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Entry version 212 (08 May 2019)
Sequence version 3 (27 Mar 2002)
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Protein

Protein kinase C theta type

Gene

PRKCQ

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 mediates non-redundant functions in T-cell receptor (TCR) signaling, including T-cells activation, proliferation, differentiation and survival, by mediating activation of multiple transcription factors such as NF-kappa-B, JUN, NFATC1 and NFATC2. In TCR-CD3/CD28-co-stimulated T-cells, is required for the activation of NF-kappa-B and JUN, which in turn are essential for IL2 production, and participates in the calcium-dependent NFATC1 and NFATC2 transactivation. Mediates the activation of the canonical NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11 on several serine residues, inducing CARD11 association with lipid rafts and recruitment of the BCL10-MALT1 complex, which then activates IKK complex, resulting in nuclear translocation and activation of NFKB1. May also play an indirect role in activation of the non-canonical NF-kappa-B (NFKB2) pathway. In the signaling pathway leading to JUN activation, acts by phosphorylating the mediator STK39/SPAK and may not act through MAP kinases signaling. Plays a critical role in TCR/CD28-induced NFATC1 and NFATC2 transactivation by participating in the regulation of reduced inositol 1,4,5-trisphosphate generation and intracellular calcium mobilization. After costimulation of T-cells through CD28 can phosphorylate CBLB and is required for the ubiquitination and subsequent degradation of CBLB, which is a prerequisite for the activation of TCR. During T-cells differentiation, plays an important role in the development of T-helper 2 (Th2) cells following immune and inflammatory responses, and, in the development of inflammatory autoimmune diseases, is necessary for the activation of IL17-producing Th17 cells. May play a minor role in Th1 response. Upon TCR stimulation, mediates T-cell protective survival signal by phosphorylating BAD, thus protecting T-cells from BAD-induced apoptosis, and by up-regulating BCL-X(L)/BCL2L1 levels through NF-kappa-B and JUN pathways. In platelets, regulates signal transduction downstream of the ITGA2B, CD36/GP4, F2R/PAR1 and F2RL3/PAR4 receptors, playing a positive role in 'outside-in' signaling and granule secretion signal transduction. May relay signals from the activated ITGA2B receptor by regulating the uncoupling of WASP and WIPF1, thereby permitting the regulation of actin filament nucleation and branching activity of the Arp2/3 complex. May mediate inhibitory effects of free fatty acids on insulin signaling by phosphorylating IRS1, which in turn blocks IRS1 tyrosine phosphorylation and downstream activation of the PI3K/AKT pathway. Phosphorylates MSN (moesin) in the presence of phosphatidylglycerol or phosphatidylinositol. Phosphorylates PDPK1 at 'Ser-504' and 'Ser-532' and negatively regulates its ability to phosphorylate PKB/AKT1.8 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+

<p>This subsection of the ‘Function’ 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-538 (activation loop of the kinase domain), Ser-676 (turn motif) and Ser-695 (hydrophobic region), need to be phosphorylated for its full activation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei409ATP1
<p>This subsection of the ‘Function’ 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 sitei504Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 fingeri159 – 209Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri231 – 281Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd BLAST51
<p>This subsection of the ‘Function’ 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 bindingi386 – 394ATPPROSITE-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 processImmunity, Inflammatory response
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.11.13 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-111465 Apoptotic cleavage of cellular proteins
R-HSA-114508 Effects of PIP2 hydrolysis
R-HSA-202424 Downstream TCR signaling
R-HSA-2514859 Inactivation, recovery and regulation of the phototransduction cascade
R-HSA-2871837 FCERI mediated NF-kB activation
R-HSA-373752 Netrin-1 signaling
R-HSA-418597 G alpha (z) signalling events
R-HSA-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q04759

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

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SignaLinki
Q04759

SIGNOR Signaling Network Open Resource

More...
SIGNORi
Q04759

<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_and_taxonomy_section">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 theta type (EC:2.7.11.13)
Alternative name(s):
nPKC-theta
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:PRKCQ
Synonyms:PRKCT
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_manual">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 10

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:9410 PRKCQ

Online Mendelian Inheritance in Man (OMIM)

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MIMi
600448 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q04759

<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

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

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

<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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi90Y → F: Loss of function in T-cells proliferation. No effect on kinase activity. 1 Publication1
Mutagenesisi148A → E: Constitutively active form. 1 Publication1
Mutagenesisi219T → A: Loss of transactivation of the IL2 promoter and translocation to the plasma membrane. No effect on kinase activity. 1 Publication1
Mutagenesisi409K → A or E: Loss of kinase activity. 1 Publication1
Mutagenesisi538T → A: Loss of kinase activity. 2 Publications1
Mutagenesisi676S → A: Reduction in kinase activity. 1 Publication1
Mutagenesisi695S → A: Reduction in kinase activity. 2 Publications1

