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P09215

- KPCD_RAT

UniProt

P09215 - KPCD_RAT

Protein

Protein kinase C delta type

Gene

Prkcd

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 165 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      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. 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 By similarity. The catalytic subunit phosphorylates 14-3-3 proteins (YWHAB, YWHAZ and YWHAH) in a sphingosine-dependent fashion By similarity.By similarity
    Truncated isoform 2 is inactive.

    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.1 Publication

    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-3Curated
    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. calcium-independent protein kinase C activity Source: RGD
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: RGD
    5. protein kinase binding Source: RGD
    6. protein kinase C activity Source: UniProtKB
    7. TIR domain binding Source: BHF-UCL

    GO - Biological processi

    1. aging Source: RGD
    2. apoptotic process Source: UniProtKB-KW
    3. aspartate transport Source: RGD
    4. cell cycle Source: UniProtKB-KW
    5. cellular response to glucose starvation Source: RGD
    6. cellular response to insulin stimulus Source: RGD
    7. collagen metabolic process Source: RGD
    8. defense response to bacterium Source: UniProtKB
    9. intracellular signal transduction Source: RGD
    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 platelet aggregation Source: UniProtKB
    14. positive regulation of apoptotic process Source: RGD
    15. positive regulation of glucose import Source: RGD
    16. positive regulation of MAPK cascade Source: RGD
    17. positive regulation of MAP kinase activity Source: RGD
    18. positive regulation of superoxide anion generation Source: UniProtKB
    19. protein autophosphorylation Source: RGD
    20. protein phosphorylation Source: RGD
    21. response to amino acid Source: RGD
    22. response to drug Source: RGD
    23. response to ethanol Source: RGD
    24. response to glucose Source: RGD
    25. response to heat Source: RGD
    26. response to hydrogen peroxide Source: RGD
    27. response to hypoxia Source: RGD
    28. response to mechanical stimulus Source: RGD
    29. response to organic cyclic compound Source: RGD
    30. response to organonitrogen compound Source: RGD
    31. response to oxidative stress Source: RGD

    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. 5301.
    ReactomeiREACT_194374. Role of phospholipids in phagocytosis.
    REACT_196423. HuR stabilizes mRNA.
    REACT_196446. Interferon gamma signaling.
    REACT_220575. DAG and IP3 signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein kinase C delta type (EC:2.7.11.13)
    Alternative name(s):
    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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi67383. Prkcd.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication. Cytoplasmperinuclear region 1 Publication. Endoplasmic reticulum By similarity. Mitochondrion By similarity. Membrane 1 Publication; Peripheral membrane protein 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: RGD
    2. cytosol Source: RGD
    3. endoplasmic reticulum Source: UniProtKB
    4. membrane Source: RGD
    5. mitochondrion Source: RGD
    6. nucleus Source: RGD
    7. perinuclear region of cytoplasm Source: UniProtKB-SubCell
    8. plasma membrane Source: RGD

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Membrane, Mitochondrion, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi505 – 5051T → A: Decrease in the phosphorylation level. 1 Publication

    Keywords - Diseasei

    Tumor suppressor

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 673673Protein kinase C delta typePRO_0000055696Add
    BLAST
    Chaini1 – 327327Protein kinase C delta type regulatory subunitPRO_0000421671Add
    BLAST
    Chaini328 – 673346Protein kinase C delta type catalytic subunitPRO_0000421672Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei43 – 431PhosphothreonineBy similarity
    Modified residuei64 – 641Phosphotyrosine1 Publication
    Modified residuei130 – 1301PhosphoserineBy similarity
    Modified residuei155 – 1551Phosphotyrosine1 Publication
    Modified residuei218 – 2181PhosphothreonineBy similarity
    Modified residuei299 – 2991Phosphoserine; by autocatalysisBy similarity
    Modified residuei311 – 3111Phosphotyrosine; by SRC1 Publication
    Modified residuei332 – 3321Phosphotyrosine; by SRC1 Publication
    Modified residuei372 – 3721PhosphotyrosineBy similarity
    Modified residuei505 – 5051Phosphothreonine; by autocatalysis3 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. Phosphorylated at Tyr-311 and Tyr-332 by SRC; phosphorylation leads to enhanced autophosphorylation at Thr-505.By similarity6 Publications
    Proteolytically cleaved into a catalytic subunit and a regulatory subunit by caspase-3 during apoptosis which results in kinase activation.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP09215.
    PRIDEiP09215.

    PTM databases

    PhosphoSiteiP09215.

    Miscellaneous databases

    PMAP-CutDBP09215.

    Expressioni

    Gene expression databases

    GenevestigatoriP09215.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi250924. 8 interactions.
    IntActiP09215. 2 interactions.
    MINTiMINT-143019.

