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Entry version 220 (16 Oct 2019)
Sequence version 1 (01 Jan 1998)
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Protein

3-phosphoinositide-dependent protein kinase 1

Gene

PDPK1

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

Serine/threonine kinase which acts as a master kinase, phosphorylating and activating a subgroup of the AGC family of protein kinases. Its targets include: protein kinase B (PKB/AKT1, PKB/AKT2, PKB/AKT3), p70 ribosomal protein S6 kinase (RPS6KB1), p90 ribosomal protein S6 kinase (RPS6KA1, RPS6KA2 and RPS6KA3), cyclic AMP-dependent protein kinase (PRKACA), protein kinase C (PRKCD and PRKCZ), serum and glucocorticoid-inducible kinase (SGK1, SGK2 and SGK3), p21-activated kinase-1 (PAK1), protein kinase PKN (PKN1 and PKN2). Plays a central role in the transduction of signals from insulin by providing the activating phosphorylation to PKB/AKT1, thus propagating the signal to downstream targets controlling cell proliferation and survival, as well as glucose and amino acid uptake and storage. Negatively regulates the TGF-beta-induced signaling by: modulating the association of SMAD3 and SMAD7 with TGF-beta receptor, phosphorylating SMAD2, SMAD3, SMAD4 and SMAD7, preventing the nuclear translocation of SMAD3 and SMAD4 and the translocation of SMAD7 from the nucleus to the cytoplasm in response to TGF-beta. Activates PPARG transcriptional activity and promotes adipocyte differentiation. Activates the NF-kappa-B pathway via phosphorylation of IKKB. The tyrosine phosphorylated form is crucial for the regulation of focal adhesions by angiotensin II. Controls proliferation, survival, and growth of developing pancreatic cells. Participates in the regulation of Ca2+ entry and Ca2+-activated K+ channels of mast cells. Essential for the motility of vascular endothelial cells (ECs) and is involved in the regulation of their chemotaxis. Plays a critical role in cardiac homeostasis by serving as a dual effector for cell survival and beta-adrenergic response. Plays an important role during thymocyte development by regulating the expression of key nutrient receptors on the surface of pre-T cells and mediating Notch-induced cell growth and proliferative responses. Provides negative feedback inhibition to toll-like receptor-mediated NF-kappa-B activation in macrophages. Isoform 3 is catalytically inactive.15 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 <a href="http://www.uniprot.org/help/function_section">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

Homodimerization regulates its activity by maintaining the kinase in an autoinhibitory conformation. NPRL2 down-regulates its activity by interfering with tyrosine phosphorylation at the Tyr-9, Tyr-373 and Tyr-376 residues. The 14-3-3 protein YWHAQ acts as a negative regulator by association with the residues surrounding the Ser-241 residue. STRAP positively regulates its activity by enhancing its autophosphorylation and by stimulating its dissociation from YWHAQ. SMAD2, SMAD3, SMAD4 and SMAD7 also positively regulate its activity by stimulating its dissociation from YWHAQ. Activated by phosphorylation on Tyr-9, Tyr-373 and Tyr-376 by INSR in response to insulin.4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei111ATP3 Publications1
Binding sitei166ATP3 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei205Proton acceptorPROSITE-ProRule annotation1
Binding sitei209ATP; via carbonyl oxygen1 Publication1
Binding sitei223ATP3 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi92 – 94ATP3 Publications3
Nucleotide bindingi160 – 162ATP3 Publications3

<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 functionActivator, Kinase, Serine/threonine-protein kinase, Transferase
Biological processTranscription, Transcription regulation
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
2.7.11.1 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-114604 GPVI-mediated activation cascade
R-HSA-1257604 PIP3 activates AKT signaling
R-HSA-165158 Activation of AKT2
R-HSA-202424 Downstream TCR signaling
R-HSA-2730905 Role of LAT2/NTAL/LAB on calcium mobilization
R-HSA-2871837 FCERI mediated NF-kB activation
R-HSA-354192 Integrin alphaIIb beta3 signaling
R-HSA-389357 CD28 dependent PI3K/Akt signaling
R-HSA-392451 G beta:gamma signalling through PI3Kgamma
R-HSA-444257 RSK activation
R-HSA-5218920 VEGFR2 mediated vascular permeability
R-HSA-5218921 VEGFR2 mediated cell proliferation
R-HSA-5607764 CLEC7A (Dectin-1) signaling
R-HSA-5625740 RHO GTPases activate PKNs
R-HSA-5674400 Constitutive Signaling by AKT1 E17K in Cancer
R-HSA-6804757 Regulation of TP53 Degradation
R-HSA-9634635 Estrogen-stimulated signaling through PRKCZ