Organism-specific databases

DisGeNET

More...
DisGeNETi
5588

Open Targets

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OpenTargetsi
ENSG00000065675

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA33773

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL3920

Drug and drug target database

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DrugBanki
DB04522 Phosphonoserine
DB02482 Phosphonothreonine
DB02010 Staurosporine
DB00675 Tamoxifen

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
1488

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
PRKCQ

Domain mapping of disease mutations (DMDM)

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DMDMi
20141582

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000557081 – 706Protein kinase C theta typeAdd BLAST706

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 residuei90Phosphotyrosine; by LCK1 Publication1
Modified residuei219Phosphothreonine; by autocatalysis1 Publication1
Modified residuei348PhosphoserineCombined sources1
Modified residuei538Phosphothreonine; by PDPK13 Publications1
Modified residuei676PhosphoserineCombined sources3 Publications1
Modified residuei685PhosphoserineCombined sources1
Modified residuei695PhosphoserineCombined sources4 Publications1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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

Autophosphorylation at Thr-219 is required for targeting to the TCR and cellular function of PRKCQ upon antigen receptor ligation. Following TCR stimulation, phosphorylated at Tyr-90 and Ser-685.5 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q04759

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q04759

MaxQB - The MaxQuant DataBase

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MaxQBi
Q04759

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

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PaxDbi
Q04759

PeptideAtlas

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PeptideAtlasi
Q04759

PRoteomics IDEntifications database

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PRIDEi
Q04759

ProteomicsDB human proteome resource

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ProteomicsDBi
58279
58280 [Q04759-2]

PTM databases

CarbonylDB database of protein carbonylation sites

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CarbonylDBi
Q04759

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q04759

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

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PhosphoSitePlusi
Q04759

Miscellaneous databases

CutDB - Proteolytic event database

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PMAP-CutDBi
Q04759

<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

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in skeletal muscle, T-cells, megakaryoblastic cells and platelets.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000065675 Expressed in 173 organ(s), highest expression level in vastus lateralis

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q04759 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q04759 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA065279
HPA073098

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with GLRX3 (via N-terminus). Interacts with ECT2. Part of a lipid raft complex composed at least of BCL10, CARD11, MALT1 and IKBKB.3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
111574, 30 interactors

Protein interaction database and analysis system

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IntActi
Q04759, 19 interactors

Molecular INTeraction database

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MINTi
Q04759

STRING: functional protein association networks

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STRINGi
9606.ENSP00000263125

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
Q04759

<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

1706
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XJDX-ray2.00A362-706[»]
2ENJNMR-A1-125[»]
2ENNNMR-A144-213[»]
2ENZNMR-A227-284[»]
2JEDX-ray2.32A/B361-706[»]
4Q9ZX-ray2.60A/B374-706[»]
4RA5X-ray2.61A/B374-706[»]
5F9EX-ray2.00A/B361-706[»]

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

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SMRi
Q04759

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q04759

<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_and_domains_section">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>Domaini8 – 123C2Add BLAST116
Domaini380 – 634Protein kinasePROSITE-ProRule annotationAdd BLAST255
Domaini635 – 706AGC-kinase C-terminalAdd 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 and the C2 domain is a non-calcium binding domain.

<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 fingeri159 – 209Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri231 – 281Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd BLAST51

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0694 Eukaryota
ENOG410XNPH LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000157638

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000233022

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q04759

KEGG Orthology (KO)

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KOi
K18052

Identification of Orthologs from Complete Genome Data

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OMAi
HMKLKIE

Database of Orthologous Groups

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OrthoDBi
700058at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q04759

TreeFam database of animal gene trees

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TreeFami
TF102004

Family and domain databases

Conserved Domains Database

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CDDi
cd00029 C1, 2 hits
cd05619 STKc_nPKC_theta, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.60.40.150, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR000961 AGC-kinase_C
IPR035892 C2_domain_sf
IPR020454 DAG/PE-bd
IPR011009 Kinase-like_dom_sf
IPR034668 nPKC_theta
IPR002219 PE/DAG-bd
IPR027264 PKC_theta
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

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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

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PIRSFi
PIRSF000551 PKC_delta, 1 hit
PIRSF501105 Protein_kin_C_theta, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00008 DAGPEDOMAIN

Simple Modular Architecture Research Tool; a protein domain database

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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

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SUPFAMi
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View 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

<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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

