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Protein

Protein kinase C delta type

Gene

Prkcd

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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. Negatively regulates B cell proliferation and also has an important function in self-antigen induced B cell tolerance induction. Upon DNA damage, activates the promoter of the death-promoting transcription factor BCLAF1/Btf to trigger BCLAF1-mediated p53/TP53 gene transcription and apoptosis. In response to oxidative stress, interact with and activate CHUK/IKKA in the nucleus, causing the phosphorylation of p53/TP53. In the case of ER stress or DNA damage-induced apoptosis, can form a complex with the tyrosine-protein kinase ABL1 which trigger apoptosis independently of p53/TP53. In cytosol can trigger apoptosis by activating MAPK11 or MAPK14, inhibiting AKT1 and decreasing the level of X-linked inhibitor of apoptosis protein (XIAP), whereas in nucleus induces apoptosis via the activation of MAPK8 or MAPK9. Upon ionizing radiation treatment, is required for the activation of the apoptosis regulators BAX and BAK, which trigger the mitochondrial cell death pathway. Can phosphorylate MCL1 and target it for degradation which is sufficient to trigger for BAX activation and apoptosis. Is required for the control of cell cycle progression both at G1/S and G2/M phases. Mediates phorbol 12-myristate 13-acetate (PMA)-induced inhibition of cell cycle progression at G1/S phase by up-regulating the CDK inhibitor CDKN1A/p21 and inhibiting the cyclin CCNA2 promoter activity. In response to UV irradiation can phosphorylate CDK1, which is important for the G2/M DNA damage checkpoint activation. Can protect glioma cells from the apoptosis induced by TNFSF10/TRAIL, probably by inducing increased phosphorylation and subsequent activation of AKT1. Can also act as tumor suppressor upon mitogenic stimulation with PMA or TPA. In N-formyl-methionyl-leucyl-phenylalanine (fMLP)-treated cells, is required for NCF1 (p47-phox) phosphorylation and activation of NADPH oxidase activity, and regulates TNF-elicited superoxide anion production in neutrophils, by direct phosphorylation and activation of NCF1 or indirectly through MAPK1/3 (ERK1/2) signaling pathways. May also play a role in the regulation of NADPH oxidase activity in eosinophil after stimulation with IL5, leukotriene B4 or PMA. In collagen-induced platelet aggregation, acts a negative regulator of filopodia formation and actin polymerization by interacting with and negatively regulating VASP phosphorylation. Downstream of PAR1, PAR4 and CD36/GP4 receptors, regulates differentially platelet dense granule secretion; acts as a positive regulator in PAR-mediated granule secretion, whereas it negatively regulates CD36/GP4-mediated granule release. Phosphorylates MUC1 in the C-terminal and regulates the interaction between MUC1 and beta-catenin. The catalytic subunit phosphorylates 14-3-3 proteins (YWHAB, YWHAZ and YWHAH) in a sphingosine-dependent fashion. Phosphorylates ELAVL1 in response to angiotensin-2 treatment (By similarity).By similarity5 Publications

Catalytic activityi

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

Enzyme regulationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei376ATPPROSITE-ProRule annotation1
Active sitei471Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri158 – 208Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri230 – 280Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd BLAST51
Nucleotide bindingi353 – 361ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

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. 3474.
ReactomeiR-MMU-111465. Apoptotic cleavage of cellular proteins.
R-MMU-111933. Calmodulin induced events.
R-MMU-114508. Effects of PIP2 hydrolysis.
R-MMU-1489509. DAG and IP3 signaling.
R-MMU-2029485. Role of phospholipids in phagocytosis.
R-MMU-450520. HuR (ELAVL1) binds and stabilizes mRNA.
R-MMU-5218921. VEGFR2 mediated cell proliferation.
R-MMU-5607764. CLEC7A (Dectin-1) signaling.
R-MMU-6798695. Neutrophil degranulation.
R-MMU-877300. Interferon gamma signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein kinase C delta type (EC:2.7.11.13)
Alternative name(s):
Tyrosine-protein kinase PRKCD (EC:2.7.10.2)
nPKC-delta
Cleaved into the following 2 chains:
Alternative name(s):
Sphingosine-dependent protein kinase-1
Short name:
SDK1
Gene namesi
Name:Prkcd
Synonyms:Pkcd
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:97598. Prkcd.