SABIO-RK: Biochemical Reaction Kinetics Database

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SABIO-RKi
O15530

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

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SignaLinki
O15530

SIGNOR Signaling Network Open Resource

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SIGNORi
O15530

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

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MoonDBi
O15530 Predicted

<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:
3-phosphoinositide-dependent protein kinase 1 (EC:2.7.11.1)
Short name:
hPDK1
<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:PDPK1
Synonyms:PDK1
<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 16

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:8816 PDPK1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
605213 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_O15530

<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 junction, Cell membrane, Cytoplasm, Membrane, 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

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>Mutagenesisi9Y → F: Slight reduction in pervanadate-stimulated tyrosine phosphorylation. 1 Publication1
Mutagenesisi25S → A: No effect. 1 Publication1
Mutagenesisi241S → A: No activation. 1 Publication1
Mutagenesisi277A → V: 3-fold increase in kinase activity. 1 Publication1
Mutagenesisi354T → A: Abolishes phosphorylation by MELK. 1 Publication1
Mutagenesisi373Y → F: Reduction in basal activity. 1 Publication1
Mutagenesisi376Y → F: Reduction in basal activity. 1 Publication1
Mutagenesisi393S → A: No effect. 1 Publication1
Mutagenesisi394S → A: Abolishes phosphorylation by MAP3K5; when associated with A-398. 1 Publication1
Mutagenesisi396S → A: No effect. 1 Publication1
Mutagenesisi398S → A: Abolishes phosphorylation by MAP3K5; when associated with A-394. 1 Publication1
Mutagenesisi410S → A: No effect. 1 Publication1
Mutagenesisi474R → A: No PDGF-dependent translocation to the membrane. 1 Publication1
Mutagenesisi513T → E: Enhanced kinase activity towards PKB. 1 Publication1

Organism-specific databases

DisGeNET

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DisGeNETi
5170

Open Targets

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OpenTargetsi
ENSG00000140992

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA33160

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
O15530

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL2534

Drug and drug target database

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DrugBanki
DB07132 1-{2-OXO-3-[(1R)-1-(1H-PYRROL-2-YL)ETHYL]-2H-INDOL-5-YL}UREA
DB06932 10,11-dimethoxy-4-methyldibenzo[c,f]-2,7-naphthyridine-3,6-diamine
DB07300 2-(1H-imidazol-1-yl)-9-methoxy-8-(2-methoxyethoxy)benzo[c][2,7]naphthyridin-4-amine
DB07456 3-(1H-indol-3-yl)-4-(1-{2-[(2S)-1-methylpyrrolidinyl]ethyl}-1H-indol-3-yl)-1H-pyrrole-2,5-dione
DB01946 3-[1-(3-Aminopropyl)-1h-Indol-3-Yl]-4-(1-Methyl-1h-Indol-3-Yl)-1h-Pyrrole-2,5-Dione
DB07457 3-[1-(3-AMINOPROPYL)-1H-INDOL-3-YL]-4-(1H-INDOL-3-YL)-1H-PYRROLE-2,5-DIONE
DB07033 5-HYDROXY-3-[(1R)-1-(1H-PYRROL-2-YL)ETHYL]-2H-INDOL-2-ONE
DB01933 7-Hydroxystaurosporine
DB00482 Celecoxib
DB04522 Dexfosfoserine
DB12010 Fostamatinib
DB01863 Inositol 1,3,4,5-Tetrakisphosphate
DB03777 Rbt205 Inhibitor
DB02010 Staurosporine

DrugCentral

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DrugCentrali
O15530

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
1519

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
PDPK1

<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_00000865001 – 5563-phosphoinositide-dependent protein kinase 1Add BLAST556

