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Entry version 228 (02 Jun 2021)
Sequence version 2 (02 Sep 2008)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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 (PubMed:21810427, PubMed:21406692).

Negatively regulates B cell proliferation and also has an important function in self-antigen induced B cell tolerance induction (By similarity).

Upon DNA damage, activates the promoter of the death-promoting transcription factor BCLAF1/Btf to trigger BCLAF1-mediated p53/TP53 gene transcription and apoptosis (PubMed:21810427, PubMed:21406692).

In response to oxidative stress, interact with and activate CHUK/IKKA in the nucleus, causing the phosphorylation of p53/TP53 (PubMed:21810427, PubMed:21406692).

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 (PubMed:21810427, PubMed:21406692).

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 (By similarity).

Can protect glioma cells from the apoptosis induced by TNFSF10/TRAIL, probably by inducing increased phosphorylation and subsequent activation of AKT1 (PubMed:15774464).

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). Involved in antifungal immunity by mediating phosphorylation and activation of CARD9 downstream of C-type lectin receptors activation, promoting interaction between CARD9 and BCL10, followed by activation of NF-kappa-B and MAP kinase p38 pathways (By similarity).

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 (PubMed:19801500).

May also play a role in the regulation of NADPH oxidase activity in eosinophil after stimulation with IL5, leukotriene B4 or PMA (PubMed:11748588).

In collagen-induced platelet aggregation, acts a negative regulator of filopodia formation and actin polymerization by interacting with and negatively regulating VASP phosphorylation (PubMed:16940418).

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 (PubMed:19587372).

Phosphorylates MUC1 in the C-terminal and regulates the interaction between MUC1 and beta-catenin (PubMed:11877440).

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).

Phosphorylates mitochondrial phospolipid scramblase 3 (PLSCR3), resulting in increased cardiolipin expression on the mitochondrial outer membrane which facilitates apoptosis (PubMed:12649167).

Phosphorylates SMPD1 which induces SMPD1 secretion (PubMed:17303575).

2 PublicationsBy similarity9 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=10.5 nM for PLSC31 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei378ATPPROSITE-ProRule annotation1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei473Proton acceptorPROSITE-ProRule annotation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri158 – 208Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd BLAST51
    Zinc fingeri230 – 280Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd BLAST51
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi355 – 363ATPPROSITE-ProRule annotation9

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    2.7.11.13, 2681

    Pathway Commons web resource for biological pathway data

    More...
    PathwayCommonsi
    Q05655

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-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-5668599, RHO GTPases Activate NADPH Oxidases
    R-HSA-6798695, Neutrophil degranulation
    R-HSA-877300, Interferon gamma signaling

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    Q05655

    SignaLink: a signaling pathway resource with multi-layered regulatory networks

    More...
    SignaLinki
    Q05655

    SIGNOR Signaling Network Open Resource

    More...
    SIGNORi
    Q05655

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Protein kinase C delta typeCurated (EC:2.7.11.132 Publications)
    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
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:PRKCDImported
    Synonyms:PKCD1 Publication
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 3

    Organism-specific databases

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:9399, PRKCD

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    176977, gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_Q05655

    Eukaryotic Pathogen, Vector and Host Database Resources

    More...
    VEuPathDBi
    HostDB:ENSG00000163932.13

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Mitochondrion, Nucleus

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    <p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

    Autoimmune lymphoproliferative syndrome 3 (ALPS3)1 Publication
    The disease is caused by variants 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.
    Related information in OMIM

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi299S → A: Loss of phosphorylation. 1 Publication1
    Mutagenesisi507T → A: No effect on kinase activity. 1 Publication1

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    5580

    MalaCards human disease database

    More...
    MalaCardsi
    PRKCD
    MIMi615559, phenotype

    Open Targets

    More...
    OpenTargetsi
    ENSG00000163932

    Orphanet; a database dedicated to information on rare diseases and orphan drugs

    More...
    Orphaneti
    3261, Autoimmune lymphoproliferative syndrome
    300345, Autosomal systemic lupus erythematosus
    1572, Common variable immunodeficiency

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA33763

    Miscellaneous databases

    Pharos NIH Druggable Genome Knowledgebase

    More...
    Pharosi
    Q05655, Tclin

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL2996

    Drug and drug target database

    More...
    DrugBanki
    DB04376, 13-Acetylphorbol
    DB12010, Fostamatinib
    DB05013, Ingenol mebutate
    DB00675, Tamoxifen

    DrugCentral

    More...
    DrugCentrali
    Q05655

    IUPHAR/BPS Guide to PHARMACOLOGY

    More...
    GuidetoPHARMACOLOGYi
    1485

    Genetic variation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    PRKCD

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    205371776

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>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
    <p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>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