This entry describes 3 <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 3 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: Q04759-1) [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
MSPFLRIGLS NFDCGSCQSC QGEAVNPYCA VLVKEYVESE NGQMYIQKKP
60 70 80 90 100
TMYPPWDSTF DAHINKGRVM QIIVKGKNVD LISETTVELY SLAERCRKNN
110 120 130 140 150
GKTEIWLELK PQGRMLMNAR YFLEMSDTKD MNEFETEGFF ALHQRRGAIK
160 170 180 190 200
QAKVHHVKCH EFTATFFPQP TFCSVCHEFV WGLNKQGYQC RQCNAAIHKK
210 220 230 240 250
CIDKVIAKCT GSAINSRETM FHKERFKIDM PHRFKVYNYK SPTFCEHCGT
260 270 280 290 300
LLWGLARQGL KCDACGMNVH HRCQTKVANL CGINQKLMAE ALAMIESTQQ
310 320 330 340 350
ARCLRDTEQI FREGPVEIGL PCSIKNEARP PCLPTPGKRE PQGISWESPL
360 370 380 390 400
DEVDKMCHLP EPELNKERPS LQIKLKIEDF ILHKMLGKGS FGKVFLAEFK
410 420 430 440 450
KTNQFFAIKA LKKDVVLMDD DVECTMVEKR VLSLAWEHPF LTHMFCTFQT
460 470 480 490 500
KENLFFVMEY LNGGDLMYHI QSCHKFDLSR ATFYAAEIIL GLQFLHSKGI
510 520 530 540 550
VYRDLKLDNI LLDKDGHIKI ADFGMCKENM LGDAKTNTFC GTPDYIAPEI
560 570 580 590 600
LLGQKYNHSV DWWSFGVLLY EMLIGQSPFH GQDEEELFHS IRMDNPFYPR
610 620 630 640 650
WLEKEAKDLL VKLFVREPEK RLGVRGDIRQ HPLFREINWE ELERKEIDPP
660 670 680 690 700
FRPKVKSPFD CSNFDKEFLN EKPRLSFADR ALINSMDQNM FRNFSFMNPG

MERLIS
Length:706
Mass (Da):81,865
Last modified:March 27, 2002 - v3
<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:iB3C53AB892D5210A
GO
Isoform 2 (identifier: Q04759-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     550-612: Missing.

Show »
Length:643
Mass (Da):74,287
Checksum:iA3B688EBE8809B9E
GO
Isoform 3 (identifier: Q04759-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     2-126: Missing.

Note: No experimental confirmation available.
Show »
Length:581
Mass (Da):67,560
Checksum:iABB524BD5B3E2898
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A087X0I9A0A087X0I9_HUMAN
Protein kinase C
PRKCQ
670Annotation score:

Annotation score:3 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 conflicti700G → R in AAA75571 (PubMed:7686153).Curated1
Sequence conflicti700G → R in AAU29340 (Ref. 4) 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_042319240K → N in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_042320306D → V1 PublicationCorresponds to variant dbSNP:rs45590231Ensembl.1
Natural variantiVAR_020401330P → L3 PublicationsCorresponds to variant dbSNP:rs2236379Ensembl.1
Natural variantiVAR_042321354D → N1 PublicationCorresponds to variant dbSNP:rs34524148Ensembl.1

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_0545502 – 126Missing in isoform 3. 1 PublicationAdd BLAST125
Alternative sequenceiVSP_017294550 – 612Missing in isoform 2. 1 PublicationAdd BLAST63

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
L01087 mRNA Translation: AAA75571.1
L07032 mRNA Translation: AAA60101.1
AY702977 mRNA Translation: AAU29340.1
AK293935 mRNA Translation: BAG57313.1
AL158043 Genomic DNA No translation available.
AL137145 Genomic DNA No translation available.
BC101465 mRNA Translation: AAI01466.1
BC113359 mRNA Translation: AAI13360.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS55701.1 [Q04759-2]
CCDS60482.1 [Q04759-3]
CCDS7079.1 [Q04759-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
A45416

NCBI Reference Sequences

More...
RefSeqi
NP_001229342.1, NM_001242413.2 [Q04759-2]
NP_001269573.1, NM_001282644.1
NP_001269574.1, NM_001282645.1 [Q04759-3]
NP_001310194.1, NM_001323265.1 [Q04759-1]
NP_001310195.1, NM_001323266.1 [Q04759-3]
NP_006248.1, NM_006257.4 [Q04759-1]
XP_006717528.1, XM_006717465.3
XP_016871899.1, XM_017016410.1
XP_016871900.1, XM_017016411.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000263125; ENSP00000263125; ENSG00000065675 [Q04759-1]
ENST00000397176; ENSP00000380361; ENSG00000065675 [Q04759-2]
ENST00000539722; ENSP00000441752; ENSG00000065675 [Q04759-3]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
5588