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 residuei9Phosphotyrosine; by SRC and INSR3 Publications1
Modified residuei25Phosphoserine1 Publication1
Modified residuei241Phosphoserine; by autocatalysis5 Publications1
Modified residuei304N6-acetyllysineBy similarity1
Modified residuei354Phosphothreonine; by MELK1 Publication1
Modified residuei373Phosphotyrosine; by SRC and INSR3 Publications1
Modified residuei376Phosphotyrosine; by SRC and INSR3 Publications1
Modified residuei393Phosphoserine1 Publication1
Modified residuei394Phosphoserine; by MAP3K51 Publication1
Modified residuei396Phosphoserine2 Publications1
Modified residuei398Phosphoserine; by MAP3K51 Publication1
Modified residuei410Phosphoserine1 Publication1
Modified residuei501Phosphoserine; by PKC/PRKCQBy similarity1
Modified residuei513Phosphothreonine; by autocatalysis1 Publication1
Modified residuei529Phosphoserine; by PKC/PRKCQBy similarity1

<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

Phosphorylation on Ser-241 in the activation loop is required for full activity. PDPK1 itself can autophosphorylate Ser-241, leading to its own activation. Autophosphorylation is inhibited by the apoptotic C-terminus cleavage product of PKN2 (By similarity). Tyr-9 phosphorylation is critical for stabilization of both PDPK1 and the PDPK1/SRC complex via HSP90-mediated protection of PDPK1 degradation. Angiotensin II stimulates the tyrosine phosphorylation of PDPK1 in vascular smooth muscle in a calcium- and SRC-dependent manner. Phosphorylated on Tyr-9, Tyr-373 and Tyr-376 by INSR in response to insulin. Palmitate negatively regulates autophosphorylation at Ser-241 and palmitate-induced phosphorylation at Ser-529 and Ser-501 by PKC/PRKCQ negatively regulates its ability to phosphorylate PKB/AKT1. Phosphorylation at Thr-354 by MELK partially inhibits kinase activity, the inhibition is cooperatively enhanced by phosphorylation at Ser-394 and Ser-398 by MAP3K5.By similarity8 Publications
Autophosphorylated; autophosphorylation is inhibited by the apoptotic C-terminus cleavage product of PKN2.By similarity
Monoubiquitinated in the kinase domain, deubiquitinated by USP4.

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

The CPTAC Assay portal

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CPTACi
CPTAC-1052

Encyclopedia of Proteome Dynamics

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EPDi
O15530

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
O15530

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
O15530

MaxQB - The MaxQuant DataBase

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MaxQBi
O15530

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

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PaxDbi
O15530

PeptideAtlas

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PeptideAtlasi
O15530

PRoteomics IDEntifications database

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PRIDEi
O15530

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
34858
48736 [O15530-1]
48737 [O15530-2]
48738 [O15530-3]
48739 [O15530-4]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
O15530

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

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PhosphoSitePlusi
O15530

<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

Appears to be expressed ubiquitously. The Tyr-9 phosphorylated form is markedly increased in diseased tissue compared with normal tissue from lung, liver, colon and breast.1 Publication

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Stimulated by insulin, and the oxidants hydrogen peroxide and peroxovanadate.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000140992 Expressed in 226 organ(s), highest expression level in secondary oocyte

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
O15530 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O15530 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB004272
HPA035199
HPA068961

<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

Homodimer in its autoinhibited state. Active as monomer.

Interacts with NPRL2, PPARG, PAK1, PTK2B, GRB14, PKN1 (via C-terminus), STRAP and IKKB. The Tyr-9 phosphorylated form interacts with SRC, RASA1 and CRK (via their SH2 domains).

Interacts with SGK3 in a phosphorylation-dependent manner. The tyrosine-phosphorylated form interacts with PTPN6. The Ser-241 phosphorylated form interacts with YWHAH and YWHAQ. Binds INSR in response to insulin.

Interacts (via PH domain) with SMAD3, SMAD4 and SMAD7.

Interacts with PKN2; the interaction stimulates PDPK1 autophosphorylation, its PI(3,4,5)P3-dependent kinase activity toward 'Ser-473' of AKT1 but also activates its kinase activity toward PRKCD and PRKCZ.

