]
    XP_006518759.1. XM_006518696.1. [P28867-2]
    UniGeneiMm.2314.

    Genome annotation databases

    EnsembliENSMUST00000022521; ENSMUSP00000022521; ENSMUSG00000021948. [P28867-2]
    ENSMUST00000112208; ENSMUSP00000107827; ENSMUSG00000021948. [P28867-1]
    ENSMUST00000112210; ENSMUSP00000107829; ENSMUSG00000021948. [P28867-1]
    ENSMUST00000112211; ENSMUSP00000107830; ENSMUSG00000021948. [P28867-2]
    GeneIDi18753.
    KEGGimmu:18753.
    UCSCiuc007sve.2. mouse. [P28867-1]
    uc007svg.2. mouse. [P28867-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M69042 mRNA. Translation: AAA73056.1 .
    X60304 mRNA. Translation: CAA42845.1 .
    AF274044 Genomic DNA. Translation: AAF79208.1 .
    AF251036 mRNA. Translation: AAF64316.1 .
    AB011812 mRNA. Translation: BAA36408.1 .
    CCDSi CCDS26895.1. [P28867-1 ]
    PIRi A40281. KIMSCD.
    RefSeqi NP_035233.1. NM_011103.3. [P28867-1 ]
    XP_006518758.1. XM_006518695.1. [P28867-2 ]
    XP_006518759.1. XM_006518696.1. [P28867-2 ]
    UniGenei Mm.2314.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1PTQ X-ray 1.95 A 231-280 [» ]
    1PTR X-ray 2.20 A 231-280 [» ]
    3UEJ X-ray 1.30 A/B 231-280 [» ]
    3UEY X-ray 1.30 A/B 231-280 [» ]
    3UFF X-ray 1.30 A/B 231-280 [» ]
    3UGD X-ray 1.45 A/B 231-280 [» ]
    3UGI X-ray 1.36 A/B 231-280 [» ]
    3UGL X-ray 1.36 A/B 231-280 [» ]
    ProteinModelPortali P28867.
    SMRi P28867. Positions 1-123, 149-666.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202197. 7 interactions.
    DIPi DIP-1169N.
    IntActi P28867. 3 interactions.
    MINTi MINT-97906.

    Chemistry

    BindingDBi P28867.
    ChEMBLi CHEMBL2560.

    PTM databases

    PhosphoSitei P28867.

    Proteomic databases

    MaxQBi P28867.
    PaxDbi P28867.
    PRIDEi P28867.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000022521 ; ENSMUSP00000022521 ; ENSMUSG00000021948 . [P28867-2 ]
    ENSMUST00000112208 ; ENSMUSP00000107827 ; ENSMUSG00000021948 . [P28867-1 ]
    ENSMUST00000112210 ; ENSMUSP00000107829 ; ENSMUSG00000021948 . [P28867-1 ]
    ENSMUST00000112211 ; ENSMUSP00000107830 ; ENSMUSG00000021948 . [P28867-2 ]
    GeneIDi 18753.
    KEGGi mmu:18753.
    UCSCi uc007sve.2. mouse. [P28867-1 ]
    uc007svg.2. mouse. [P28867-2 ]

    Organism-specific databases

    CTDi 5580.
    MGIi MGI:97598. Prkcd.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00750000117339.
    HOGENOMi HOG000233022.
    HOVERGENi HBG108317.
    KOi K06068.
    OMAi GEDEAKF.
    OrthoDBi EOG77M8QM.
    PhylomeDBi P28867.
    TreeFami TF102004.

    Enzyme and pathway databases

    BRENDAi 2.7.11.13. 3474.
    Reactomei REACT_188269. DAG and IP3 signaling.
    REACT_198660. Interferon gamma signaling.
    REACT_198691. HuR stabilizes mRNA.
    REACT_210240. Role of phospholipids in phagocytosis.
    REACT_215587. Calmodulin induced events.
    REACT_219232. Effects of PIP2 hydrolysis.
    REACT_224460. Apoptotic cleavage of cellular proteins.

    Miscellaneous databases

    ChiTaRSi PRKCD. mouse.
    EvolutionaryTracei P28867.
    NextBioi 294929.
    PROi P28867.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P28867.
    Bgeei P28867.
    CleanExi MM_PRKCD.
    Genevestigatori P28867.