Subcellular locationi

  • Cytoplasm By similarity
  • Cytoplasmperinuclear region By similarity
  • Nucleus By similarity
  • Cell membrane By similarity; Peripheral membrane protein By similarity

GO - Cellular componenti

  • cell-cell junction Source: MGI
  • cytoplasm Source: MGI
  • cytosol Source: MGI
  • endoplasmic reticulum Source: UniProtKB
  • extracellular exosome Source: MGI
  • membrane Source: MGI
  • nuclear matrix Source: MGI
  • nucleus Source: MGI
  • perinuclear region of cytoplasm Source: UniProtKB-SubCell
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Disruption phenotypei

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

Keywords - Diseasei

Tumor suppressor

Chemistry databases

ChEMBLiCHEMBL2560.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000556951 – 674Protein kinase C delta typeAdd BLAST674
ChainiPRO_00004216691 – 327Protein kinase C delta type regulatory subunitBy similarityAdd BLAST327
ChainiPRO_0000421670328 – 674Protein kinase C delta type catalytic subunitBy similarityAdd BLAST347

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei43PhosphothreonineCombined sources1
Modified residuei50PhosphothreonineBy similarity1
Modified residuei64PhosphotyrosineBy similarity1
Modified residuei130PhosphoserineBy similarity1
Modified residuei141PhosphothreonineBy similarity1
Modified residuei155PhosphotyrosineBy similarity1
Modified residuei218PhosphothreonineBy similarity1
Modified residuei299Phosphoserine; by autocatalysisBy similarity1
Modified residuei311Phosphotyrosine; by SRCCombined sources1
Modified residuei332Phosphotyrosine; by SRCBy similarity1
Modified residuei372PhosphotyrosineBy similarity1
Modified residuei449PhosphothreonineBy similarity1
Modified residuei504PhosphoserineBy similarity1
Modified residuei505Phosphothreonine; by autocatalysisCombined sources2 Publications1
Modified residuei565PhosphotyrosineBy similarity1
Modified residuei643PhosphoserineCombined sources1
Modified residuei652PhosphoserineBy similarity1
Modified residuei662PhosphoserineCombined sources1

Post-translational modificationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei327 – 328Cleavage; by caspase-3By similarity2

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP28867.
PaxDbiP28867.
PeptideAtlasiP28867.
PRIDEiP28867.

PTM databases

iPTMnetiP28867.
PhosphoSitePlusiP28867.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSMUSG00000021948.
CleanExiMM_PRKCD.
ExpressionAtlasiP28867. baseline and differential.
GenevisibleiP28867. MM.

Interactioni

Subunit structurei

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei48Interaction with phosphotyrosine-containing peptideBy similarity1
Sitei62Interaction with phosphotyrosine-containing peptideBy similarity1
Sitei67Interaction with phosphotyrosine-containing peptideBy similarity1
Sitei123Interaction with phosphotyrosine-containing peptideBy similarity1

Binary interactionsi

WithEntry#Exp.IntActNotes
Gja1P232424EBI-1551324,EBI-298630

GO - Molecular functioni

  • enzyme binding Source: MGI
  • insulin receptor substrate binding Source: BHF-UCL
  • kinase binding Source: MGI
  • protein kinase binding Source: MGI

Protein-protein interaction databases

BioGridi202197. 7 interactors.
DIPiDIP-1169N.
IntActiP28867. 4 interactors.
MINTiMINT-97906.
STRINGi10090.ENSMUSP00000107827.

Chemistry databases

BindingDBiP28867.

Structurei

Secondary structure

1674
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi233 – 236Combined sources4
Turni245 – 247Combined sources3
Beta strandi253 – 256Combined sources4
Beta strandi258 – 261Combined sources4
Turni262 – 264Combined sources3
Helixi270 – 273Combined sources4
Beta strandi278 – 280Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PTQX-ray1.95A231-280[»]
1PTRX-ray2.20A231-280[»]
3UEJX-ray1.30A/B231-280[»]
3UEYX-ray1.30A/B231-280[»]
3UFFX-ray1.30A/B231-280[»]
3UGDX-ray1.45A/B231-280[»]
3UGIX-ray1.36A/B231-280[»]
3UGLX-ray1.36A/B231-280[»]
ProteinModelPortaliP28867.
SMRiP28867.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28867.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 90C2Add BLAST90
Domaini347 – 601Protein kinasePROSITE-ProRule annotationAdd BLAST255
Domaini602 – 673AGC-kinase C-terminalAdd BLAST72

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)DescriptionActionsGraphical viewLength
Zinc fingeri158 – 208Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri230 – 280Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd BLAST51

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG0694. Eukaryota.
ENOG410XNPH. LUCA.
GeneTreeiENSGT00820000126964.
HOGENOMiHOG000233022.
HOVERGENiHBG108317.
InParanoidiP28867.
KOiK06068.
OMAiGEDEAKF.
OrthoDBiEOG091G0QRS.
PhylomeDBiP28867.
TreeFamiTF102004.