14 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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
111196, 62 interactors

Database of interacting proteins

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DIPi
DIP-38372N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
O15530

Protein interaction database and analysis system

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IntActi
O15530, 65 interactors

Molecular INTeraction database

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MINTi
O15530

STRING: functional protein association networks

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STRINGi
9606.ENSP00000344220

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
O15530

<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

1556
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

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SMRi
O15530

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
O15530

<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>Domaini82 – 342Protein kinasePROSITE-ProRule annotationAdd BLAST261
Domaini459 – 550PHAdd BLAST92

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni113 – 157PIF-pocket1 PublicationAdd BLAST45

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi389 – 398Poly-Ser10

<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 PH domain plays a pivotal role in the localization and nuclear import of PDPK1 and is also essential for its homodimerization.
The PIF-pocket is a small lobe in the catalytic domain required by the enzyme for the binding to the hydrophobic motif of its substrates. It is an allosteric regulatory site that can accommodate small compounds acting as allosteric inhibitors.1 Publication

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0592 Eukaryota
ENOG410XRT8 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000155267

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000233026

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O15530

KEGG Orthology (KO)

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KOi
K06276

Identification of Orthologs from Complete Genome Data

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OMAi
LEWCKAI

Database of Orthologous Groups

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OrthoDBi
1157543at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
O15530

TreeFam database of animal gene trees

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TreeFami
TF105423

Family and domain databases

Conserved Domains Database

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CDDi
cd01262 PH_PDK1, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.30.29.30, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR033931 PDK1-typ_PH
IPR039046 PDPK1
IPR011993 PH-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS

The PANTHER Classification System

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PANTHERi
PTHR24356:SF163 PTHR24356:SF163, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF14593 PH_3, 1 hit
PF00069 Pkinase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
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

More...
PROSITEi
View protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

<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>. 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 (5+)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 5 <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 5 described isoforms and 6 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: O15530-1) [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
MARTTSQLYD AVPIQSSVVL CSCPSPSMVR TQTESSTPPG IPGGSRQGPA
60 70 80 90 100
MDGTAAEPRP GAGSLQHAQP PPQPRKKRPE DFKFGKILGE GSFSTVVLAR
110 120 130 140 150
ELATSREYAI KILEKRHIIK ENKVPYVTRE RDVMSRLDHP FFVKLYFTFQ
160 170 180 190 200
DDEKLYFGLS YAKNGELLKY IRKIGSFDET CTRFYTAEIV SALEYLHGKG
210 220 230 240 250
IIHRDLKPEN ILLNEDMHIQ ITDFGTAKVL SPESKQARAN SFVGTAQYVS
260 270 280 290 300
PELLTEKSAC KSSDLWALGC IIYQLVAGLP PFRAGNEYLI FQKIIKLEYD
310 320 330 340 350
FPEKFFPKAR DLVEKLLVLD ATKRLGCEEM EGYGPLKAHP FFESVTWENL
360 370 380 390 400
HQQTPPKLTA YLPAMSEDDE DCYGNYDNLL SQFGCMQVSS SSSSHSLSAS
410 420 430 440 450
DTGLPQRSGS NIEQYIHDLD SNSFELDLQF SEDEKRLLLE KQAGGNPWHQ
460 470 480 490 500
FVENNLILKM GPVDKRKGLF ARRRQLLLTE GPHLYYVDPV NKVLKGEIPW
510 520 530 540 550
SQELRPEAKN FKTFFVHTPN RTYYLMDPSG NAHKWCRKIQ EVWRQRYQSH

PDAAVQ
Length:556
Mass (Da):63,152
Last modified:January 1, 1998 - v1
<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:iED8C0306DC4D0653
GO
Isoform 2 (identifier: O15530-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-50: Missing.

Show »
Length:506
Mass (Da):58,035
Checksum:i22D376B8A13FD3F3
GO
Isoform 3 (identifier: O15530-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     238-263: Missing.

