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P28867 (KPCD_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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):
Tyrosine-protein kinase PRKCD
EC=2.7.10.2
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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length674 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. The catalytic subunit phosphorylates 14-3-3 proteins (YWHAB, YWHAZ and YWHAH) in a sphingosine-dependent fashion. Ref.5 Ref.6 Ref.9 Ref.13

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 By similarity.

Subunit structure

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

Subcellular location

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

Tissue specificity

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.

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. Ref.7 Ref.9

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

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
Reference proteome
Gene Ontology (GO)
   Biological_processB cell proliferation

Inferred from mutant phenotype PubMed 11976687. Source: MGI

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cellular senescence

Inferred from electronic annotation. Source: Ensembl

defense response to bacterium

Inferred from mutant phenotype PubMed 22885697. Source: UniProtKB

immunoglobulin mediated immune response

Inferred from mutant phenotype PubMed 11976687. Source: MGI

interleukin-10 production

Inferred from mutant phenotype PubMed 15817708. Source: MGI

interleukin-12 production

Inferred from mutant phenotype PubMed 15817708. Source: MGI

intracellular signal transduction

Inferred from electronic annotation. Source: InterPro

negative regulation of MAP kinase activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of actin filament polymerization

Inferred from mutant phenotype PubMed 16940418. Source: UniProtKB

negative regulation of filopodium assembly

Inferred from mutant phenotype PubMed 16940418. Source: UniProtKB

negative regulation of glial cell apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of insulin receptor signaling pathway

Inferred from mutant phenotype PubMed 18285345. Source: BHF-UCL

negative regulation of peptidyl-tyrosine phosphorylation

Inferred from mutant phenotype PubMed 14583092. Source: BHF-UCL

negative regulation of platelet aggregation

Inferred from mutant phenotype PubMed 16940418. Source: UniProtKB

neutrophil activation

Inferred from electronic annotation. Source: Ensembl

peptidyl-threonine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic signaling pathway

Inferred from direct assay PubMed 15731106. Source: MGI

positive regulation of ceramide biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of glucosylceramide catabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of phospholipid scramblase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein dephosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of response to DNA damage stimulus

Inferred from electronic annotation. Source: Ensembl

positive regulation of sphingomyelin catabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of superoxide anion generation

Inferred from sequence or structural similarity. Source: UniProtKB

termination of signal transduction

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell-cell junction

Inferred from direct assay PubMed 10882525. Source: MGI

cytoplasm

Inferred from direct assay PubMed 10882525. Source: MGI

endoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear matrix

Inferred from direct assay PubMed 10882525. Source: MGI

nucleus

Inferred from direct assay PubMed 10882525. Source: MGI

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

enzyme activator activity

Inferred from electronic annotation. Source: Ensembl

insulin receptor substrate binding

Inferred from physical interaction PubMed 18285345. Source: BHF-UCL

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

non-membrane spanning protein tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein kinase C activity

Inferred from direct assay PubMed 22885697. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P28867-1)

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: P28867-2)

Also known as: PKC-delta-II;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 674674Protein kinase C delta type
PRO_0000055695
Chain1 – 327327Protein kinase C delta type regulatory subunit By similarity
PRO_0000421669
Chain328 – 674347Protein kinase C delta type catalytic subunit By similarity
PRO_0000421670

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 By similarity

Amino acid modifications

Modified residue431Phosphothreonine Ref.11
Modified residue641Phosphotyrosine By similarity
Modified residue1301Phosphoserine By similarity
Modified residue1551Phosphotyrosine By similarity
Modified residue2181Phosphothreonine By similarity
Modified residue2991Phosphoserine; by autocatalysis By similarity
Modified residue3111Phosphotyrosine; alternate Ref.8 Ref.10 Ref.11 Ref.12
Modified residue3111Phosphotyrosine; by SRC; alternate Probable
Modified residue3321Phosphotyrosine; by SRC By similarity
Modified residue3721Phosphotyrosine By similarity
Modified residue5051Phosphothreonine; by autocatalysis Ref.7 Ref.9
Modified residue5651Phosphotyrosine By similarity
Modified residue6431Phosphoserine Probable
Modified residue6521Phosphoserine By similarity
Modified residue6621Phosphoserine Ref.11

Natural variations

Alternative sequence3261L → LGEAGSHISLKLSFPSRAKE KDSSETC in isoform 2.
VSP_004741

Experimental info

Sequence conflict2141N → I in BAA36408. Ref.4
Sequence conflict2261N → S in BAA36408. Ref.4
Sequence conflict3191E → D in AAA73056. Ref.1
Sequence conflict3301G → W in AAA73056. Ref.1
Sequence conflict3371E → V in AAA73056. Ref.1
Sequence conflict5011G → D in AAA73056. Ref.1
Sequence conflict5031A → P in AAA73056. Ref.1
Sequence conflict5131I → S in AAA73056. Ref.1
Sequence conflict518 – 5203LQG → PARA in BAA36408. Ref.4
Sequence conflict5381E → R in BAA36408. Ref.4

Secondary structure

.............. 674
Helix Strand Turn

Details...