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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 (PubMed:19801500). Autophosphorylated at Ser-299, Ser-302 and Ser-304 (PubMed:17603046). Upon TNFSF10/TRAIL treatment, phosphorylated at Tyr-155; phosphorylation is required for its translocation to the endoplasmic reticulum and cleavage by caspase-3 (PubMed:15774464). Phosphorylated at Tyr-313, Tyr-334 and Tyr-567; phosphorylation of Tyr-313 and Tyr-567 following thrombin or zymosan stimulation potentiates its kinase activity (PubMed:17570831). Phosphorylated by protein kinase PDPK1; phosphorylation is inhibited by the apoptotic C-terminal cleavage product of PKN2 (PubMed:11781095). Phosphorylated at Tyr-313 through a SYK and SRC mechanism downstream of C-type lectin receptors activation, promoting its activation (By similarity).By similarity5 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
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei329 – 330Cleavage; by caspase-3By similarity2

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    The CPTAC Assay portal

    More...
    CPTACi
    CPTAC-1743

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    Q05655

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    Q05655

    MassIVE - Mass Spectrometry Interactive Virtual Environment

    More...
    MassIVEi
    Q05655

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    Q05655

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    Q05655

    PeptideAtlas

    More...
    PeptideAtlasi
    Q05655

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q05655

    ProteomicsDB: a multi-organism proteome resource

    More...
    ProteomicsDBi
    58342 [Q05655-1]
    58343 [Q05655-2]

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    Q05655

    Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

    More...
    PhosphoSitePlusi
    Q05655

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000163932, Expressed in blood and 191 other tissues

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    Q05655, baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    Q05655, HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    ENSG00000163932, Low tissue specificity

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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).

    Interacts with PLSC3; interaction is enhanced by UV irradiation (PubMed:12649167).

    By similarity7 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

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    Hide details

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...
    BioGRIDi
    111566, 122 interactors

    CORUM comprehensive resource of mammalian protein complexes

    More...
    CORUMi
    Q05655

    Database of interacting proteins

    More...
    DIPi
    DIP-29954N

    The Eukaryotic Linear Motif resource for Functional Sites in Proteins

    More...
    ELMi
    Q05655

    Protein interaction database and analysis system

    More...
    IntActi
    Q05655, 52 interactors

    Molecular INTeraction database

    More...
    MINTi
    Q05655

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000378217

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    Q05655

    Miscellaneous databases

    RNAct, Protein-RNA interaction predictions for model organisms.

    More...
    RNActi
    Q05655, protein

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1676
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    Q05655

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    Q05655

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1 – 106C2PROSITE-ProRule annotationAdd BLAST106
    Domaini349 – 603Protein kinasePROSITE-ProRule annotationAdd BLAST255
    Domaini604 – 675AGC-kinase C-terminalPROSITE-ProRule annotationAdd BLAST72

    <p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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.

    <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>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

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG0694, Eukaryota

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000155327

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_000288_54_4_1

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q05655

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    YAAEIMC

    Database of Orthologous Groups

    More...
    OrthoDBi
    222529at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    Q05655

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF102004

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd00029, C1, 2 hits
    cd05620, STKc_nPKC_delta, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    2.60.40.150, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View 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

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00130, C1_1, 2 hits
    PF00069, Pkinase, 1 hit
    PF00433, Pkinase_C, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF000551, PKC_delta, 1 hit
    PIRSF501104, Protein_kin_C_delta, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00008, DAGPEDOMAIN

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00109, C1, 2 hits
    SM00133, S_TK_X, 1 hit
    SM00220, S_TKc, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF56112, SSF56112, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51285, AGC_KINASE_CTER, 1 hit
    PS50004, C2, 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

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

    This entry has 2 described isoforms and 6 potential isoforms that are computationally mapped.Show allAlign All

    Isoform 1 (identifier: Q05655-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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.Curated
    Show »
    Length:707
    Mass (Da):80,953
    Checksum:iF1380490CC52EF07
    GO

    <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

    There are 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    C9K0E3C9K0E3_HUMAN
    Protein kinase C delta type
    PRKCD
    223Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    C9J9P1C9J9P1_HUMAN
    Protein kinase C delta type
    PRKCD
    125Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    A0A494C1T7A0A494C1T7_HUMAN
    Protein kinase C delta type
    PRKCD
    295Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    A0A494BZX2A0A494BZX2_HUMAN
    Protein kinase C delta type
    PRKCD
    112Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    C9JZU8C9JZU8_HUMAN
    Protein kinase C delta type
    PRKCD
    77Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    A0A494C125A0A494C125_HUMAN
    Protein kinase C delta type
    PRKCD
    38Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti524K → R in BAG36031 (PubMed:14702039).Curated1
    Sequence conflicti533S → A no nucleotide entry (PubMed:7988719).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>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:rs35891605EnsemblClinVar.1
    Natural variantiVAR_020610494M → V1 Publication1
    Natural variantiVAR_006176593V → M1 Publication1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_043899328Q → QGEAGSIAPLRFLFPLRPKK GDCPPFHCQVRQ in isoform 2. 1 Publication1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    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

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS2870.1 [Q05655-1]

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S35704

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_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

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000330452; ENSP00000331602; ENSG00000163932 [Q05655-1]
    ENST00000394729; ENSP00000378217; ENSG00000163932 [Q05655-1]
    ENST00000650739; ENSP00000498623; ENSG00000163932 [Q05655-1]
    ENST00000652449; ENSP00000498400; ENSG00000163932 [Q05655-1]
    ENST00000654719; ENSP00000499558; ENSG00000163932 [Q05655-1]