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:5588

UCSC genome browser

More...
UCSCi
uc001ijj.3 human [Q04759-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L01087 mRNA Translation: AAA75571.1
L07032 mRNA Translation: AAA60101.1
AY702977 mRNA Translation: AAU29340.1
AK293935 mRNA Translation: BAG57313.1
AL158043 Genomic DNA No translation available.
AL137145 Genomic DNA No translation available.
BC101465 mRNA Translation: AAI01466.1
BC113359 mRNA Translation: AAI13360.1
CCDSiCCDS55701.1 [Q04759-2]
CCDS60482.1 [Q04759-3]
CCDS7079.1 [Q04759-1]
PIRiA45416
RefSeqiNP_001229342.1, NM_001242413.2 [Q04759-2]
NP_001269573.1, NM_001282644.1
NP_001269574.1, NM_001282645.1 [Q04759-3]
NP_001310194.1, NM_001323265.1 [Q04759-1]
NP_001310195.1, NM_001323266.1 [Q04759-3]
NP_006248.1, NM_006257.4 [Q04759-1]
XP_006717528.1, XM_006717465.3
XP_016871899.1, XM_017016410.1
XP_016871900.1, XM_017016411.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XJDX-ray2.00A362-706[»]
2ENJNMR-A1-125[»]
2ENNNMR-A144-213[»]
2ENZNMR-A227-284[»]
2JEDX-ray2.32A/B361-706[»]
4Q9ZX-ray2.60A/B374-706[»]
4RA5X-ray2.61A/B374-706[»]
5F9EX-ray2.00A/B361-706[»]
SMRiQ04759
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111574, 30 interactors
IntActiQ04759, 19 interactors
MINTiQ04759
STRINGi9606.ENSP00000263125

Chemistry databases

BindingDBiQ04759
ChEMBLiCHEMBL3920
DrugBankiDB04522 Phosphonoserine
DB02482 Phosphonothreonine
DB02010 Staurosporine
DB00675 Tamoxifen
GuidetoPHARMACOLOGYi1488

PTM databases

CarbonylDBiQ04759
iPTMnetiQ04759
PhosphoSitePlusiQ04759

Polymorphism and mutation databases

BioMutaiPRKCQ
DMDMi20141582

Proteomic databases

EPDiQ04759
jPOSTiQ04759
MaxQBiQ04759
PaxDbiQ04759
PeptideAtlasiQ04759
PRIDEiQ04759
ProteomicsDBi58279
58280 [Q04759-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
5588
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263125; ENSP00000263125; ENSG00000065675 [Q04759-1]
ENST00000397176; ENSP00000380361; ENSG00000065675 [Q04759-2]
ENST00000539722; ENSP00000441752; ENSG00000065675 [Q04759-3]
GeneIDi5588
KEGGihsa:5588
UCSCiuc001ijj.3 human [Q04759-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5588
DisGeNETi5588

GeneCards: human genes, protein and diseases

More...
GeneCardsi
PRKCQ
HGNCiHGNC:9410 PRKCQ
HPAiHPA065279
HPA073098
MIMi600448 gene
neXtProtiNX_Q04759
OpenTargetsiENSG00000065675
PharmGKBiPA33773

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0694 Eukaryota
ENOG410XNPH LUCA
GeneTreeiENSGT00940000157638
HOGENOMiHOG000233022
InParanoidiQ04759
KOiK18052
OMAiHMKLKIE
OrthoDBi700058at2759
PhylomeDBiQ04759
TreeFamiTF102004

Enzyme and pathway databases

BRENDAi2.7.11.13 2681
ReactomeiR-HSA-111465 Apoptotic cleavage of cellular proteins
R-HSA-114508 Effects of PIP2 hydrolysis
R-HSA-202424 Downstream TCR signaling
R-HSA-2514859 Inactivation, recovery and regulation of the phototransduction cascade
R-HSA-2871837 FCERI mediated NF-kB activation
R-HSA-373752 Netrin-1 signaling
R-HSA-418597 G alpha (z) signalling events
R-HSA-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function
SABIO-RKiQ04759
SignaLinkiQ04759
SIGNORiQ04759

Miscellaneous databases

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

More...
ChiTaRSi
PRKCQ human
EvolutionaryTraceiQ04759

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
PRKCQ

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

More...
GenomeRNAii
5588
PMAP-CutDBiQ04759

Protein Ontology

More...
PROi
PR:Q04759

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000065675 Expressed in 173 organ(s), highest expression level in vastus lateralis
ExpressionAtlasiQ04759 baseline and differential
GenevisibleiQ04759 HS

Family and domain databases

CDDicd00029 C1, 2 hits
cd05619 STKc_nPKC_theta, 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
IPR034668 nPKC_theta
IPR002219 PE/DAG-bd
IPR027264 PKC_theta
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
PIRSF501105 Protein_kin_C_theta, 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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<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 nameiKPCT_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: Q04759
Secondary accession number(s): B4DF52
, Q14DH6, Q3MJF1, Q64FY5, Q9H508, Q9H549
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: March 27, 2002
Last modified: May 8, 2019
This is version 212 of the entry and version 3 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, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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