P28867 (KPCD_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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:

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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	674 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.14
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. Cytoplasm › perinuclear 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 process	Apoptosis Cell cycle
Cellular component	Cytoplasm Endoplasmic reticulum Membrane Mitochondrion Nucleus
Coding sequence diversity	Alternative splicing
Disease	Tumor suppressor
Domain	Repeat Zinc-finger
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	B cell proliferation Inferred from mutant phenotype PubMed 11976687. Source: MGI apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW aspartate transport Inferred from electronic annotation. Source: Compara cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cellular response to glucose starvation Inferred from electronic annotation. Source: Compara cellular response to insulin stimulus Inferred from electronic annotation. Source: Compara cellular senescence Inferred from electronic annotation. Source: Compara collagen metabolic process Inferred from electronic annotation. Source: Compara defense response to bacterium Inferred from mutant phenotype PubMed 22885697. Source: UniProtKB immunoglobulin mediated immune response Inferred from mutant phenotype PubMed 11976687. Source: MGI induction of apoptosis Inferred from electronic annotation. Source: Compara 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: Compara negative regulation of MAP kinase activity Inferred from electronic annotation. Source: Compara 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: Compara peptidyl-threonine phosphorylation Inferred from electronic annotation. Source: Compara positive regulation of MAP kinase activity Inferred from electronic annotation. Source: Compara positive regulation of ceramide biosynthetic process Inferred from electronic annotation. Source: Compara positive regulation of glucose import Inferred from electronic annotation. Source: Compara positive regulation of glucosylceramide catabolic process Inferred from electronic annotation. Source: Compara positive regulation of phospholipid scramblase activity Inferred from electronic annotation. Source: Compara positive regulation of protein dephosphorylation Inferred from electronic annotation. Source: Compara positive regulation of response to DNA damage stimulus Inferred from electronic annotation. Source: Compara positive regulation of sphingomyelin catabolic process Inferred from electronic annotation. Source: Compara positive regulation of superoxide anion generation Inferred from sequence or structural similarity. Source: UniProtKB protein autophosphorylation Inferred from electronic annotation. Source: Compara response to amino acid stimulus Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to ethanol Inferred from electronic annotation. Source: Compara response to glucose stimulus Inferred from electronic annotation. Source: Compara response to heat Inferred from electronic annotation. Source: Compara response to hydrogen peroxide Inferred from electronic annotation. Source: Compara response to hypoxia Inferred from electronic annotation. Source: Compara response to mechanical stimulus Inferred from electronic annotation. Source: Compara response to organic cyclic compound Inferred from electronic annotation. Source: Compara termination of signal transduction Inferred from electronic annotation. Source: Compara
Cellular_component	cell-cell junction Inferred from direct assay PubMed 10882525. Source: MGI cytosol Inferred from electronic annotation. Source: Compara endoplasmic reticulum Inferred from sequence or structural similarity. Source: UniProtKB mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear matrix Inferred from direct assay PubMed 10882525. Source: MGI perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calcium-independent protein kinase C activity Inferred from electronic annotation. Source: Compara enzyme activator activity Inferred from electronic annotation. Source: Compara metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW non-membrane spanning protein tyrosine kinase activity Inferred from electronic annotation. Source: 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 674

674

Protein kinase C delta type

PRO_0000055695

Chain

1 – 327

327

Protein kinase C delta type regulatory subunit By similarity

PRO_0000421669

Chain

328 – 674

347

Protein kinase C delta type catalytic subunit By similarity

PRO_0000421670

Regions

Domain

1 – 90

90

C2

Domain

347 – 601

255

Protein kinase

Domain

602 – 673

72

AGC-kinase C-terminal

Zinc finger

158 – 208

51

Phorbol-ester/DAG-type 1

Zinc finger

230 – 280

51

Phorbol-ester/DAG-type 2

Nucleotide binding

353 – 361

9

ATP By similarity

Sites

Active site

471

1

Proton acceptor By similarity

Binding site

376

1

ATP By similarity

Site

48

1

Interaction with phosphotyrosine-containing peptide By similarity

Site

62

1

Interaction with phosphotyrosine-containing peptide By similarity

Site

67

1

Interaction with phosphotyrosine-containing peptide By similarity

Site

123

1

Interaction with phosphotyrosine-containing peptide By similarity

Site

327 – 328

2

Cleavage; by caspase-3 By similarity

Amino acid modifications

Modified residue

43

1

Phosphothreonine Ref.12

Modified residue

64

1

Phosphotyrosine By similarity

Modified residue

130

1

Phosphoserine By similarity

Modified residue

155

1

Phosphotyrosine By similarity

Modified residue

218

1

Phosphothreonine By similarity

Modified residue

299

1

Phosphoserine; by autocatalysis By similarity

Modified residue

311

1

Phosphotyrosine; by SRC Probable

Modified residue

332

1

Phosphotyrosine; by SRC By similarity

Modified residue

372

1

Phosphotyrosine By similarity

Modified residue

505

1

Phosphothreonine; by autocatalysis Ref.7 Ref.9

Modified residue

565

1

Phosphotyrosine By similarity

Modified residue

643

1

Phosphoserine Probable

Modified residue

652

1

Phosphoserine By similarity

Modified residue

662

1

Phosphoserine Ref.11 Ref.12

Natural variations

Alternative sequence

326

1

L → LGEAGSHISLKLSFPSRAKE KDSSETC in isoform 2.

