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P09215 (KPCD_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 161. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein kinase C delta type

EC=2.7.11.13
Alternative name(s):
nPKC-delta

Cleaved into the following 2 chains:

  1. Protein kinase C delta type regulatory subunit
  2. Protein kinase C delta type catalytic subunit
    Alternative name(s):
    Sphingosine-dependent protein kinase-1
    Short name=SDK1
Gene names
Name:Prkcd
Synonyms:Pkcd
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length673 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

ATP + a protein = ADP + a phosphoprotein.

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

Enzyme regulation

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. Ref.8

Subunit structure

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

Subcellular location

Cytoplasm. Nucleus. Cytoplasmperinuclear region. Endoplasmic reticulum By similarity. Mitochondrion By similarity. Membrane; Peripheral membrane protein Ref.10.

Domain

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.

Post-translational modification

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-terminus cleavage product of PKN2 By similarity. Phosphorylated at Tyr-311 and Tyr-332 by SRC; phosphorylation leads to enhanced autophosphorylation at Thr-505. Ref.7 Ref.10 Ref.11 Ref.12

Proteolytically cleaved into a catalytic subunit and a regulatory subunit by caspase-3 during apoptosis which results in kinase activation. Ref.8

Sequence similarities

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily.

Contains 1 AGC-kinase C-terminal domain.

Contains 1 C2 domain.

Contains 2 phorbol-ester/DAG-type zinc fingers.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processApoptosis
Cell cycle
   Cellular componentCytoplasm
Endoplasmic reticulum
Membrane
Mitochondrion
Nucleus
   Coding sequence diversityAlternative splicing
   DiseaseTumor suppressor
   DomainRepeat
Zinc-finger
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processaging

Inferred from expression pattern PubMed 17008461. Source: RGD

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

aspartate transport

Inferred from mutant phenotype PubMed 17364745. Source: RGD

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to glucose starvation

Inferred from expression pattern PubMed 17728702. Source: RGD

cellular response to insulin stimulus

Inferred from expression pattern PubMed 17046201. Source: RGD

collagen metabolic process

Inferred from mutant phenotype PubMed 17728702. Source: RGD

defense response to bacterium

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular signal transduction

Inferred from direct assay PubMed 11562372. Source: RGD

negative regulation of actin filament polymerization

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of filopodium assembly

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of glial cell apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of platelet aggregation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of MAP kinase activity

Inferred from mutant phenotype PubMed 16935468. Source: RGD

positive regulation of MAPK cascade

Inferred from mutant phenotype PubMed 12790799. Source: RGD

positive regulation of apoptotic process

Inferred from mutant phenotype PubMed 12663471. Source: RGD

positive regulation of glucose import

Inferred from mutant phenotype PubMed 17098211. Source: RGD

positive regulation of superoxide anion generation

Inferred from sequence or structural similarity. Source: UniProtKB

protein autophosphorylation

Inferred from direct assay PubMed 10085132. Source: RGD

protein phosphorylation

Inferred from direct assay Ref.6. Source: RGD

response to amino acid

Inferred from expression pattern PubMed 17210758. Source: RGD

response to drug

Inferred from expression pattern PubMed 17123493. Source: RGD

response to ethanol

Inferred from expression pattern PubMed 17728104. Source: RGD

response to glucose

Inferred from expression pattern PubMed 12960081. Source: RGD

response to heat

Inferred from expression pattern PubMed 16990486. Source: RGD

response to hydrogen peroxide

Inferred from expression pattern PubMed 12226102PubMed 17397968. Source: RGD

response to hypoxia

Inferred from expression pattern PubMed 16936002. Source: RGD

response to mechanical stimulus

Inferred from expression pattern PubMed 17487266. Source: RGD

response to organic cyclic compound

Inferred from expression pattern PubMed 11478406. Source: RGD

response to organonitrogen compound

Inferred from expression pattern PubMed 17563398. Source: RGD

response to oxidative stress

Inferred from mutant phenotype PubMed 11576956. Source: RGD

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 12663471. Source: RGD

cytosol

Inferred from direct assay PubMed 18945317PubMed 9705215PubMed 9950866. Source: RGD

endoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

membrane

Inferred from direct assay PubMed 9705215. Source: RGD

mitochondrion

Inferred from direct assay PubMed 17008461. Source: RGD

nucleus

Inferred from direct assay PubMed 12663471. Source: RGD

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay PubMed 18945317. Source: RGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

TIR domain binding

Inferred from physical interaction PubMed 17161867. Source: BHF-UCL

calcium-independent protein kinase C activity

Inferred from direct assay Ref.6. Source: RGD

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein kinase C activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein kinase binding

Inferred from physical interaction PubMed 15337529. Source: RGD

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P09215-1)

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.
Isoform 2 (identifier: P09215-2)

Also known as: PKC-delta-III;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 673673Protein kinase C delta type
PRO_0000055696
Chain1 – 327327Protein kinase C delta type regulatory subunit
PRO_0000421671
Chain328 – 673346Protein kinase C delta type catalytic subunit
PRO_0000421672

Regions

Domain1 – 9090C2
Domain347 – 601255Protein kinase
Domain602 – 67372AGC-kinase C-terminal
Zinc finger158 – 20851Phorbol-ester/DAG-type 1
Zinc finger230 – 28051Phorbol-ester/DAG-type 2
Nucleotide binding353 – 3619ATP By similarity

Sites

Active site4711Proton acceptor By similarity
Binding site3761ATP By similarity
Site481Interaction with phosphotyrosine-containing peptide By similarity
Site621Interaction with phosphotyrosine-containing peptide By similarity
Site671Interaction with phosphotyrosine-containing peptide By similarity
Site1231Interaction with phosphotyrosine-containing peptide By similarity
Site327 – 3282Cleavage; by caspase-3 Probable