Show »
Length:530
Mass (Da):60,396
Checksum:iCEAF882CBD3EB1F2
GO
Isoform 4 (identifier: O15530-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     110-237: IKILEKRHII...KVLSPESKQA → T

Show »
Length:429
Mass (Da):48,201
Checksum:i860C8A8C06161CE1
GO
Isoform 5 (identifier: O15530-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     448-556: WHQFVENNLI...YQSHPDAAVQ → CLTGRII

Note: No experimental confirmation available.
Show »
Length:454
Mass (Da):50,838
Checksum:i8D812DCC8CED2998
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
E9PER6E9PER6_HUMAN
3-phosphoinositide-dependent protei...
PDPK1
529Annotation 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>
H3BQ10H3BQ10_HUMAN
3-phosphoinositide-dependent protei...
PDPK1
149Annotation 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>
H3BPW1H3BPW1_HUMAN
3-phosphoinositide-dependent protei...
PDPK1
88Annotation 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>
H3BNV5H3BNV5_HUMAN
3-phosphoinositide-dependent protei...
PDPK1
35Annotation 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>
H3BPR5H3BPR5_HUMAN
3-phosphoinositide-dependent protei...
PDPK1
40Annotation 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>
H3BQA3H3BQA3_HUMAN
3-phosphoinositide-dependent protei...
PDPK1
55Annotation 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>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence BAD93072 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

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_0048941 – 50Missing in isoform 2. CuratedAdd BLAST50
Alternative sequenceiVSP_041902110 – 237IKILE…ESKQA → T in isoform 4. 1 PublicationAdd BLAST128
Alternative sequenceiVSP_004895238 – 263Missing in isoform 3. 1 PublicationAdd BLAST26
Alternative sequenceiVSP_044796448 – 556WHQFV…DAAVQ → CLTGRII in isoform 5. 1 PublicationAdd BLAST109

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF017995 mRNA Translation: AAC51825.1
Y15056 mRNA Translation: CAA75341.1
CR536517 mRNA Translation: CAG38755.1
AB209835 mRNA Translation: BAD93072.1 Different initiation.
AC093525 Genomic DNA No translation available.
AC141586 Genomic DNA No translation available.
BC006339 mRNA Translation: AAH06339.2
BC012103 mRNA Translation: AAH12103.1
BC033494 mRNA Translation: AAH33494.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS10472.1 [O15530-1]
CCDS10473.1 [O15530-4]
CCDS58411.1 [O15530-5]

NCBI Reference Sequences

More...
RefSeqi
NP_001248745.1, NM_001261816.1 [O15530-5]
NP_002604.1, NM_002613.4 [O15530-1]
NP_112558.2, NM_031268.5 [O15530-4]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000268673; ENSP00000268673; ENSG00000140992 [O15530-4]
ENST00000342085; ENSP00000344220; ENSG00000140992 [O15530-1]
ENST00000441549; ENSP00000395357; ENSG00000140992 [O15530-5]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
5170

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:5170

UCSC genome browser

More...
UCSCi
uc002cqs.5 human [O15530-1]

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF017995 mRNA Translation: AAC51825.1
Y15056 mRNA Translation: CAA75341.1
CR536517 mRNA Translation: CAG38755.1
AB209835 mRNA Translation: BAD93072.1 Different initiation.
AC093525 Genomic DNA No translation available.
AC141586 Genomic DNA No translation available.
BC006339 mRNA Translation: AAH06339.2
BC012103 mRNA Translation: AAH12103.1
BC033494 mRNA Translation: AAH33494.1
CCDSiCCDS10472.1 [O15530-1]
CCDS10473.1 [O15530-4]
CCDS58411.1 [O15530-5]
RefSeqiNP_001248745.1, NM_001261816.1 [O15530-5]
NP_002604.1, NM_002613.4 [O15530-1]
NP_112558.2, NM_031268.5 [O15530-4]

