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Protein

Death-associated protein kinase 3

Gene

DAPK3

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 is involved in the regulation of apoptosis, autophagy, transcription, translation and actin cytoskeleton reorganization. Involved in the regulation of smooth muscle contraction. Regulates both type I (caspase-dependent) apoptotic and type II (caspase-independent) autophagic cell deaths signal, depending on the cellular setting. Involved in regulation of starvation-induced autophagy. Regulates myosin phosphorylation in both smooth muscle and non-muscle cells. In smooth muscle, regulates myosin either directly by phosphorylating MYL12B and MYL9 or through inhibition of smooth muscle myosin phosphatase (SMPP1M) via phosphorylation of PPP1R12A; the inhibition of SMPP1M functions to enhance muscle responsiveness to Ca2+ and promote a contractile state. Phosphorylates MYL12B in non-muscle cells leading to reorganization of actin cytoskeleton. Isoform 2 can phosphorylate myosin, PPP1R12A and MYL12B. Overexpression leads to condensation of actin stress fibers into thick bundles. Involved in actin filament focal adhesion dynamics. The function in both reorganization of actin cytoskeleton and focal adhesion dissolution is modulated by RhoD. Positively regulates canonical Wnt/beta-catenin signaling through interaction with NLK and TCF7L2. Phosphorylates RPL13A on 'Ser-77' upon interferon-gamma activation which is causing RPL13A release from the ribosome, RPL13A association with the GAIT complex and its subsequent involvement in transcript-selective translation inhibition. Enhances transcription from AR-responsive promoters in a hormone- and kinase-dependent manner. Involved in regulation of cell cycle progression and cell proliferation. May be a tumor suppressor.16 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+1 Publication

<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

A sequential activation is proposed: autophosphorylation at consensus sites is leading to dimerization of the catalytic domain stabilized by phosphorylation at Ser-50 and activation segment exchange (producing an active confirmation of both kinase modules in trans) followed by phosphorylation at Thr-180 in the activation segment and at other regulatory sites (Probable). Phosphorylation at Thr-180, Thr-225 and Thr-265 is essential for activity. Oligomerization is required for full enzymatic activity. Inhibited by pyridone 6 (K00225), a potent, ATP-competitive inhibitor.1 Publication3 Publications

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

  1. KM=12 µM for myosin (isoform 2)1 Publication
  2. KM=6.2 µM for myosin (isoform 1)1 Publication
  3. KM=73 µM for MYL12B (isoform 2)1 Publication
  4. KM=10.4 µM for MYL12B (isoform 1)1 Publication
  1. Vmax=248 nmol/min/mg enzyme toward myosin (isoform 2)1 Publication
  2. Vmax=120 nmol/min/mg enzyme toward myosin (isoform 1)1 Publication
  3. Vmax=1.3 µmol/min/mg enzyme toward MYL12B (isoform 2)1 Publication
  4. Vmax=271 nmol/min/mg enzyme toward MYL12B (isoform 1)1 Publication

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 sitei42ATPCurated1
Binding sitei94Inhibitor1 Publication1
Binding sitei96Inhibitor1 Publication1
<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 sitei139Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bindingi19 – 27ATPPROSITE-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

  • ATP binding Source: UniProtKB
  • cAMP response element binding protein binding Source: ParkinsonsUK-UCL
  • identical protein binding Source: IntAct
  • leucine zipper domain binding Source: UniProtKB
  • protein C-terminus binding Source: Ensembl
  • protein homodimerization activity Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB
  • Rho GTPase binding Source: UniProtKB

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, Chromatin regulator, Kinase, Serine/threonine-protein kinase, Transferase
Biological processApoptosis, Transcription, Transcription regulation, Translation regulation
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-418889 Caspase activation via Dependence Receptors in the absence of ligand

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
O43293

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

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SignaLinki
O43293

SIGNOR Signaling Network Open Resource

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SIGNORi
O43293

<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:
Death-associated protein kinase 3 (EC:2.7.11.16 Publications)
Short name:
DAP kinase 3
Alternative name(s):
DAP-like kinase
Short name:
Dlk
MYPT1 kinase
Zipper-interacting protein kinase
Short name:
ZIP-kinase
<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:DAPK3
Synonyms:ZIPK
<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 19

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000167657.11

Human Gene Nomenclature Database

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HGNCi
HGNC:2676 DAPK3

Online Mendelian Inheritance in Man (OMIM)

