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Protein

Protein kinase C delta type

Gene

PRKCD

Organism
Homo sapiens (Human)
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 as well as survival of several cancers, 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. Is highly expressed in a number of cancer cells and promotes cell survival and resistance against chemotherapeutic drugs by inducing cyclin D1 (CCND1) and hyperphosphorylation of RB1, and via several pro-survival pathways, including NF-kappa-B, AKT1 and MAPK1/3 (ERK1/2). 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 (By similarity). Phosphorylates ELAVL1 in response to angiotensin-2 treatment (PubMed:18285462).By similarity7 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication
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-507 (activation loop of the kinase domain), Ser-645 (turn motif) and Ser-664 (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 sitei378ATPPROSITE-ProRule annotation1
Active sitei473Proton 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 bindingi355 – 363ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • calcium-independent protein kinase C activity Source: BHF-UCL
  • enzyme activator activity Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • insulin receptor substrate binding Source: BHF-UCL
  • kinase binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
  • protein kinase activity Source: UniProtKB
  • protein kinase binding Source: ParkinsonsUK-UCL
  • protein kinase C activity Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  • activation of phospholipase C activity Source: Reactome
  • activation of protein kinase activity Source: ParkinsonsUK-UCL
  • apoptotic process Source: UniProtKB
  • B cell proliferation Source: Ensembl
  • cell chemotaxis Source: UniProtKB
  • cell cycle Source: UniProtKB-KW
  • cellular component disassembly involved in execution phase of apoptosis Source: Reactome
  • cellular response to angiotensin Source: UniProtKB
  • cellular response to hydrogen peroxide Source: ParkinsonsUK-UCL
  • cellular response to hydroperoxide Source: UniProtKB
  • cellular senescence Source: BHF-UCL
  • defense response to bacterium Source: UniProtKB
  • Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  • histone phosphorylation Source: UniProtKB
  • immunoglobulin mediated immune response Source: Ensembl
  • interferon-gamma-mediated signaling pathway Source: Reactome
  • interleukin-10 production Source: Ensembl
  • interleukin-12 production Source: Ensembl
  • intrinsic apoptotic signaling pathway in response to oxidative stress Source: ParkinsonsUK-UCL
  • negative regulation of actin filament polymerization Source: UniProtKB
  • negative regulation of filopodium assembly Source: UniProtKB
  • negative regulation of glial cell apoptotic process Source: UniProtKB
  • negative regulation of inflammatory response Source: BHF-UCL
  • negative regulation of insulin receptor signaling pathway Source: BHF-UCL
  • negative regulation of MAP kinase activity Source: BHF-UCL
  • negative regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
  • negative regulation of platelet aggregation Source: UniProtKB
  • negative regulation of protein binding Source: BHF-UCL
  • neutrophil activation Source: UniProtKB
  • peptidyl-serine phosphorylation Source: UniProtKB
  • peptidyl-threonine phosphorylation Source: UniProtKB
  • platelet activation Source: Reactome
  • positive regulation of apoptotic signaling pathway Source: Ensembl
  • positive regulation of ceramide biosynthetic process Source: BHF-UCL
  • positive regulation of endodeoxyribonuclease activity Source: UniProtKB
  • positive regulation of glucosylceramide catabolic process Source: BHF-UCL
  • positive regulation of phospholipid scramblase activity Source: UniProtKB
  • positive regulation of protein dephosphorylation Source: BHF-UCL
  • positive regulation of protein import into nucleus Source: UniProtKB
  • positive regulation of response to DNA damage stimulus Source: UniProtKB
  • positive regulation of sphingomyelin catabolic process Source: BHF-UCL
  • positive regulation of superoxide anion generation Source: UniProtKB
  • protein phosphorylation Source: UniProtKB
  • protein stabilization Source: UniProtKB
  • regulation of actin cytoskeleton organization Source: CACAO
  • regulation of mRNA stability Source: Reactome
  • regulation of receptor activity Source: BHF-UCL
  • signal transduction Source: Reactome
  • stimulatory C-type lectin receptor signaling pathway Source: Reactome
  • termination of signal transduction Source: BHF-UCL
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

BioCyciZFISH:HS08969-MONOMER.
BRENDAi2.7.11.13. 2681.
ReactomeiR-HSA-111465. Apoptotic cleavage of cellular proteins.
R-HSA-111933. Calmodulin induced events.
R-HSA-114508. Effects of PIP2 hydrolysis.
R-HSA-1250196. SHC1 events in ERBB2 signaling.
R-HSA-1489509. DAG and IP3 signaling.
R-HSA-2029485. Role of phospholipids in phagocytosis.
R-HSA-418597. G alpha (z) signalling events.
R-HSA-450520. HuR (ELAVL1) binds and stabilizes mRNA.
R-HSA-5218921. VEGFR2 mediated cell proliferation.
R-HSA-5607764. CLEC7A (Dectin-1) signaling.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-877300. Interferon gamma signaling.
SABIO-RKQ05655.
SignaLinkiQ05655.
SIGNORiQ05655.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein kinase C delta type (EC:2.7.11.131 Publication)
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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:9399. PRKCD.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Autoimmune lymphoproliferative syndrome 3 (ALPS3)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA primary immunodeficiency characterized by antibody deficiency, hypogammaglobulinemia, recurrent bacterial infections and an inability to mount an antibody response to antigen. The defect results from a failure of B-cell differentiation and impaired secretion of immunoglobulins; the numbers of circulating B-cells is usually in the normal range, but can be low. CVID9 patients have B-cell deficiency and severe autoimmunity.
See also OMIM:615559

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi299S → A: Loss of phosphorylation. 1 Publication1
Mutagenesisi507T → A: No effect on kinase activity. 1 Publication1

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

DisGeNETi5580.
MalaCardsiPRKCD.
MIMi615559. phenotype.
OpenTargetsiENSG00000163932.
Orphaneti3261. Autoimmune lymphoproliferative syndrome.
300345. Autosomal recessive systemic lupus erythematosus.
1572. Common variable immunodeficiency.
PharmGKBiPA33763.

Chemistry databases

ChEMBLiCHEMBL2996.
DrugBankiDB05013. Ingenol Mebutate.
DB00675. Tamoxifen.
GuidetoPHARMACOLOGYi1485.

Polymorphism and mutation databases

BioMutaiPRKCD.
DMDMi205371776.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000556941 – 676Protein kinase C delta typeAdd BLAST676
ChainiPRO_00004216671 – 329Protein kinase C delta type regulatory subunitBy similarityAdd BLAST329
ChainiPRO_0000421668330 – 676Protein kinase C delta type catalytic subunitBy similarityAdd BLAST347

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei43PhosphothreonineBy similarity1
Modified residuei50Phosphothreonine1 Publication1
Modified residuei64PhosphotyrosineBy similarity1
Modified residuei130PhosphoserineCombined sources1
Modified residuei141PhosphothreonineCombined sources1 Publication1
Modified residuei155Phosphotyrosine1 Publication1
Modified residuei218PhosphothreonineCombined sources1
Modified residuei299Phosphoserine; by autocatalysisCombined sources1 Publication1
Modified residuei302Phosphoserine; by autocatalysisCombined sources1 Publication1
Modified residuei304Phosphoserine; by autocatalysisCombined sources2 Publications1
Modified residuei307PhosphoserineCombined sources1
Modified residuei313PhosphotyrosineCombined sources1 Publication1
Modified residuei334Phosphotyrosine; by SRC1 Publication1
Modified residuei374PhosphotyrosineCombined sources1
Modified residuei451Phosphothreonine1 Publication1
Modified residuei503PhosphoserineCombined sources1
Modified residuei506Phosphoserine1 Publication1
Modified residuei507Phosphothreonine; by autocatalysis1 Publication1 Publication1
Modified residuei567Phosphotyrosine1 Publication1
Modified residuei645PhosphoserineCombined sources1 Publication1
Modified residuei654PhosphoserineCombined sources1
Modified residuei658PhosphoserineCombined sources1
Modified residuei664PhosphoserineCombined sources1 Publication1

Post-translational modificationi

Autophosphorylated and/or phosphorylated at Thr-507, within the activation loop; phosphorylation at Thr-507 is not a prerequisite for enzymatic activity. Autophosphorylated at Ser-299, Ser-302 and Ser-304. 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-313, Tyr-334 and Tyr-567; phosphorylation of Tyr-313 and Tyr-567 following thrombin stimulation potentiates its kinase activity. Phosphorylated by protein kinase PDPK1; phosphorylation is inhibited by the apoptotic C-terminal cleavage product of PKN2.5 Publications
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
Sitei329 – 330Cleavage; by caspase-3By similarity2

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ05655.
MaxQBiQ05655.
PaxDbiQ05655.
PeptideAtlasiQ05655.
PRIDEiQ05655.

PTM databases

iPTMnetiQ05655.
PhosphoSitePlusiQ05655.

Miscellaneous databases

PMAP-CutDBQ05655.

Expressioni

Gene expression databases

BgeeiENSG00000163932.
CleanExiHS_PRKCD.
ExpressionAtlasiQ05655. baseline and differential.
GenevisibleiQ05655. HS.

Organism-specific databases

HPAiCAB010469.
CAB013225.
HPA001863.
HPA001890.

Interactioni

Subunit structurei

Interacts with PDPK1 (via N-terminal region), RAD9A, CDCP1, MUC1 and VASP.5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei48Interaction with phosphotyrosine-containing peptide1
Sitei62Interaction with phosphotyrosine-containing peptide1
Sitei67Interaction with phosphotyrosine-containing peptide1
Sitei123Interaction with phosphotyrosine-containing peptide1

Binary interactionsi

WithEntry#Exp.IntActNotes
CARD11Q9BXL77EBI-704279,EBI-7006141
DIABLOQ9NR284EBI-704279,EBI-517508
FYNP062415EBI-704279,EBI-515315
GAP43P176774EBI-704279,EBI-1267511
IL32C6GKH13EBI-704279,EBI-9547476
IL32P24001-27EBI-704279,EBI-8800907
NCF2P198783EBI-704279,EBI-489611
TOP2AP1138810EBI-704279,EBI-539628
TP53P046374EBI-704279,EBI-366083
TP63Q9H3D42EBI-704279,EBI-2337775

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi111566. 94 interactors.
DIPiDIP-29954N.
IntActiQ05655. 48 interactors.
MINTiMINT-1346366.
STRINGi9606.ENSP00000331602.

Chemistry databases

BindingDBiQ05655.

Structurei

Secondary structure

1676
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1 – 13Combined sources13
Beta strandi20 – 23Combined sources4
Beta strandi27 – 38Combined sources12
Beta strandi41 – 45Combined sources5
Beta strandi58 – 62Combined sources5
Beta strandi68 – 76Combined sources9
Beta strandi79 – 87Combined sources9
Helixi88 – 96Combined sources9
Turni97 – 100Combined sources4
Beta strandi101 – 107Combined sources7
Beta strandi109 – 111Combined sources3
Beta strandi113 – 123Combined sources11
Helixi156 – 158Combined sources3
Beta strandi161 – 164Combined sources4
Beta strandi173 – 175Combined sources3
Beta strandi181 – 183Combined sources3
Beta strandi186 – 189Combined sources4
Turni190 – 192Combined sources3
Helixi200 – 202Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YRKX-ray1.70A1-123[»]
2YUUNMR-A149-218[»]
ProteinModelPortaliQ05655.
SMRiQ05655.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ05655.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 90C2Add BLAST90
Domaini349 – 603Protein kinasePROSITE-ProRule annotationAdd BLAST255
Domaini604 – 675AGC-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.

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.
InParanoidiQ05655.
KOiK06068.
OMAiGEDEAKF.
OrthoDBiEOG091G0QRS.
PhylomeDBiQ05655.
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: Q05655-1) [UniParc]FASTAAdd to basket

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
MAPFLRIAFN SYELGSLQAE DEANQPFCAV KMKEALSTER GKTLVQKKPT
60 70 80 90 100
MYPEWKSTFD AHIYEGRVIQ IVLMRAAEEP VSEVTVGVSV LAERCKKNNG
110 120 130 140 150
KAEFWLDLQP QAKVLMSVQY FLEDVDCKQS MRSEDEAKFP TMNRRGAIKQ
160 170 180 190 200
AKIHYIKNHE FIATFFGQPT FCSVCKDFVW GLNKQGYKCR QCNAAIHKKC
210 220 230 240 250
IDKIIGRCTG TAANSRDTIF QKERFNIDMP HRFKVHNYMS PTFCDHCGSL
260 270 280 290 300
LWGLVKQGLK CEDCGMNVHH KCREKVANLC GINQKLLAEA LNQVTQRASR
310 320 330 340 350
RSDSASSEPV GIYQGFEKKT GVAGEDMQDN SGTYGKIWEG SSKCNINNFI
360 370 380 390 400
FHKVLGKGSF GKVLLGELKG RGEYFAIKAL KKDVVLIDDD VECTMVEKRV
410 420 430 440 450
LTLAAENPFL THLICTFQTK DHLFFVMEFL NGGDLMYHIQ DKGRFELYRA
460 470 480 490 500
TFYAAEIMCG LQFLHSKGII YRDLKLDNVL LDRDGHIKIA DFGMCKENIF
510 520 530 540 550
GESRASTFCG TPDYIAPEIL QGLKYTFSVD WWSFGVLLYE MLIGQSPFHG
560 570 580 590 600
DDEDELFESI RVDTPHYPRW ITKESKDILE KLFEREPTKR LGVTGNIKIH
610 620 630 640 650
PFFKTINWTL LEKRRLEPPF RPKVKSPRDY SNFDQEFLNE KARLSYSDKN
660 670
LIDSMDQSAF AGFSFVNPKF EHLLED
Length:676
Mass (Da):77,505
Last modified:September 2, 2008 - v2
Checksum:i013F4314A2EE331A
GO
Isoform 2 (identifier: Q05655-2) [UniParc]FASTAAdd to basket
Also known as: PKCdeltaVIII

The sequence of this isoform differs from the canonical sequence as follows:
     328-328: Q → QGEAGSIAPLRFLFPLRPKKGDCPPFHCQVRQ

Note: Antiapoptotic isoform, resistant to caspase-3 cleavage.
Show »
Length:707
Mass (Da):80,953
Checksum:iF1380490CC52EF07
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti524K → R in BAG36031 (PubMed:14702039).Curated1
Sequence conflicti533S → A no nucleotide entry (PubMed:7988719).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_035347348N → S.Corresponds to variant rs33911937dbSNPEnsembl.1
Natural variantiVAR_006175375F → S.1 PublicationCorresponds to variant rs1056998dbSNPEnsembl.1
Natural variantiVAR_035348410L → F.Corresponds to variant rs34502209dbSNPEnsembl.1
Natural variantiVAR_046009483R → W.Corresponds to variant rs35891605dbSNPEnsembl.1
Natural variantiVAR_020610494M → V.1 Publication1
Natural variantiVAR_006176593V → M.1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_043899328Q → QGEAGSIAPLRFLFPLRPKK GDCPPFHCQVRQ in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07860 mRNA. Translation: AAA03176.1.
L07861 mRNA. Translation: AAA03175.1.
AK313216 mRNA. Translation: BAG36031.1.
CH471055 Genomic DNA. Translation: EAW65279.1.
BC043350 mRNA. Translation: AAH43350.1.
Z22521 mRNA. Translation: CAA80249.1.
D10495 mRNA. Translation: BAA01381.1.
DQ516383 mRNA. Translation: ABF68960.1.
CCDSiCCDS2870.1. [Q05655-1]
PIRiS35704.
RefSeqiNP_001303256.1. NM_001316327.1. [Q05655-1]
NP_006245.2. NM_006254.3. [Q05655-1]
NP_997704.1. NM_212539.1. [Q05655-1]
XP_006713322.1. XM_006713259.2. [Q05655-1]
XP_016862344.1. XM_017006855.1. [Q05655-1]
XP_016862345.1. XM_017006856.1. [Q05655-1]
UniGeneiHs.155342.

