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P28867

- KPCD_MOUSE

UniProt

P28867 - KPCD_MOUSE

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Protein

Protein kinase C delta type

Gene

Prkcd

Organism
Mus musculus (Mouse)
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. 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.5 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)LengthDescriptionGraphical viewFeature identifierActions
Sitei48 – 481Interaction with phosphotyrosine-containing peptideBy similarity
Sitei62 – 621Interaction with phosphotyrosine-containing peptideBy similarity
Sitei67 – 671Interaction with phosphotyrosine-containing peptideBy similarity
Sitei123 – 1231Interaction with phosphotyrosine-containing peptideBy similarity
Sitei327 – 3282Cleavage; by caspase-3By similarity
Binding sitei376 – 3761ATPPROSITE-ProRule annotation
Active sitei471 – 4711Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri158 – 20851Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri230 – 28051Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi353 – 3619ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. enzyme activator activity Source: Ensembl
  3. insulin receptor substrate binding Source: BHF-UCL
  4. metal ion binding Source: UniProtKB-KW
  5. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
  6. protein kinase C activity Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. B cell proliferation Source: MGI
  3. cell cycle Source: UniProtKB-KW
  4. cellular senescence Source: Ensembl
  5. defense response to bacterium Source: UniProtKB
  6. immunoglobulin mediated immune response Source: MGI
  7. interleukin-10 production Source: MGI
  8. interleukin-12 production Source: MGI
  9. intracellular signal transduction Source: InterPro
  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 insulin receptor signaling pathway Source: BHF-UCL
  14. negative regulation of MAP kinase activity Source: Ensembl
  15. negative regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
  16. negative regulation of platelet aggregation Source: UniProtKB
  17. neutrophil activation Source: Ensembl
  18. peptidyl-threonine phosphorylation Source: Ensembl
  19. positive regulation of apoptotic signaling pathway Source: MGI
  20. positive regulation of ceramide biosynthetic process Source: Ensembl
  21. positive regulation of glucosylceramide catabolic process Source: Ensembl
  22. positive regulation of phospholipid scramblase activity Source: Ensembl
  23. positive regulation of protein dephosphorylation Source: Ensembl
  24. positive regulation of response to DNA damage stimulus Source: Ensembl
  25. positive regulation of sphingomyelin catabolic process Source: Ensembl
  26. positive regulation of superoxide anion generation Source: UniProtKB
  27. termination of signal transduction Source: Ensembl
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.
ReactomeiREACT_188269. DAG and IP3 signaling.
REACT_198660. Interferon gamma signaling.
REACT_198691. HuR stabilizes mRNA.
REACT_210240. Role of phospholipids in phagocytosis.
REACT_215587. Calmodulin induced events.
REACT_219232. Effects of PIP2 hydrolysis.
REACT_224460. Apoptotic cleavage of cellular proteins.
REACT_245086. VEGFR2 mediated cell proliferation.
REACT_258013. G alpha (z) signalling events.

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
ProteomesiUP000000589: Chromosome 14

Organism-specific databases

MGIiMGI:97598. Prkcd.

Subcellular locationi

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

GO - Cellular componenti

  1. cell-cell junction Source: MGI
  2. cytoplasm Source: MGI
  3. cytosol Source: Ensembl
  4. endoplasmic reticulum Source: UniProtKB
  5. extracellular vesicular exosome Source: Ensembl
  6. mitochondrion Source: UniProtKB-KW
  7. nuclear matrix Source: MGI
  8. nucleus Source: MGI
  9. plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane, Mitochondrion, 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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 674674Protein kinase C delta typePRO_0000055695Add
BLAST
Chaini1 – 327327Protein kinase C delta type regulatory subunitBy similarityPRO_0000421669Add
BLAST
Chaini328 – 674347Protein kinase C delta type catalytic subunitBy similarityPRO_0000421670Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei43 – 431Phosphothreonine1 Publication
Modified residuei64 – 641PhosphotyrosineBy similarity
Modified residuei130 – 1301PhosphoserineBy similarity
Modified residuei155 – 1551PhosphotyrosineBy similarity
Modified residuei218 – 2181PhosphothreonineBy similarity
Modified residuei299 – 2991Phosphoserine; by autocatalysisBy similarity
Modified residuei311 – 3111Phosphotyrosine; alternate4 Publications
Modified residuei311 – 3111Phosphotyrosine; by SRC; alternate4 Publications
Modified residuei332 – 3321Phosphotyrosine; by SRCBy similarity
Modified residuei372 – 3721PhosphotyrosineBy similarity
Modified residuei505 – 5051Phosphothreonine; by autocatalysis2 Publications
Modified residuei565 – 5651PhosphotyrosineBy similarity
Modified residuei643 – 6431PhosphoserineCurated
Modified residuei652 – 6521PhosphoserineBy similarity
Modified residuei662 – 6621Phosphoserine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP28867.
PaxDbiP28867.
PRIDEiP28867.