    Family and domain databases

    Gene3Di 2.60.40.150. 1 hit.
    InterProi IPR000961. AGC-kinase_C.
    IPR000008. C2_dom.
    IPR020454. DAG/PE-bd.
    IPR011009. Kinase-like_dom.
    IPR027436. PKC_delta.
    IPR017892. Pkinase_C.
    IPR014376. Prot_kin_PKC_delta.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00130. C1_1. 2 hits.
    PF00069. Pkinase. 1 hit.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000551. PKC_delta. 1 hit.
    PIRSF501104. Protein_kin_C_delta. 1 hit.
    PRINTSi PR00008. DAGPEDOMAIN.
    SMARTi SM00109. C1. 2 hits.
    SM00239. C2. 1 hit.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49562. SSF49562. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS51285. AGC_KINASE_CTER. 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. "Mouse protein kinase C-delta, the major isoform expressed in mouse hemopoietic cells: sequence of the cDNA, expression patterns, and characterization of the protein."
      Mischak H., Bodenteich A., Kolch W., Goodnight J., Hofer F., Mushinski J.F.
      Biochemistry 30:7925-7931(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Structure and properties of a ubiquitously expressed protein kinase C, nPKC delta."
      Mizuno K., Kubo K., Saido T.C., Akita Y., Osada S., Kuroki T., Ohno S., Suzuki K.
      Eur. J. Biochem. 202:931-940(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: ICR.
      Tissue: Brain.
    3. "Intron/exon structure of the murine protein kinase C delta gene."
      Wheeler D.L., Gillis M.E., Verma A.K.
      Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
      Strain: 129/SvJ.
    4. "Novel protein kinase C delta isoform insensitive to caspase-3."
      Sakurai Y., Onishi Y., Tanimoto Y., Kizaki H.
      Biol. Pharm. Bull. 24:973-977(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    5. "A novel sphingosine-dependent protein kinase (SDK1) specifically phosphorylates certain isoforms of 14-3-3 protein."
      Megidish T., Cooper J., Zhang L., Fu H., Hakomori S.
      J. Biol. Chem. 273:21834-21845(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Protein kinase Cdelta controls self-antigen-induced B-cell tolerance."
      Mecklenbraeuker I., Saijo K., Zheng N.Y., Leitges M., Tarakhovsky A.
      Nature 416:860-865(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1."
      Le Good J.A., Ziegler W.H., Parekh D.B., Alessi D.R., Cohen P., Parker P.J.
      Science 281:2042-2045(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-505.
    8. "Increased proliferation of B cells and auto-immunity in mice lacking protein kinase Cdelta."
      Miyamoto A., Nakayama K., Imaki H., Hirose S., Jiang Y., Abe M., Tsukiyama T., Nagahama H., Ohno S., Hatakeyama S., Nakayama K.I.
      Nature 416:865-869(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION IN B CELL PROLIFERATION, FUNCTION IN B-CELL IMMUNE RESPONSES.
    9. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
      Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
      J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-311, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Mast cell.
    10. "A critical role of protein kinase C delta activation loop phosphorylation in formyl-methionyl-leucyl-phenylalanine-induced phosphorylation of p47(phox) and rapid activation of nicotinamide adenine dinucleotide phosphate oxidase."
      Cheng N., He R., Tian J., Dinauer M.C., Ye R.D.
      J. Immunol. 179:7720-7728(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT THR-505.
    11. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
      Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
      J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-311, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    12. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-43; TYR-311 AND SER-662, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-311, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    14. "The protein kinase Cdelta catalytic fragment is critical for maintenance of the G2/M DNA damage checkpoint."
      LaGory E.L., Sitailo L.A., Denning M.F.
      J. Biol. Chem. 285:1879-1887(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF CDK1.
    15. "Crystal structure of the cys2 activator-binding domain of protein kinase C delta in complex with phorbol ester."
      Zhang G., Kazanietz M.G., Blumberg P.M., Hurley J.H.
      Cell 81:917-924(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 231-280 IN COMPLEX WITH PHORBOL ESTER AND ZINC IONS.

    Entry informationi

    Entry nameiKPCD_MOUSE
    AccessioniPrimary (citable) accession number: P28867
    Secondary accession number(s): Q91V85, Q9Z333
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: March 27, 2002
    Last modified: October 1, 2014
    This is version 156 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3