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MIMi
603289 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_O43293

<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; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, 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>Mutagenesisi42K → A: Loss of kinase activity at low concentrations of ATP. 1 Publication1
Mutagenesisi161D → A: Loss of kinase activity. 1 Publication1
Mutagenesisi180T → A: Greatly reduced kinase activity. 1 Publication1
Mutagenesisi225T → A: Loss of kinase activity. 1 Publication1
Mutagenesisi265T → A: Loss of phosphorylation by ROCK1, catalytically inactive. 1 Publication1
Mutagenesisi294 – 295RR → AA: Cytoplasmic localization. 1 Publication2
Mutagenesisi299 – 300TT → AA: Predominantly nuclear localization. 1 Publication2
Mutagenesisi299T → A: Loss of phosphorylation by ROCK1. 1 Publication1
Mutagenesisi299T → D: Predominantly cytoplasmic localization; phosphomimetic. 1 Publication1
Mutagenesisi427V → A: Predominantly nuclear localization; when associated with A-434 and A-441. 1 Publication1
Mutagenesisi434V → A: Predominantly nuclear localization; when associated with A-427 and A-441. 1 Publication1
Mutagenesisi441L → A: Predominantly nuclear localization; when associated with A-427 and A-434. 1 Publication1

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

DisGeNET

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DisGeNETi
1613

Open Targets

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OpenTargetsi
ENSG00000167657

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA27144

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL2468

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2004

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
DAPK3

<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_00000859141 – 454Death-associated protein kinase 3Add BLAST454

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 residuei50Phosphoserine; by autocatalysis1 Publication1
Modified residuei180Phosphothreonine2 Publications1
Modified residuei225Phosphothreonine1 Publication1
Modified residuei265Phosphothreonine; by autocatalysis and ROCK13 Publications1
Modified residuei299Phosphothreonine; by autocatalysis, DAPK1 and ROCK14 Publications1
Modified residuei306Phosphothreonine; by autocatalysis1 Publication1
Modified residuei309Phosphoserine; by DAPK11 Publication1
Modified residuei311Phosphoserine; by autocatalysis and DAPK12 Publications1
Modified residuei312Phosphoserine; by DAPK1Combined sources1 Publication1
Modified residuei318Phosphoserine; by DAPK11 Publication1
Modified residuei326Phosphoserine; by DAPK11 Publication1

<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

The phosphorylation status is critical for kinase activity, oligomerization and intracellular localization. Phosphorylation at Thr-180, Thr-225 and Thr-265 is essential for activity. The phosphorylated form is localized in the cytoplasm promoted by phosphorylation at Thr-299; nuclear translocation or retention is maximal when it is not phosphorylated. Phosphorylation increases the trimeric form, and its dephosphorylation favors a kinase-inactive monomeric form. Both isoform 1 and isoform 2 can undergo autophosphorylation.4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
O43293

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
O43293

MaxQB - The MaxQuant DataBase

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MaxQBi
O43293

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

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PaxDbi
O43293

PeptideAtlas

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PeptideAtlasi
O43293

PRoteomics IDEntifications database

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PRIDEi
O43293

ProteomicsDB human proteome resource

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ProteomicsDBi
48863
48864 [O43293-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
O43293

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

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PhosphoSitePlusi
O43293

<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

Widely expressed. Isoform 1 and isoform 2 are expressed in the bladder smooth muscle.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000167657 Expressed in 219 organ(s), highest expression level in heart left ventricle

CleanEx database of gene expression profiles

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CleanExi
HS_DAPK3

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
O43293 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O43293 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA028569
HPA064809

<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

Homooligomer in its kinase-active form (homotrimers and homodimers are reported); monomeric in its kinase-inactive form. Homodimerization is required for activation segment autophosphorylation (Probable). Isoform 1 and isoform 2 interact with myosin and PPP1R12A; interaction of isoform 1 with PPP1R12A is inhibited by RhoA dominant negative form. Interacts with NLK, DAXX, STAT3, RHOD (GTP-bound form) and TCP10L. Interacts with PAWR; the interaction is reported conflictingly: according to PubMed:17953487 does not interact with PAWR. Interacts with ULK1; may be a substrate of ULK1.1 Publication10 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
107983, 56 interactors

Protein interaction database and analysis system

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IntActi
O43293, 46 interactors

Molecular INTeraction database

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MINTi
O43293

STRING: functional protein association networks

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STRINGi
9606.ENSP00000301264