    Structurei

    Secondary structure

    1
    673
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 1311
    Beta strandi27 – 359
    Helixi38 – 403
    Beta strandi43 – 464
    Beta strandi58 – 625
    Beta strandi68 – 769
    Beta strandi79 – 879
    Helixi88 – 969
    Turni97 – 1004
    Beta strandi101 – 1077
    Beta strandi109 – 1113
    Beta strandi113 – 12210

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BDYX-ray2.20A/B1-123[»]
    ProteinModelPortaliP09215.
    SMRiP09215. Positions 1-123, 149-218, 227-283, 343-666.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP09215.

    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.
    HOGENOMiHOG000233022.
    HOVERGENiHBG108317.
    KOiK06068.
    PhylomeDBiP09215.

    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: P09215-1) [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 SYELGSLQAE DDASQPFCAV KMKEALTTDR GKTLVQKKPT    50
    MYPEWKSTFD AHIYEGRVIQ IVLMRAAEDP MSEVTVGVSV LAERCKKNNG 100
    KAEFWLDLQP QAKVLMCVQY FLEDGDCKQS MRSEEEAMFP TMNRRGAIKQ 150
    AKIHYIKNHE FIATFFGQPT FCSVCKEFVW GLNKQGYKCR QCNAAIHKKC 200
    IDKIIGRCTG TATNSRDTIF QKERFNIDMP HRFKVYNYMS PTFCDHCGTL 250
    LWGLVKQGLK CEDCGMNVHH KCREKVANLC GINQKLLAEA LNQVTQKASR 300
    KPETPETVGI YQGFEKKTAV SGNDIPDNNG TYGKIWEGSN RCRLENFTFQ 350
    KVLGKGSFGK VLLAELKGKE RYFAIKYLKK DVVLIDDDVE CTMVEKRVLA 400
    LAWENPFLTH LICTFQTKDH LFFVMEFLNG GDLMFHIQDK GRFELYRATF 450
    YAAEIICGLQ FLHGKGIIYR DLKLDNVMLD KDGHIKIADF GMCKENIFGE 500
    NRASTFCGTP DYIAPEILQG LKYSFSVDWW SFGVLLYEML IGQSPFHGDD 550
    EDELFESIRV DTPHYPRWIT KESKDIMEKL FERDPAKRLG VTGNIRLHPF 600
    FKTINWNLLE KRKVEPPFKP KVKSPSDYSN FDPEFLNEKP QLSFSDKNLI 650
    DSMDQTAFKG FSFVNPKYEQ FLE 673
    Length:673
    Mass (Da):77,520
    Last modified:July 1, 1989 - v1
    Checksum:iD2C767E55863A23C
    GO
    Isoform 2 (identifier: P09215-2) [UniParc]FASTAAdd to Basket

    Also known as: PKC-delta-III

    The sequence of this isoform differs from the canonical sequence as follows:
         327-673: DNNGTYGKIW...VNPKYEQFLE → GESGSHIPLK...AALARYCLQN

    Show »
    Length:393
    Mass (Da):44,305
    Checksum:i88104F3B17991F6C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti147 – 1471A → S AA sequence (PubMed:1915352)Curated
    Sequence conflicti249 – 2491T → S in CAB75578. (PubMed:10721703)Curated
    Sequence conflicti249 – 2491T → S in AAH76505. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei327 – 673347DNNGT…EQFLE → GESGSHIPLKLPFPDRAREK NSSETWDKTTTGPMARSGRG ATGAALRTSPSRKYLAKAAL ARYCLQN in isoform 2. 1 PublicationVSP_004742Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M18330 mRNA. Translation: AAA41871.1.
    AJ230617
    , AJ230618, AJ230619, AJ230620, AJ230621, AJ230622, AJ230623, AJ230624, AJ230625, AJ230626, AJ230627, AJ230628, AJ230629, AJ230630, AJ230631, AJ230632, AJ230633 Genomic DNA. Translation: CAB75578.1.
    AF219629 mRNA. Translation: AAF32345.1.
    BC076505 mRNA. Translation: AAH76505.1.
    PIRiA28163. KIRTCD.
    RefSeqiNP_579841.1. NM_133307.1. [P09215-1]
    UniGeneiRn.98279.

    Genome annotation databases

    GeneIDi170538.
    KEGGirno:170538.
    UCSCiRGD:67383. rat. [P09215-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M18330 mRNA. Translation: AAA41871.1 .
    AJ230617
    , AJ230618 , AJ230619 , AJ230620 , AJ230621 , AJ230622 , AJ230623 , AJ230624 , AJ230625 , AJ230626 , AJ230627 , AJ230628 , AJ230629 , AJ230630 , AJ230631 , AJ230632 , AJ230633 Genomic DNA. Translation: CAB75578.1 .
    AF219629 mRNA. Translation: AAF32345.1 .
    BC076505 mRNA. Translation: AAH76505.1 .
    PIRi A28163. KIRTCD.
    RefSeqi NP_579841.1. NM_133307.1. [P09215-1 ]
    UniGenei Rn.98279.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BDY X-ray 2.20 A/B 1-123 [» ]
    ProteinModelPortali P09215.
    SMRi P09215. Positions 1-123, 149-218, 227-283, 343-666.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 250924. 8 interactions.
    IntActi P09215. 2 interactions.
    MINTi MINT-143019.