Sequences

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

Last modified March 27, 2002. Version 3.
Checksum: 6E9F753348F03D59

FASTA67477,547
        10         20         30         40         50         60 
MAPFLRISFN SYELGSLQVE DEASQPFCAV KMKEALSTER GKTLVQKKPT MYPEWKTTFD 

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

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

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

       250        260        270        280        290        300 
PTFCDHCGSL LWGLVKQGLK CEDCGMNVHH KCREKVANLC GINQKLLAEA LNQVTQRSSR 

       310        320        330        340        350        360 
KLDTTESVGI YQGFEKKPEV SGSDILDNNG TYGKIWEGST RCTLENFTFQ KVLGKGSFGK 

       370        380        390        400        410        420 
VLLAELKGKD KYFAIKCLKK DVVLIDDDVE CTMVEKRVLA LAWESPFLTH LICTFQTKDH 

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

       490        500        510        520        530        540 
RDGHIKIADF GMCKENIFGE GRASTFCGTP DYIAPEILQG LKYSFSVDWW SFGVLLYEML 

       550        560        570        580        590        600 
IGQSPFHGDD EDELFESIRV DTPHYPRWIT KESKDIMEKL FERDPDKRLG VTGNIRIHPF 

       610        620        630        640        650        660 
FKTINWSLLE KRKVEPPFKP KVKSPSDYSN FDPEFLNEKP QLSFSDKNLI DSMDQEAFHG 

       670 
FSFVNPKFEQ FLDI 

« Hide

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

Checksum: CFB6D8A58220C962
Show »

FASTA70080,294

References

« Hide 'large scale' references
[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]"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.
[9]"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.
[10]"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.
[11]"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].
[12]"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.
[13]"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.
[14]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRKIMSCD. A40281.
RefSeqNP_035233.1. NM_011103.3.
XP_006518758.1. XM_006518695.1.
XP_006518759.1. XM_006518696.1.
UniGeneMm.2314.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP28867.
SMRP28867. Positions 1-123, 149-670.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202197. 7 interactions.
DIPDIP-1169N.
IntActP28867. 3 interactions.
MINTMINT-97906.

Chemistry

BindingDBP28867.
ChEMBLCHEMBL2560.

PTM databases

PhosphoSiteP28867.

Proteomic databases

PaxDbP28867.
PRIDEP28867.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022521; ENSMUSP00000022521; ENSMUSG00000021948. [P28867-2]
ENSMUST00000112208; ENSMUSP00000107827; ENSMUSG00000021948. [P28867-1]
ENSMUST00000112210; ENSMUSP00000107829; ENSMUSG00000021948. [P28867-1]
ENSMUST00000112211; ENSMUSP00000107830; ENSMUSG00000021948. [P28867-2]
GeneID18753.
KEGGmmu:18753.
UCSCuc007sve.2. mouse. [P28867-1]
uc007svg.2. mouse. [P28867-2]

Organism-specific databases

CTD5580.
MGIMGI:97598. Prkcd.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00750000117339.
HOGENOMHOG000233022.
HOVERGENHBG108317.
KOK06068.
OMAGEDEAKF.
OrthoDBEOG77M8QM.
PhylomeDBP28867.
TreeFamTF102004.

Enzyme and pathway databases

BRENDA2.7.11.13. 3474.

Gene expression databases

ArrayExpressP28867.
BgeeP28867.
CleanExMM_PRKCD.
GenevestigatorP28867.

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

ChiTaRSPRKCD. mouse.
EvolutionaryTraceP28867.
NextBio294929.
PROP28867.
SOURCESearch...

Entry information

Entry nameKPCD_MOUSE
AccessionPrimary (citable) accession number: P28867
Secondary accession number(s): Q91V85, Q9Z333
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: March 27, 2002
Last modified: April 16, 2014
This is version 151 of the entry and version 3 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

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot