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Protein

Protein kinase C delta type

Gene

PRKCD

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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: Reactome
  • enzyme activator activity Source: UniProtKB
  • enzyme binding Source: BHF-UCL
  • 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: UniProtKB
  • protein kinase C activity Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  • 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 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
  • neutrophil degranulation Source: Reactome
  • 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 signaling receptor activity Source: BHF-UCL
  • signal transduction Source: ProtInc
  • stimulatory C-type lectin receptor signaling pathway Source: Reactome
  • termination of signal transduction Source: BHF-UCL

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processApoptosis, Cell cycle
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

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

EuPathDBiHostDB:ENSG00000163932.13
HGNCiHGNC:9399 PRKCD
MIMi176977 gene
neXtProtiNX_Q05655

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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
DrugBankiDB04376 13-Acetylphorbol
DB05013 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 SRCBy similarity1
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) (PubMed:11781095). Interacts with RAD9A (PubMed:12628935). Interacts with CDCP1 (PubMed:15851033). Interacts with MUC1 (PubMed:11877440). Interacts with VASP (PubMed:16940418). Interacts with CAVIN3 (By similarity). Interacts with PRKD2 (via N-terminus and zing-finger domain 1 and 2) in response to oxidative stress; the interaction is independent of PRKD2 tyrosine phosphorylation (PubMed:28428613).By similarity6 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

Show more details

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi111566, 98 interactors
CORUMiQ05655
DIPiDIP-29954N
ELMiQ05655
IntActiQ05655, 49 interactors
MINTiQ05655
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

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
OMAiFIFHKVL
OrthoDBiEOG091G0QRS
PhylomeDBiQ05655
TreeFamiTF102004

Family and domain databases

CDDicd00029 C1, 2 hits
cd05620 STKc_nPKC_delta, 1 hit
Gene3Di2.60.40.150, 1 hit
InterProiView protein in InterPro
IPR000961 AGC-kinase_C
IPR035892 C2_domain_sf
IPR020454 DAG/PE-bd
IPR011009 Kinase-like_dom_sf
IPR034667 nPKC_delta
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
PfamiView protein in Pfam
PF00130 C1_1, 2 hits
PF00069 Pkinase, 1 hit
PF00433 Pkinase_C, 1 hit
PIRSFiPIRSF000551 PKC_delta, 1 hit
PIRSF501104 Protein_kin_C_delta, 1 hit
PRINTSiPR00008 DAGPEDOMAIN
SMARTiView protein in SMART
SM00109 C1, 2 hits
SM00133 S_TK_X, 1 hit
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
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

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 dbSNP:rs33911937EnsemblClinVar.1
Natural variantiVAR_006175375F → S1 PublicationCorresponds to variant dbSNP:rs1056998Ensembl.1
Natural variantiVAR_035348410L → F. Corresponds to variant dbSNP:rs34502209Ensembl.1
Natural variantiVAR_046009483R → W. Corresponds to variant dbSNP:rs35891605Ensembl.1
Natural variantiVAR_020610494M → V1 Publication1
Natural variantiVAR_006176593V → M1 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
XP_016862344.1, XM_017006855.1
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

Similar proteinsi

Entry informationi

Entry nameiKPCD_HUMAN
AccessioniPrimary (citable) accession number: Q05655
Secondary accession number(s): B0KZ81
, B2R834, Q15144, Q86XJ6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: September 2, 2008
Last modified: May 23, 2018
This is version 203 of the entry and version 2 of the sequence. See 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

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