    Chemistry

    BindingDBi P09215.
    ChEMBLi CHEMBL3633.

    PTM databases

    PhosphoSitei P09215.

    Proteomic databases

    PaxDbi P09215.
    PRIDEi P09215.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 170538.
    KEGGi rno:170538.
    UCSCi RGD:67383. rat. [P09215-1 ]

    Organism-specific databases

    CTDi 5580.
    RGDi 67383. Prkcd.

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233022.
    HOVERGENi HBG108317.
    KOi K06068.
    PhylomeDBi P09215.

    Enzyme and pathway databases

    BRENDAi 2.7.11.13. 5301.
    Reactomei REACT_194374. Role of phospholipids in phagocytosis.
    REACT_196423. HuR stabilizes mRNA.
    REACT_196446. Interferon gamma signaling.
    REACT_220575. DAG and IP3 signaling.

    Miscellaneous databases

    EvolutionaryTracei P09215.
    NextBioi 621024.
    PMAP-CutDB P09215.

    Gene expression databases

    Genevestigatori P09215.

    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. "The structure, expression, and properties of additional members of the protein kinase C family."
      Ono Y., Fujii T., Ogita K., Kikkawa U., Igarashi K., Nishizuka Y.
      J. Biol. Chem. 263:6927-6932(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    2. "Genomic structure and chromosomal localization of the rat PKCdelta-gene."
      Kurkinen K.M.A., Keinanen R.A., Karhu R., Koistinaho J.
      Gene 242:115-123(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Wistar Kyoto.
    3. "cDNA cloning of an alternative splicing variant of protein kinase C delta (PKC deltaIII), a new truncated form of PKCdelta, in rats."
      Ueyama T., Ren Y., Ohmori S., Sakai K., Tamaki N., Saito N.
      Biochem. Biophys. Res. Commun. 269:557-563(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    4. "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] (ISOFORM 1).
      Tissue: Lung.
    5. "Identification of three additional members of rat protein kinase C family: delta-, epsilon- and zeta-subspecies."
      Ono Y., Fujii T., Ogita K., Kikkawa U., Igarashi K., Nishizuka Y.
      FEBS Lett. 226:125-128(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE OF 123-286.
    6. "Expression and characterization of protein kinase C-delta."
      Olivier A.R., Parker P.J.
      Eur. J. Biochem. 200:805-810(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 142-153.
    7. "The broad specificity of dominant inhibitory protein kinase C mutants infers a common step in phosphorylation."
      Garcia-Paramio P., Cabrerizo Y., Bornancin F., Parker P.J.
      Biochem. J. 333:631-636(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF THR-505, PHOSPHORYLATION AT THR-505.
    8. "Sphingosine-dependent protein kinase-1, directed to 14-3-3, is identified as the kinase domain of protein kinase C delta."
      Hamaguchi A., Suzuki E., Murayama K., Fujimura T., Hikita T., Iwabuchi K., Handa K., Withers D.A., Masters S.C., Fu H., Hakomori S.
      J. Biol. Chem. 278:41557-41565(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, CLEAVAGE BY CASPASE-3, ENZYME REGULATION.
    9. "Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS."
      Moser K., White F.M.
      J. Proteome Res. 5:98-104(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-662, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Induction of apoptosis is driven by nuclear retention of protein kinase C delta."
      DeVries-Seimon T.A., Ohm A.M., Humphries M.J., Reyland M.E.
      J. Biol. Chem. 282:22307-22314(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-64 AND TYR-155.
    11. "Protein kinase Cepsilon (PKCepsilon) and Src control PKCdelta activation loop phosphorylation in cardiomyocytes."
      Rybin V.O., Guo J., Gertsberg Z., Elouardighi H., Steinberg S.F.
      J. Biol. Chem. 282:23631-23638(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-505.
    12. "Tyrosine phosphorylation modifies protein kinase C delta-dependent phosphorylation of cardiac troponin I."
      Sumandea M.P., Rybin V.O., Hinken A.C., Wang C., Kobayashi T., Harleton E., Sievert G., Balke C.W., Feinmark S.J., Solaro R.J., Steinberg S.F.
      J. Biol. Chem. 283:22680-22689(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-311; TYR-332 AND THR-505.
    13. "Crystal structure of the C2 domain from protein kinase C-delta."
      Pappa H., Murray-Rust J., Dekker L.V., Parker P.J., McDonald N.Q.
      Structure 6:885-894(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-123.

    Entry informationi

    Entry nameiKPCD_RAT
    AccessioniPrimary (citable) accession number: P09215
    Secondary accession number(s): Q6DG48, Q9JK29, Q9JL03
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 165 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3