VSP_004741

Experimental info

Sequence conflict

214

1

N → I in BAA36408. Ref.4

Sequence conflict

226

1

N → S in BAA36408. Ref.4

Sequence conflict

319

1

E → D in AAA73056. Ref.1

Sequence conflict

330

1

G → W in AAA73056. Ref.1

Sequence conflict

337

1

E → V in AAA73056. Ref.1

Sequence conflict

501

1

G → D in AAA73056. Ref.1

Sequence conflict

503

1

A → P in AAA73056. Ref.1

Sequence conflict

513

1

I → S in AAA73056. Ref.1

Sequence conflict

518 – 520

3

LQG → PARA in BAA36408. Ref.4

Sequence conflict

538

1

E → R in BAA36408. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

674

Helix Strand Turn

Details...

Beta strand

233 – 236

4

Turn

245 – 247

3

Beta strand

253 – 256

4

Beta strand

258 – 261

4

Turn

262 – 264

3

Helix

270 – 273

4

Beta strand

278 – 280

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (PKC-delta-I) [UniParc]. Last modified March 27, 2002. Version 3. Checksum: 6E9F753348F03D59	FASTA	674	77,547
	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
	Isoform 2 (PKC-delta-II) [UniParc]. Checksum: CFB6D8A58220C962	FASTA	700	80,294
	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 SGSDILGEAG SHISLKLSFP SRAKEKDSSE TCDNNGTYGK 370 380 390 400 410 420 IWEGSTRCTL ENFTFQKVLG KGSFGKVLLA ELKGKDKYFA IKCLKKDVVL IDDDVECTMV 430 440 450 460 470 480 EKRVLALAWE SPFLTHLICT FQTKDHLFFV MEFLNGGDLM FHIQDKGRFE LYRATFYAAE 490 500 510 520 530 540 IICGLQFLHS KGIIYRDLKL DNVMLDRDGH IKIADFGMCK ENIFGEGRAS TFCGTPDYIA 550 560 570 580 590 600 PEILQGLKYS FSVDWWSFGV LLYEMLIGQS PFHGDDEDEL FESIRVDTPH YPRWITKESK 610 620 630 640 650 660 DIMEKLFERD PDKRLGVTGN IRIHPFFKTI NWSLLEKRKV EPPFKPKVKS PSDYSNFDPE 670 680 690 700 FLNEKPQLSF SDKNLIDSMD QEAFHGFSFV NPKFEQFLDI

References

	« Hide 'large scale' referencesShow '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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Brain.
[11]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-662, MASS SPECTROMETRY. Tissue: Melanoma.
[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, MASS SPECTROMETRY. Tissue: Macrophage.
[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, MASS SPECTROMETRY. 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.
+	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.

IPI

IPI00125855.
IPI00227880.

PIR

KIMSCD. A40281.

RefSeq

NP_035233.1. NM_011103.3.

UniGene

Mm.2314.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P28867.

SMR

P28867. Positions 1-123, 149-666.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1169N.

IntAct

P28867. 2 interactions.

MINT

MINT-97906.

PTM databases

PhosphoSite

P28867.

Proteomic databases

PaxDb

P28867.

PRIDE

P28867.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000022521; ENSMUSP00000022521; ENSMUSG00000021948.
ENSMUST00000112208; ENSMUSP00000107827; ENSMUSG00000021948.
ENSMUST00000112210; ENSMUSP00000107829; ENSMUSG00000021948.
ENSMUST00000112211; ENSMUSP00000107830; ENSMUSG00000021948.

GeneID

18753.

KEGG

mmu:18753.

UCSC

uc007svg.2. mouse.

Organism-specific databases

CTD

5580.

MGI

MGI:97598. Prkcd.

Phylogenomic databases

eggNOG

COG0515.

GeneTree

ENSGT00700000104479.

HOGENOM

HOG000233022.

HOVERGEN

HBG108317.

KO

K06068.

OMA

GEDEAKF.

OrthoDB

EOG4M91QX.

Enzyme and pathway databases

BRENDA

2.7.11.13. 3474.

Gene expression databases

ArrayExpress

P28867.

Bgee

P28867.

CleanEx

MM_PRKCD.

Genevestigator

P28867.

GermOnline

ENSMUSG00000021948. Mus musculus.

Family and domain databases

InterPro

IPR000961. AGC-kinase_C.
IPR000008. C2_Ca-dep.
IPR008973. C2_Ca/lipid-bd_dom_CaLB.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR017892. Pkinase_C.
IPR014376. Prot_kin_PKC_delta.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]

Pfam

PF00130. C1_1. 2 hits.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]

PIRSF

PIRSF000551. PKC_delta. 1 hit.

PRINTS

PR00008. DAGPEDOMAIN.

SMART

SM00109. C1. 2 hits.
SM00239. C2. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF49562. C2_CaLB. 1 hit.
SSF56112. Kinase_like. 1 hit.

PROSITE

PS51285. AGC_KINASE_CTER. 1 hit.
PS50004. C2. False negative.
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]

ProtoNet

Search...

Other

BindingDB

P28867.

ChEMBL

CHEMBL2560.

ChiTaRS

PRKCD. mouse.

EvolutionaryTrace

P28867.

NextBio

294929.

SOURCE

Search...

Entry information

Entry name

KPCD_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 141 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program