PTM databases

PhosphoSiteiP28867.

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

BgeeiP28867.
CleanExiMM_PRKCD.
ExpressionAtlasiP28867. baseline and differential.
GenevestigatoriP28867.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi202197. 7 interactions.
DIPiDIP-1169N.
IntActiP28867. 3 interactions.
MINTiMINT-97906.

Structurei

Secondary structure

1
674
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi233 – 2364Combined sources
Turni245 – 2473Combined sources
Beta strandi253 – 2564Combined sources
Beta strandi258 – 2614Combined sources
Turni262 – 2643Combined sources
Helixi270 – 2734Combined sources
Beta strandi278 – 2803Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-123, 149-666.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28867.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9090C2Add
BLAST
Domaini347 – 601255Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini602 – 67372AGC-kinase C-terminalAdd
BLAST

Domaini

The C1 domain, containing the phorbol ester/DAG-type region 1 (C1A) and 2 (C1B), is the diacylglycerol sensor.
The C2 domain is a non-calcium binding domain. It binds proteins containing phosphotyrosine in a sequence-specific manner (By similarity).By similarity

Sequence similaritiesi

Contains 1 AGC-kinase C-terminal domain.Curated
Contains 1 C2 domain.Curated
Contains 2 phorbol-ester/DAG-type zinc fingers.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Zinc finger

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

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00770000120449.
HOGENOMiHOG000233022.
HOVERGENiHBG108317.
InParanoidiP28867.
KOiK06068.
OMAiGEDEAKF.
OrthoDBiEOG77M8QM.
PhylomeDBiP28867.
TreeFamiTF102004.

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.
IPR002219. PE/DAG-bd.
IPR027436. PKC_delta.
IPR017892. Pkinase_C.
IPR014376. Prot_kin_PKC_delta.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
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: 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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti214 – 2141N → I in BAA36408. (PubMed:11558579)Curated
Sequence conflicti226 – 2261N → S in BAA36408. (PubMed:11558579)Curated
Sequence conflicti319 – 3191E → D in AAA73056. (PubMed:1868068)Curated
Sequence conflicti330 – 3301G → W in AAA73056. (PubMed:1868068)Curated
Sequence conflicti337 – 3371E → V in AAA73056. (PubMed:1868068)Curated
Sequence conflicti501 – 5011G → D in AAA73056. (PubMed:1868068)Curated
Sequence conflicti503 – 5031A → P in AAA73056. (PubMed:1868068)Curated
Sequence conflicti513 – 5131I → S in AAA73056. (PubMed:1868068)Curated
Sequence conflicti518 – 5203LQG → PARA in BAA36408. (PubMed:11558579)Curated
Sequence conflicti538 – 5381E → R in BAA36408. (PubMed:11558579)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei326 – 3261L → LGEAGSHISLKLSFPSRAKE KDSSETC in isoform 2. 1 PublicationVSP_004741