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
O43293

<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

1454
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
1YRPX-ray3.10A/B1-277[»]
2J90X-ray2.00A/B9-289[»]
3BHYX-ray1.24A9-289[»]
3BQRX-ray1.75A9-289[»]
5A6NX-ray1.70A/B9-289[»]
5A6OX-ray1.60A/B9-289[»]
5VJAX-ray2.46A/B/C/D9-289[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
O43293

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

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SMRi
O43293

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
O43293

<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>Domaini13 – 275Protein kinasePROSITE-ProRule annotationAdd BLAST263

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>Regioni161 – 204Activation segmentBy similarityAdd BLAST44
Regioni427 – 441Leucine-zipper1 PublicationAdd BLAST15

<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
KOG0032 Eukaryota
ENOG410XRMJ LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000161753

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000204872

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG054968

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O43293

KEGG Orthology (KO)

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KOi
K08803

Identification of Orthologs from Complete Genome Data

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OMAi
PWIKVIK

Database of Orthologous Groups

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OrthoDBi
813445at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
O43293

TreeFam database of animal gene trees

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TreeFami
TF314166

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR011009 Kinase-like_dom_sf
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
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

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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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

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

This entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: O43293-1) [UniParc]FASTAAdd to basket
Also known as: ZIPK-L

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
MSTFRQEDVE DHYEMGEELG SGQFAIVRKC RQKGTGKEYA AKFIKKRRLS
60 70 80 90 100
SSRRGVSREE IEREVNILRE IRHPNIITLH DIFENKTDVV LILELVSGGE
110 120 130 140 150
LFDFLAEKES LTEDEATQFL KQILDGVHYL HSKRIAHFDL KPENIMLLDK
160 170 180 190 200
NVPNPRIKLI DFGIAHKIEA GNEFKNIFGT PEFVAPEIVN YEPLGLEADM
210 220 230 240 250
WSIGVITYIL LSGASPFLGE TKQETLTNIS AVNYDFDEEY FSNTSELAKD
260 270 280 290 300
FIRRLLVKDP KRRMTIAQSL EHSWIKAIRR RNVRGEDSGR KPERRRLKTT
310 320 330 340 350
RLKEYTIKSH SSLPPNNSYA DFERFSKVLE EAAAAEEGLR ELQRSRRLCH
360 370 380 390 400
EDVEALAAIY EEKEAWYREE SDSLGQDLRR LRQELLKTEA LKRQAQEEAK
410 420 430 440 450
GALLGTSGLK RRFSRLENRY EALAKQVASE MRFVQDLVRA LEQEKLQGVE

CGLR
Length:454
Mass (Da):52,536
Last modified:June 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:i56773008A6A61CF0
GO
Isoform 2 (identifier: O43293-2) [UniParc]FASTAAdd to basket
Also known as: ZIPK-S

The sequence of this isoform differs from the canonical sequence as follows:
     313-322: LPPNNSYADF → ASPIVAPVDA
     323-454: Missing.

Note: The internal splice site between exon 8 and the 3' UTR, which yields this truncated isoform, is non-canonical.
Show »
Length:322
Mass (Da):37,048
Checksum:i616983FE83F8DDA6
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 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
M0R0D0M0R0D0_HUMAN
Death-associated protein kinase 3
DAPK3
158Annotation 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>
M0QYW5M0QYW5_HUMAN
Death-associated protein kinase 3
DAPK3
141Annotation 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>
M0QYY8M0QYY8_HUMAN
Death-associated protein kinase 3
DAPK3
92Annotation 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>

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_040438112T → M in a colorectal adenocarcinoma sample; somatic mutation; greatly reduces kinase activity, increases cell proliferation and cell survival. 2 Publications1
Natural variantiVAR_040439161D → N in an ovarian mucinous carcinoma sample; somatic mutation; greatly reduces kinase activity, increases cell proliferation and cell survival. 2 Publications1
Natural variantiVAR_040440216P → S in a lung neuroendocrine carcinoma sample; somatic mutation; greatly reduces kinase activity, increases cell proliferation, cell adhesion and cell survival. 2 Publications1

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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_042059313 – 322LPPNNSYADF → ASPIVAPVDA in isoform 2. 1 Publication10
Alternative sequenceiVSP_042060323 – 454Missing in isoform 2. 1 PublicationAdd BLAST132