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
1H1WX-ray2.00A71-359[»]
1OKYX-ray2.30A51-360[»]
1OKZX-ray2.51A51-360[»]
1UU3X-ray1.70A51-360[»]
1UU7X-ray1.90A51-360[»]
1UU8X-ray2.50A51-360[»]
1UU9X-ray1.95A72-357[»]
1UVRX-ray2.81A71-359[»]
1W1DX-ray1.50A409-556[»]
1W1GX-ray1.45A409-556[»]
1W1HX-ray1.45A/B/C/D409-556[»]
1Z5MX-ray2.17A74-359[»]
2BIYX-ray1.95A51-360[»]
2PE0X-ray2.35A74-359[»]
2PE1X-ray2.14A74-359[»]
2PE2X-ray2.13A74-359[»]
2R7BX-ray2.70A48-359[»]
2VKIX-ray1.80A409-556[»]
2XCHX-ray2.00A51-359[»]
2XCKX-ray2.30A51-359[»]
3H9OX-ray2.30A51-359[»]
3HRCX-ray1.91A50-359[»]
3HRFX-ray1.90A50-359[»]
3IONX-ray2.40A48-359[»]
3IOPX-ray2.20A48-359[»]
3NAXX-ray1.75A66-362[»]
3NAYX-ray2.60A/B66-362[»]
3NUNX-ray2.20A67-358[»]
3NUSX-ray2.75A73-358[»]
3NUUX-ray1.98A73-358[»]
3NUYX-ray2.10A73-358[»]
3ORXX-ray2.20A/B/C/D/E/F/G/H51-359[»]
3ORZX-ray2.00A/B/C/D51-359[»]
3OTUX-ray2.10A51-359[»]
3PWYX-ray3.50A51-359[»]
3QC4X-ray1.80A/B51-359[»]
3QCQX-ray2.50A48-359[»]
3QCSX-ray2.49A48-359[»]
3QCXX-ray2.30A48-359[»]
3QCYX-ray2.20A48-359[»]
3QD0X-ray1.99A48-359[»]
3QD3X-ray2.00A48-359[»]
3QD4X-ray2.30A48-359[»]
3RCJX-ray1.70A50-359[»]
3RWPX-ray1.92A51-359[»]
3RWQX-ray2.55A51-359[»]
3SC1X-ray2.70A50-359[»]
4A06X-ray2.00A50-359[»]
4A07X-ray1.85A50-359[»]
4AW0X-ray1.43A51-359[»]
4AW1X-ray1.68A51-359[»]
4CT1X-ray1.85A50-359[»]
4CT2X-ray1.25A50-359[»]
4RQKX-ray1.55A50-359[»]
4RQVX-ray1.50A50-359[»]
4RRVX-ray1.41A50-359[»]
4XX9X-ray1.40A50-359[»]
5ACKX-ray1.24A50-359[»]
5HKMX-ray2.10A51-359[»]
5HNGX-ray3.01A51-359[»]
5HO7X-ray3.00A51-359[»]
5HO8X-ray2.70A51-359[»]
5LVLX-ray1.40A50-359[»]
5LVMX-ray1.26A50-359[»]
5LVNX-ray1.38A50-359[»]
5LVOX-ray1.09A50-359[»]
5LVPX-ray2.50A/B/C/D50-359[»]
5MRDX-ray1.41A50-359[»]
SMRiO15530
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi111196, 62 interactors
DIPiDIP-38372N
ELMiO15530
IntActiO15530, 65 interactors
MINTiO15530
STRINGi9606.ENSP00000344220

Chemistry databases

BindingDBiO15530
ChEMBLiCHEMBL2534
DrugBankiDB07132 1-{2-OXO-3-[(1R)-1-(1H-PYRROL-2-YL)ETHYL]-2H-INDOL-5-YL}UREA
DB06932 10,11-dimethoxy-4-methyldibenzo[c,f]-2,7-naphthyridine-3,6-diamine
DB07300 2-(1H-imidazol-1-yl)-9-methoxy-8-(2-methoxyethoxy)benzo[c][2,7]naphthyridin-4-amine
DB07456 3-(1H-indol-3-yl)-4-(1-{2-[(2S)-1-methylpyrrolidinyl]ethyl}-1H-indol-3-yl)-1H-pyrrole-2,5-dione
DB01946 3-[1-(3-Aminopropyl)-1h-Indol-3-Yl]-4-(1-Methyl-1h-Indol-3-Yl)-1h-Pyrrole-2,5-Dione
DB07457 3-[1-(3-AMINOPROPYL)-1H-INDOL-3-YL]-4-(1H-INDOL-3-YL)-1H-PYRROLE-2,5-DIONE
DB07033 5-HYDROXY-3-[(1R)-1-(1H-PYRROL-2-YL)ETHYL]-2H-INDOL-2-ONE
DB01933 7-Hydroxystaurosporine
DB00482 Celecoxib
DB04522 Dexfosfoserine
DB12010 Fostamatinib
DB01863 Inositol 1,3,4,5-Tetrakisphosphate
DB03777 Rbt205 Inhibitor
DB02010 Staurosporine
DrugCentraliO15530
GuidetoPHARMACOLOGYi1519

