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P09215

- KPCD_RAT

UniProt

P09215 - KPCD_RAT

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Protein

Protein kinase C delta type

Gene
Prkcd, Pkcd
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.
Truncated isoform 2 is inactive.

Catalytic activityi

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

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 peptide By similarity
Sitei62 – 621Interaction with phosphotyrosine-containing peptide By similarity
Sitei67 – 671Interaction with phosphotyrosine-containing peptide By similarity
Sitei123 – 1231Interaction with phosphotyrosine-containing peptide By similarity
Sitei327 – 3282Cleavage; by caspase-3 Inferred
Binding sitei376 – 3761ATP By similarity
Active sitei471 – 4711Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri158 – 20851Phorbol-ester/DAG-type 1Add
BLAST
Zinc fingeri230 – 28051Phorbol-ester/DAG-type 2Add
BLAST
Nucleotide bindingi353 – 3619ATP By similarity

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
Complete GO annotation...

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. Nucleus. Cytoplasmperinuclear region. Endoplasmic reticulum By similarity. Mitochondrion By similarity. Membrane; 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
Complete GO annotation...

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 – 431Phosphothreonine By similarity
Modified residuei64 – 641Phosphotyrosine1 Publication
Modified residuei130 – 1301Phosphoserine By similarity
Modified residuei155 – 1551Phosphotyrosine1 Publication
Modified residuei218 – 2181Phosphothreonine By similarity
Modified residuei299 – 2991Phosphoserine; by autocatalysis By similarity
Modified residuei311 – 3111Phosphotyrosine; by SRC1 Publication
Modified residuei332 – 3321Phosphotyrosine; by SRC1 Publication
Modified residuei372 – 3721Phosphotyrosine By similarity
Modified residuei505 – 5051Phosphothreonine; by autocatalysis3 Publications
Modified residuei565 – 5651Phosphotyrosine By similarity
Modified residuei643 – 6431Phosphoserine Inferred
Modified residuei652 – 6521Phosphoserine By 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-505.4 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.

Miscellaneous databases

EvolutionaryTraceiP09215.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9090C2Add
BLAST
Domaini347 – 601255Protein kinaseAdd
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.

Sequence similaritiesi

Contains 1 C2 domain.

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri158 – 20851Phorbol-ester/DAG-type 1Add
BLAST
Zinc fingeri230 – 28051Phorbol-ester/DAG-type 2Add
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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei327 – 673347DNNGT…EQFLE → GESGSHIPLKLPFPDRAREK NSSETWDKTTTGPMARSGRG ATGAALRTSPSRKYLAKAAL ARYCLQN in isoform 2. VSP_004742Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti147 – 1471A → S AA sequence 1 Publication
Sequence conflicti249 – 2491T → S in CAB75578. 1 Publication
Sequence conflicti249 – 2491T → S in AAH76505. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 164 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

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