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AB007144 mRNA Translation: BAA24955.1
AB022341 mRNA Translation: BAA81746.1
AK074799 mRNA Translation: BAG52004.1
BC126430 mRNA Translation: AAI26431.1
BC126432 mRNA Translation: AAI26433.1
AB265224 mRNA Translation: BAF34614.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS12116.1 [O43293-1]

NCBI Reference Sequences

More...
RefSeqi
NP_001339.1, NM_001348.2 [O43293-1]
XP_005259565.1, XM_005259508.1 [O43293-1]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.631844

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000301264; ENSP00000301264; ENSG00000167657 [O43293-1]
ENST00000545797; ENSP00000442973; ENSG00000167657 [O43293-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
1613

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:1613

UCSC genome browser

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UCSCi
uc002lzc.2 human [O43293-1]

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
AB007144 mRNA Translation: BAA24955.1
AB022341 mRNA Translation: BAA81746.1
AK074799 mRNA Translation: BAG52004.1
BC126430 mRNA Translation: AAI26431.1
BC126432 mRNA Translation: AAI26433.1
AB265224 mRNA Translation: BAF34614.1
CCDSiCCDS12116.1 [O43293-1]
RefSeqiNP_001339.1, NM_001348.2 [O43293-1]
XP_005259565.1, XM_005259508.1 [O43293-1]
UniGeneiHs.631844

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YRPX-ray3.10A/B1-277[»]
2J90X-ray2.00A/B9-289[»]
3BHYX-ray1.24A9-289[»]
3BQRX-ray1.75A9-289[»]
5A6NX-ray1.70A/B9-289[»]
5A6OX-ray1.60A/B9-289[»]
5VJAX-ray2.46A/B/C/D9-289[»]
ProteinModelPortaliO43293
SMRiO43293
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107983, 56 interactors
IntActiO43293, 46 interactors
MINTiO43293
STRINGi9606.ENSP00000301264

Chemistry databases

BindingDBiO43293
ChEMBLiCHEMBL2468
GuidetoPHARMACOLOGYi2004

PTM databases

iPTMnetiO43293
PhosphoSitePlusiO43293

Polymorphism and mutation databases

BioMutaiDAPK3

Proteomic databases

EPDiO43293
jPOSTiO43293
MaxQBiO43293
PaxDbiO43293
PeptideAtlasiO43293
PRIDEiO43293
ProteomicsDBi48863
48864 [O43293-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
1613
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000301264; ENSP00000301264; ENSG00000167657 [O43293-1]
ENST00000545797; ENSP00000442973; ENSG00000167657 [O43293-1]
GeneIDi1613
KEGGihsa:1613
UCSCiuc002lzc.2 human [O43293-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1613
DisGeNETi1613
EuPathDBiHostDB:ENSG00000167657.11

GeneCards: human genes, protein and diseases

More...
GeneCardsi
DAPK3
HGNCiHGNC:2676 DAPK3
HPAiHPA028569
HPA064809
MIMi603289 gene
neXtProtiNX_O43293
OpenTargetsiENSG00000167657
PharmGKBiPA27144

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0032 Eukaryota
ENOG410XRMJ LUCA
GeneTreeiENSGT00940000161753
HOGENOMiHOG000204872
HOVERGENiHBG054968
InParanoidiO43293
KOiK08803
OMAiPWIKVIK
OrthoDBi813445at2759
PhylomeDBiO43293
TreeFamiTF314166

Enzyme and pathway databases

ReactomeiR-HSA-418889 Caspase activation via Dependence Receptors in the absence of ligand
SABIO-RKiO43293
SignaLinkiO43293
SIGNORiO43293

Miscellaneous databases

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

More...
ChiTaRSi
DAPK3 human
EvolutionaryTraceiO43293

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
DAPK3

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

More...
GenomeRNAii
1613

Protein Ontology

More...
PROi
PR:O43293

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000167657 Expressed in 219 organ(s), highest expression level in heart left ventricle
CleanExiHS_DAPK3
ExpressionAtlasiO43293 baseline and differential
GenevisibleiO43293 HS

Family and domain databases

InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
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...

<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 nameiDAPK3_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: O43293
Secondary accession number(s): A0AVN4, B3KQE2, Q05JY4
<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: November 28, 2003
Last sequence update: June 1, 1998
Last modified: January 16, 2019
This is version 179 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, Reference proteome

Documents

  1. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
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