Amino acid modifications

Modified residue431Phosphothreonine By similarity
Modified residue641Phosphotyrosine Ref.10
Modified residue1301Phosphoserine By similarity
Modified residue1551Phosphotyrosine Ref.10
Modified residue2181Phosphothreonine By similarity
Modified residue2991Phosphoserine; by autocatalysis By similarity
Modified residue3111Phosphotyrosine; by SRC Ref.12
Modified residue3321Phosphotyrosine; by SRC Ref.12
Modified residue3721Phosphotyrosine By similarity
Modified residue5051Phosphothreonine; by autocatalysis Ref.7 Ref.11 Ref.12
Modified residue5651Phosphotyrosine By similarity
Modified residue6431Phosphoserine Probable
Modified residue6521Phosphoserine By similarity
Modified residue6621Phosphoserine Ref.9

Natural variations

Alternative sequence327 – 673347DNNGT…EQFLE → GESGSHIPLKLPFPDRAREK NSSETWDKTTTGPMARSGRG ATGAALRTSPSRKYLAKAAL ARYCLQN in isoform 2.
VSP_004742

Experimental info

Mutagenesis5051T → A: Decrease in the phosphorylation level. Ref.7
Sequence conflict1471A → S AA sequence Ref.6
Sequence conflict2491T → S in CAB75578. Ref.2
Sequence conflict2491T → S in AAH76505. Ref.4

Secondary structure

...................... 673
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (PKC-delta-I) [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: D2C767E55863A23C

FASTA67377,520
        10         20         30         40         50         60 
MAPFLRISFN SYELGSLQAE DDASQPFCAV KMKEALTTDR GKTLVQKKPT MYPEWKSTFD 

        70         80         90        100        110        120 
AHIYEGRVIQ IVLMRAAEDP MSEVTVGVSV LAERCKKNNG KAEFWLDLQP QAKVLMCVQY 

       130        140        150        160        170        180 
FLEDGDCKQS MRSEEEAMFP TMNRRGAIKQ AKIHYIKNHE FIATFFGQPT FCSVCKEFVW 

       190        200        210        220        230        240 
GLNKQGYKCR QCNAAIHKKC IDKIIGRCTG TATNSRDTIF QKERFNIDMP HRFKVYNYMS 

       250        260        270        280        290        300 
PTFCDHCGTL LWGLVKQGLK CEDCGMNVHH KCREKVANLC GINQKLLAEA LNQVTQKASR 

       310        320        330        340        350        360 
KPETPETVGI YQGFEKKTAV SGNDIPDNNG TYGKIWEGSN RCRLENFTFQ KVLGKGSFGK 

       370        380        390        400        410        420 
VLLAELKGKE RYFAIKYLKK DVVLIDDDVE CTMVEKRVLA LAWENPFLTH LICTFQTKDH 

       430        440        450        460        470        480 
LFFVMEFLNG GDLMFHIQDK GRFELYRATF YAAEIICGLQ FLHGKGIIYR DLKLDNVMLD 

       490        500        510        520        530        540 
KDGHIKIADF GMCKENIFGE NRASTFCGTP DYIAPEILQG LKYSFSVDWW SFGVLLYEML 

       550        560        570        580        590        600 
IGQSPFHGDD EDELFESIRV DTPHYPRWIT KESKDIMEKL FERDPAKRLG VTGNIRLHPF 

       610        620        630        640        650        660 
FKTINWNLLE KRKVEPPFKP KVKSPSDYSN FDPEFLNEKP QLSFSDKNLI DSMDQTAFKG 

       670 
FSFVNPKYEQ FLE 

« Hide

Isoform 2 (PKC-delta-III) [UniParc].

Checksum: 88104F3B17991F6C
Show »

FASTA39344,305

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M18330 mRNA. Translation: AAA41871.1.
AJ230617 expand/collapse EMBL AC list , 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.
PIRKIRTCD. A28163.
RefSeqNP_579841.1. NM_133307.1.
UniGeneRn.98279.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BDYX-ray2.20A/B1-123[»]
ProteinModelPortalP09215.
SMRP09215. Positions 1-123, 149-218, 227-283, 343-666.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid250924. 8 interactions.
IntActP09215. 2 interactions.
MINTMINT-143019.

Chemistry

BindingDBP09215.
ChEMBLCHEMBL3633.

PTM databases

PhosphoSiteP09215.

Proteomic databases

PaxDbP09215.
PRIDEP09215.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID170538.
KEGGrno:170538.
UCSCRGD:67383. rat. [P09215-1]

Organism-specific databases

CTD5580.
RGD67383. Prkcd.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233022.
HOVERGENHBG108317.
KOK06068.
PhylomeDBP09215.

Enzyme and pathway databases

BRENDA2.7.11.13. 5301.

Gene expression databases

GenevestigatorP09215.

Family and domain databases

Gene3D2.60.40.150. 1 hit.
InterProIPR000961. 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]
PfamPF00130. C1_1. 2 hits.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFPIRSF000551. PKC_delta. 1 hit.
PIRSF501104. Protein_kin_C_delta. 1 hit.
PRINTSPR00008. DAGPEDOMAIN.
SMARTSM00109. C1. 2 hits.
SM00239. C2. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF49562. SSF49562. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS51285. 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]
ProtoNetSearch...

Other

EvolutionaryTraceP09215.
NextBio621024.
PMAP-CutDBP09215.

Entry information

Entry nameKPCD_RAT
AccessionPrimary (citable) accession number: P09215
Secondary accession number(s): Q6DG48, Q9JK29, Q9JL03
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: April 16, 2014
This is version 161 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references