Family and domain databases

CDDicd00029. C1. 2 hits.
Gene3Di2.60.40.150. 1 hit.
InterProiIPR000961. AGC-kinase_C.
IPR000008. C2_dom.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR002219. PE/DAG-bd.
IPR027436. PKC_delta.
IPR017892. Pkinase_C.
IPR014376. Prot_kin_PKC_delta.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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.
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. AlignAdd to basket

Isoform 1 (identifier: P28867-1) [UniParc]FASTAAdd to basket
Also known as: PKC-delta-I

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

« Hide

        10         20         30         40         50
MAPFLRISFN SYELGSLQVE DEASQPFCAV KMKEALSTER GKTLVQKKPT
60 70 80 90 100
MYPEWKTTFD AHIYEGRVIQ IVLMRAAEDP VSEVTVGVSV LAERCKKNNG
110 120 130 140 150
KAEFWLDLQP QAKVLMCVQY FLEDGDCKQS MRSEEEAKFP TMNRRGAIKQ
160 170 180 190 200
AKIHYIKNHE FIATFFGQPT FCSVCKEFVW GLNKQGYKCR QCNAAIHKKC
210 220 230 240 250
IDKIIGRCTG TATNSRDTIF QKERFNIDMP HRFKVYNYMS PTFCDHCGSL
260 270 280 290 300
LWGLVKQGLK CEDCGMNVHH KCREKVANLC GINQKLLAEA LNQVTQRSSR
310 320 330 340 350
KLDTTESVGI YQGFEKKPEV SGSDILDNNG TYGKIWEGST RCTLENFTFQ
360 370 380 390 400
KVLGKGSFGK VLLAELKGKD KYFAIKCLKK DVVLIDDDVE CTMVEKRVLA
410 420 430 440 450
LAWESPFLTH LICTFQTKDH LFFVMEFLNG GDLMFHIQDK GRFELYRATF
460 470 480 490 500
YAAEIICGLQ FLHSKGIIYR DLKLDNVMLD RDGHIKIADF GMCKENIFGE
510 520 530 540 550
GRASTFCGTP DYIAPEILQG LKYSFSVDWW SFGVLLYEML IGQSPFHGDD
560 570 580 590 600
EDELFESIRV DTPHYPRWIT KESKDIMEKL FERDPDKRLG VTGNIRIHPF
610 620 630 640 650
FKTINWSLLE KRKVEPPFKP KVKSPSDYSN FDPEFLNEKP QLSFSDKNLI
660 670
DSMDQEAFHG FSFVNPKFEQ FLDI
Length:674
Mass (Da):77,547
Last modified:March 27, 2002 - v3
Checksum:i6E9F753348F03D59
GO
Isoform 2 (identifier: P28867-2) [UniParc]FASTAAdd to basket
Also known as: PKC-delta-II