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]
PIRiA40281. KIMSCD.
RefSeqiNP_035233.1. NM_011103.3. [P28867-1]
XP_006518758.1. XM_006518695.1. [P28867-2]
XP_006518759.1. XM_006518696.1. [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 .
CCDSi CCDS26895.1. [P28867-1 ]
PIRi A40281. KIMSCD.
RefSeqi NP_035233.1. NM_011103.3. [P28867-1 ]
XP_006518758.1. XM_006518695.1. [P28867-2 ]
XP_006518759.1. XM_006518696.1. [P28867-2 ]
UniGenei Mm.2314.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1PTQ X-ray 1.95 A 231-280 [» ]
1PTR X-ray 2.20 A 231-280 [» ]
3UEJ X-ray 1.30 A/B 231-280 [» ]
3UEY X-ray 1.30 A/B 231-280 [» ]
3UFF X-ray 1.30 A/B 231-280 [» ]
3UGD X-ray 1.45 A/B 231-280 [» ]
3UGI X-ray 1.36 A/B 231-280 [» ]
3UGL X-ray 1.36 A/B 231-280 [» ]
ProteinModelPortali P28867.
SMRi P28867. Positions 1-123, 149-666.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202197. 7 interactions.
DIPi DIP-1169N.
IntActi P28867. 3 interactions.
MINTi MINT-97906.

Chemistry

BindingDBi P28867.
ChEMBLi CHEMBL2560.

PTM databases

PhosphoSitei P28867.

Proteomic databases

MaxQBi P28867.
PaxDbi P28867.
PRIDEi P28867.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000022521 ; ENSMUSP00000022521 ; ENSMUSG00000021948 . [P28867-2 ]
ENSMUST00000112208 ; ENSMUSP00000107827 ; ENSMUSG00000021948 . [P28867-1 ]
ENSMUST00000112210 ; ENSMUSP00000107829 ; ENSMUSG00000021948 . [P28867-1 ]
ENSMUST00000112211 ; ENSMUSP00000107830 ; ENSMUSG00000021948 . [P28867-2 ]
GeneIDi 18753.
KEGGi mmu:18753.
UCSCi uc007sve.2. mouse. [P28867-1 ]
uc007svg.2. mouse. [P28867-2 ]

Organism-specific databases

CTDi 5580.
MGIi MGI:97598. Prkcd.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00770000120449.
HOGENOMi HOG000233022.
HOVERGENi HBG108317.
InParanoidi P28867.
KOi K06068.
OMAi GEDEAKF.
OrthoDBi EOG77M8QM.
PhylomeDBi P28867.
TreeFami TF102004.

Enzyme and pathway databases

BRENDAi 2.7.11.13. 3474.
Reactomei REACT_188269. DAG and IP3 signaling.
REACT_198660. Interferon gamma signaling.
REACT_198691. HuR stabilizes mRNA.
REACT_210240. Role of phospholipids in phagocytosis.
REACT_215587. Calmodulin induced events.
REACT_219232. Effects of PIP2 hydrolysis.
REACT_224460. Apoptotic cleavage of cellular proteins.
REACT_245086. VEGFR2 mediated cell proliferation.
REACT_258013. G alpha (z) signalling events.

Miscellaneous databases

ChiTaRSi Prkcd. mouse.
EvolutionaryTracei P28867.
NextBioi 294929.
PROi P28867.
SOURCEi Search...

Gene expression databases

Bgeei P28867.
CleanExi MM_PRKCD.
ExpressionAtlasi P28867. baseline and differential.
Genevestigatori P28867.

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.
IPR002219. PE/DAG-bd.
IPR027436. PKC_delta.
IPR017892. Pkinase_C.
IPR014376. Prot_kin_PKC_delta.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
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. "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. "Increased proliferation of B cells and auto-immunity in mice lacking protein kinase Cdelta."
    Miyamoto A., Nakayama K., Imaki H., Hirose S., Jiang Y., Abe M., Tsukiyama T., Nagahama H., Ohno S., Hatakeyama S., Nakayama K.I.
    Nature 416:865-869(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION IN B CELL PROLIFERATION, FUNCTION IN B-CELL IMMUNE RESPONSES.
  9. "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.
  10. "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.
  11. "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.
  12. "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].
  13. "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.
  14. "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.
  15. "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.

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 26, 2014
This is version 158 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

External Data

Dasty 3