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    5580

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:5580

    UCSC genome browser

    More...
    UCSCi
    uc003dgl.4, human [Q05655-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    <p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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
    XP_016862344.1, XM_017006855.1
    XP_016862345.1, XM_017006856.1

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1YRKX-ray1.70A1-123[»]
    2YUUNMR-A149-218[»]
    SMRiQ05655
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi111566, 122 interactors
    CORUMiQ05655
    DIPiDIP-29954N
    ELMiQ05655
    IntActiQ05655, 52 interactors
    MINTiQ05655
    STRINGi9606.ENSP00000378217

    Chemistry databases

    BindingDBiQ05655
    ChEMBLiCHEMBL2996
    DrugBankiDB04376, 13-Acetylphorbol
    DB12010, Fostamatinib
    DB05013, Ingenol mebutate
    DB00675, Tamoxifen
    DrugCentraliQ05655
    GuidetoPHARMACOLOGYi1485

    PTM databases

    iPTMnetiQ05655
    PhosphoSitePlusiQ05655

    Genetic variation databases

    BioMutaiPRKCD
    DMDMi205371776

    Proteomic databases

    CPTACiCPTAC-1743
    EPDiQ05655
    jPOSTiQ05655
    MassIVEiQ05655
    MaxQBiQ05655
    PaxDbiQ05655
    PeptideAtlasiQ05655
    PRIDEiQ05655
    ProteomicsDBi58342 [Q05655-1]
    58343 [Q05655-2]

    Protocols and materials databases

    Antibodypedia a portal for validated antibodies

    More...
    Antibodypediai
    664, 1162 antibodies

    The DNASU plasmid repository

    More...
    DNASUi
    5580

    Genome annotation databases

    EnsembliENST00000330452; ENSP00000331602; ENSG00000163932 [Q05655-1]
    ENST00000394729; ENSP00000378217; ENSG00000163932 [Q05655-1]
    ENST00000650739; ENSP00000498623; ENSG00000163932 [Q05655-1]
    ENST00000652449; ENSP00000498400; ENSG00000163932 [Q05655-1]
    ENST00000654719; ENSP00000499558; ENSG00000163932 [Q05655-1]
    GeneIDi5580
    KEGGihsa:5580
    UCSCiuc003dgl.4, human [Q05655-1]

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    5580
    DisGeNETi5580

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    PRKCD
    HGNCiHGNC:9399, PRKCD
    HPAiENSG00000163932, Low tissue specificity
    MalaCardsiPRKCD
    MIMi176977, gene
    615559, phenotype
    neXtProtiNX_Q05655
    OpenTargetsiENSG00000163932
    Orphaneti3261, Autoimmune lymphoproliferative syndrome
    300345, Autosomal systemic lupus erythematosus
    1572, Common variable immunodeficiency
    PharmGKBiPA33763
    VEuPathDBiHostDB:ENSG00000163932.13

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG0694, Eukaryota
    GeneTreeiENSGT00940000155327
    HOGENOMiCLU_000288_54_4_1
    InParanoidiQ05655
    OMAiYAAEIMC
    OrthoDBi222529at2759
    PhylomeDBiQ05655
    TreeFamiTF102004

    Enzyme and pathway databases

    BRENDAi2.7.11.13, 2681
    PathwayCommonsiQ05655
    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-5668599, RHO GTPases Activate NADPH Oxidases
    R-HSA-6798695, Neutrophil degranulation
    R-HSA-877300, Interferon gamma signaling
    SABIO-RKiQ05655
    SignaLinkiQ05655
    SIGNORiQ05655

    Miscellaneous databases

    BioGRID ORCS database of CRISPR phenotype screens

    More...
    BioGRID-ORCSi
    5580, 12 hits in 1025 CRISPR screens

    ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

    More...
    ChiTaRSi
    PRKCD, human
    EvolutionaryTraceiQ05655

    The Gene Wiki collection of pages on human genes and proteins

    More...
    GeneWikii
    PRKCD

    Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

    More...
    GenomeRNAii
    5580
    PharosiQ05655, Tclin

    Protein Ontology

    More...
    PROi
    PR:Q05655
    RNActiQ05655, protein

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000163932, Expressed in blood and 191 other tissues
    ExpressionAtlasiQ05655, baseline and differential
    GenevisibleiQ05655, HS

    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
    PS50004, C2, 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

    MobiDB: a database of protein disorder and mobility annotations

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    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiKPCD_HUMAN
    <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q05655
    Secondary accession number(s): B0KZ81
    , B2R834, Q15144, Q86XJ6
    <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: September 2, 2008
    Last modified: June 2, 2021
    This is version 228 of the entry and version 2 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

    <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Reference proteome

    Documents

    1. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    2. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    3. Human entries with genetic variants
      List of human entries with genetic variants
    4. Human variants curated from literature reports
      Index of human variants curated from literature reports
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families
    UniProt is an ELIXIR core data resource
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