Genome annotation databases

EnsembliENST00000330452; ENSP00000331602; ENSG00000163932. [Q05655-1]
ENST00000394729; ENSP00000378217; ENSG00000163932. [Q05655-1]
GeneIDi5580.
KEGGihsa:5580.
UCSCiuc003dgl.4. human. [Q05655-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07860 mRNA. Translation: AAA03176.1.
L07861 mRNA. Translation: AAA03175.1.
AK313216 mRNA. Translation: BAG36031.1.
CH471055 Genomic DNA. Translation: EAW65279.1.
BC043350 mRNA. Translation: AAH43350.1.
Z22521 mRNA. Translation: CAA80249.1.
D10495 mRNA. Translation: BAA01381.1.
DQ516383 mRNA. Translation: ABF68960.1.
CCDSiCCDS2870.1. [Q05655-1]
PIRiS35704.
RefSeqiNP_001303256.1. NM_001316327.1. [Q05655-1]
NP_006245.2. NM_006254.3. [Q05655-1]
NP_997704.1. NM_212539.1. [Q05655-1]
XP_006713322.1. XM_006713259.2. [Q05655-1]
XP_016862344.1. XM_017006855.1. [Q05655-1]
XP_016862345.1. XM_017006856.1. [Q05655-1]
UniGeneiHs.155342.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YRKX-ray1.70A1-123[»]
2YUUNMR-A149-218[»]
ProteinModelPortaliQ05655.
SMRiQ05655.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111566. 94 interactors.
DIPiDIP-29954N.
IntActiQ05655. 48 interactors.
MINTiMINT-1346366.
STRINGi9606.ENSP00000331602.

Chemistry databases

BindingDBiQ05655.
ChEMBLiCHEMBL2996.
DrugBankiDB05013. Ingenol Mebutate.
DB00675. Tamoxifen.
GuidetoPHARMACOLOGYi1485.

PTM databases

iPTMnetiQ05655.
PhosphoSitePlusiQ05655.

Polymorphism and mutation databases

BioMutaiPRKCD.
DMDMi205371776.

Proteomic databases

EPDiQ05655.
MaxQBiQ05655.
PaxDbiQ05655.
PeptideAtlasiQ05655.
PRIDEiQ05655.

Protocols and materials databases

DNASUi5580.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000330452; ENSP00000331602; ENSG00000163932. [Q05655-1]
ENST00000394729; ENSP00000378217; ENSG00000163932. [Q05655-1]
GeneIDi5580.
KEGGihsa:5580.
UCSCiuc003dgl.4. human. [Q05655-1]

Organism-specific databases

CTDi5580.
DisGeNETi5580.
GeneCardsiPRKCD.
HGNCiHGNC:9399. PRKCD.
HPAiCAB010469.
CAB013225.
HPA001863.
HPA001890.
MalaCardsiPRKCD.
MIMi176977. gene.
615559. phenotype.
neXtProtiNX_Q05655.
OpenTargetsiENSG00000163932.
Orphaneti3261. Autoimmune lymphoproliferative syndrome.
300345. Autosomal recessive systemic lupus erythematosus.
1572. Common variable immunodeficiency.
PharmGKBiPA33763.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0694. Eukaryota.
ENOG410XNPH. LUCA.
GeneTreeiENSGT00820000126964.
HOGENOMiHOG000233022.
HOVERGENiHBG108317.
InParanoidiQ05655.
KOiK06068.
OMAiGEDEAKF.
OrthoDBiEOG091G0QRS.
PhylomeDBiQ05655.
TreeFamiTF102004.

Enzyme and pathway databases

BioCyciZFISH:HS08969-MONOMER.
BRENDAi2.7.11.13. 2681.
ReactomeiR-HSA-111465. Apoptotic cleavage of cellular proteins.
R-HSA-111933. Calmodulin induced events.
R-HSA-114508. Effects of PIP2 hydrolysis.
R-HSA-1250196. SHC1 events in ERBB2 signaling.
R-HSA-1489509. DAG and IP3 signaling.
R-HSA-2029485. Role of phospholipids in phagocytosis.
R-HSA-418597. G alpha (z) signalling events.
R-HSA-450520. HuR (ELAVL1) binds and stabilizes mRNA.
R-HSA-5218921. VEGFR2 mediated cell proliferation.
R-HSA-5607764. CLEC7A (Dectin-1) signaling.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-877300. Interferon gamma signaling.
SABIO-RKQ05655.
SignaLinkiQ05655.
SIGNORiQ05655.

Miscellaneous databases

ChiTaRSiPRKCD. human.
EvolutionaryTraceiQ05655.
GeneWikiiPRKCD.
GenomeRNAii5580.
PMAP-CutDBQ05655.
PROiQ05655.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000163932.
CleanExiHS_PRKCD.
ExpressionAtlasiQ05655. baseline and differential.
GenevisibleiQ05655. HS.

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_HUMAN
AccessioniPrimary (citable) accession number: Q05655
Secondary accession number(s): B0KZ81
, B2R834, Q15144, Q86XJ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: September 2, 2008
Last modified: November 30, 2016
This is version 189 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. 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.