Protein family/group databases

MoonDBiO15530 Predicted

PTM databases

iPTMnetiO15530
PhosphoSitePlusiO15530

Polymorphism and mutation databases

BioMutaiPDPK1

Proteomic databases

CPTACiCPTAC-1052
EPDiO15530
jPOSTiO15530
MassIVEiO15530
MaxQBiO15530
PaxDbiO15530
PeptideAtlasiO15530
PRIDEiO15530
ProteomicsDBi34858
48736 [O15530-1]
48737 [O15530-2]
48738 [O15530-3]
48739 [O15530-4]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
5170

Genome annotation databases

EnsembliENST00000268673; ENSP00000268673; ENSG00000140992 [O15530-4]
ENST00000342085; ENSP00000344220; ENSG00000140992 [O15530-1]
ENST00000441549; ENSP00000395357; ENSG00000140992 [O15530-5]
GeneIDi5170
KEGGihsa:5170
UCSCiuc002cqs.5 human [O15530-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5170
DisGeNETi5170

GeneCards: human genes, protein and diseases

More...
GeneCardsi
PDPK1
HGNCiHGNC:8816 PDPK1
HPAiCAB004272
HPA035199
HPA068961
MIMi605213 gene
neXtProtiNX_O15530
OpenTargetsiENSG00000140992
PharmGKBiPA33160

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0592 Eukaryota
ENOG410XRT8 LUCA
GeneTreeiENSGT00940000155267
HOGENOMiHOG000233026
InParanoidiO15530
KOiK06276
OMAiLEWCKAI
OrthoDBi1157543at2759
PhylomeDBiO15530
TreeFamiTF105423

Enzyme and pathway databases

BRENDAi2.7.11.1 2681
ReactomeiR-HSA-114604 GPVI-mediated activation cascade
R-HSA-1257604 PIP3 activates AKT signaling
R-HSA-165158 Activation of AKT2
R-HSA-202424 Downstream TCR signaling
R-HSA-2730905 Role of LAT2/NTAL/LAB on calcium mobilization
R-HSA-2871837 FCERI mediated NF-kB activation
R-HSA-354192 Integrin alphaIIb beta3 signaling
R-HSA-389357 CD28 dependent PI3K/Akt signaling
R-HSA-392451 G beta:gamma signalling through PI3Kgamma
R-HSA-444257 RSK activation
R-HSA-5218920 VEGFR2 mediated vascular permeability
R-HSA-5218921 VEGFR2 mediated cell proliferation
R-HSA-5607764 CLEC7A (Dectin-1) signaling
R-HSA-5625740 RHO GTPases activate PKNs
R-HSA-5674400 Constitutive Signaling by AKT1 E17K in Cancer
R-HSA-6804757 Regulation of TP53 Degradation
R-HSA-9634635 Estrogen-stimulated signaling through PRKCZ
SABIO-RKiO15530
SignaLinkiO15530
SIGNORiO15530

Miscellaneous databases

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

More...
ChiTaRSi
PDPK1 human
EvolutionaryTraceiO15530

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Phosphoinositide-dependent_kinase-1

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

More...
GenomeRNAii
5170
PharosiO15530

Protein Ontology

More...
PROi
PR:O15530

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000140992 Expressed in 226 organ(s), highest expression level in secondary oocyte
ExpressionAtlasiO15530 baseline and differential
GenevisibleiO15530 HS

Family and domain databases

CDDicd01262 PH_PDK1, 1 hit
Gene3Di2.30.29.30, 1 hit
InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR033931 PDK1-typ_PH
IPR039046 PDPK1
IPR011993 PH-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PANTHERiPTHR24356:SF163 PTHR24356:SF163, 1 hit
PfamiView protein in Pfam
PF14593 PH_3, 1 hit
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 nameiPDPK1_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: O15530
Secondary accession number(s): H0Y4Z0
, Q59EH6, Q6FI20, Q8IV52, Q9BRD5
<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 18, 2001
Last sequence update: January 1, 1998
Last modified: October 16, 2019
This is version 220 of the entry and version 1 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, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
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