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

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti214N → I in BAA36408 (PubMed:11558579).Curated1
Sequence conflicti226N → S in BAA36408 (PubMed:11558579).Curated1
Sequence conflicti319E → D in AAA73056 (PubMed:1868068).Curated1
Sequence conflicti330G → W in AAA73056 (PubMed:1868068).Curated1
Sequence conflicti337E → V in AAA73056 (PubMed:1868068).Curated1
Sequence conflicti501G → D in AAA73056 (PubMed:1868068).Curated1
Sequence conflicti503A → P in AAA73056 (PubMed:1868068).Curated1
Sequence conflicti513I → S in AAA73056 (PubMed:1868068).Curated1
Sequence conflicti518 – 520LQG → PARA in BAA36408 (PubMed:11558579).Curated3
Sequence conflicti538E → R in BAA36408 (PubMed:11558579).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_004741326L → LGEAGSHISLKLSFPSRAKE KDSSETC in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M69042 mRNA. Translation: AAA73056.1.
X60304 mRNA. Translation: CAA42845.1.
AF274044 Genomic DNA. Translation: AAF79208.1.
AF251036 mRNA. Translation: AAF64316.1.
AB011812 mRNA. Translation: BAA36408.1.
CCDSiCCDS26895.1. [P28867-1]
CCDS79285.1. [P28867-2]
PIRiA40281. KIMSCD.
RefSeqiNP_035233.1. NM_011103.3. [P28867-1]
XP_006518758.1. XM_006518695.2. [P28867-2]
XP_017171407.1. XM_017315918.1. [P28867-2]
UniGeneiMm.2314.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M69042 mRNA. Translation: AAA73056.1.
X60304 mRNA. Translation: CAA42845.1.
AF274044 Genomic DNA. Translation: AAF79208.1.
AF251036 mRNA. Translation: AAF64316.1.
AB011812 mRNA. Translation: BAA36408.1.
CCDSiCCDS26895.1. [P28867-1]
CCDS79285.1. [P28867-2]
PIRiA40281. KIMSCD.
RefSeqiNP_035233.1. NM_011103.3. [P28867-1]
XP_006518758.1. XM_006518695.2. [P28867-2]
XP_017171407.1. XM_017315918.1. [P28867-2]
UniGeneiMm.2314.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PTQX-ray1.95A231-280[»]
1PTRX-ray2.20A231-280[»]
3UEJX-ray1.30A/B231-280[»]
3UEYX-ray1.30A/B231-280[»]
3UFFX-ray1.30A/B231-280[»]
3UGDX-ray1.45A/B231-280[»]
3UGIX-ray1.36A/B231-280[»]
3UGLX-ray1.36A/B231-280[»]
ProteinModelPortaliP28867.
SMRiP28867.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202197. 7 interactors.
DIPiDIP-1169N.
IntActiP28867. 4 interactors.
MINTiMINT-97906.
STRINGi10090.ENSMUSP00000107827.

Chemistry databases

BindingDBiP28867.
ChEMBLiCHEMBL2560.

PTM databases

iPTMnetiP28867.
PhosphoSitePlusiP28867.

Proteomic databases

EPDiP28867.
PaxDbiP28867.
PeptideAtlasiP28867.
PRIDEiP28867.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5580.
MGIiMGI:97598. Prkcd.

Phylogenomic databases

eggNOGiKOG0694. Eukaryota.
ENOG410XNPH. LUCA.
GeneTreeiENSGT00820000126964.
HOGENOMiHOG000233022.
HOVERGENiHBG108317.
InParanoidiP28867.
KOiK06068.
OMAiGEDEAKF.
OrthoDBiEOG091G0QRS.
PhylomeDBiP28867.
TreeFamiTF102004.

Enzyme and pathway databases

BRENDAi2.7.11.13. 3474.
ReactomeiR-MMU-111465. Apoptotic cleavage of cellular proteins.
R-MMU-111933. Calmodulin induced events.
R-MMU-114508. Effects of PIP2 hydrolysis.
R-MMU-1489509. DAG and IP3 signaling.
R-MMU-2029485. Role of phospholipids in phagocytosis.
R-MMU-450520. HuR (ELAVL1) binds and stabilizes mRNA.
R-MMU-5218921. VEGFR2 mediated cell proliferation.
R-MMU-5607764. CLEC7A (Dectin-1) signaling.
R-MMU-6798695. Neutrophil degranulation.
R-MMU-877300. Interferon gamma signaling.

Miscellaneous databases

ChiTaRSiPrkcd. mouse.
EvolutionaryTraceiP28867.
PROiP28867.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000021948.
CleanExiMM_PRKCD.
ExpressionAtlasiP28867. baseline and differential.
GenevisibleiP28867. MM.

Family and domain databases

CDDicd00029. C1. 2 hits.
Gene3Di2.60.40.150. 1 hit.
InterProiIPR000961. AGC-kinase_C.
IPR000008. C2_dom.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR002219. PE/DAG-bd.
IPR027436. PKC_delta.
IPR017892. Pkinase_C.
IPR014376. Prot_kin_PKC_delta.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiKPCD_MOUSE
AccessioniPrimary (citable) accession number: P28867
Secondary accession number(s): Q91V85, Q9Z333
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: March 27, 2002
Last modified: November 30, 2016
This is version 180 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.