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Protein

Death-associated protein kinase 1

Gene

DAPK1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

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

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Calcium/calmodulin-dependent serine/threonine kinase involved in multiple cellular signaling pathways that trigger cell survival, apoptosis, and autophagy. Regulates both type I apoptotic and type II autophagic cell deaths signal, depending on the cellular setting. The former is caspase-dependent, while the latter is caspase-independent and is characterized by the accumulation of autophagic vesicles. Phosphorylates PIN1 resulting in inhibition of its catalytic activity, nuclear localization, and cellular function. Phosphorylates TPM1, enhancing stress fiber formation in endothelial cells. Phosphorylates STX1A and significantly decreases its binding to STXBP1. Phosphorylates PRKD1 and regulates JNK signaling by binding and activating PRKD1 under oxidative stress. Phosphorylates BECN1, reducing its interaction with BCL2 and BCL2L1 and promoting the induction of autophagy. Phosphorylates TSC2, disrupting the TSC1-TSC2 complex and stimulating mTORC1 activity in a growth factor-dependent pathway. Phosphorylates RPS6, MYL9 and DAPK3. Acts as a signaling amplifier of NMDA receptors at extrasynaptic sites for mediating brain damage in stroke. Cerebral ischemia recruits DAPK1 into the NMDA receptor complex and it phosphorylates GRINB at Ser-1303 inducing injurious Ca2+ influx through NMDA receptor channels, resulting in an irreversible neuronal death. Required together with DAPK3 for phosphorylation of RPL13A upon interferon-gamma activation which is causing RPL13A involvement in transcript-selective translation inhibition.
Isoform 2 cannot induce apoptosis but can induce membrane blebbing.

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

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

Mg2+

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Activated by Ca2+/calmodulin. Regulated by a locking mechanism, involving autophosphorylation at Ser-308 and calmodulin binding. In the inactive state, Ser-308 is phosphorylated. Activation involves its dephosphorylation and a release-of-autoinhibition mechanism where binding of calmodulin induces a conformational change that relieves the steric block of the active site by the autoinhibitory domain. Activity is modulated by UNC5B and NTN1. UNC5B activates it by inhibiting the phosphorylation at Ser-308, whereas NTN1 inhibits UNC5B-mediated activation of DAPK1. Endoplasmic-stress activates by causing Ser-308 dephosphorylation.3 Publications

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 sitei42ATP1
Binding sitei100ATP1
<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
Binding sitei161ATP1

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 – 27ATP9
Nucleotide bindingi94 – 96ATP3

<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
  • calmodulin binding Source: UniProtKB
  • calmodulin-dependent protein kinase activity Source: UniProtKB
  • GTP binding Source: UniProtKB-KW
  • identical protein binding Source: IntAct
  • protein kinase activity Source: UniProtKB
  • protein serine/threonine kinase activity Source: GO_Central
  • syntaxin-1 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 functionCalmodulin-binding, Kinase, Serine/threonine-protein kinase, Transferase
Biological processApoptosis, Translation regulation
LigandATP-binding, GTP-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-418889 Caspase activation via Dependence Receptors in the absence of ligand

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

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SignaLinki
P53355

SIGNOR Signaling Network Open Resource

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SIGNORi
P53355

<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 1 (EC:2.7.11.1)
Short name:
DAP kinase 1
<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:DAPK1
Synonyms:DAPK
<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 9

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000196730.12

Human Gene Nomenclature Database

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HGNCi
HGNC:2674 DAPK1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
600831 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P53355

<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, Cytoskeleton

<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 activity, apoptotic function and of autophosphorylation. 2 Publications1
Mutagenesisi289S → A: Loss of phosphorylation and significant increase in proapoptotic activity. 1
Mutagenesisi289S → E: Reduction in proapoptotic activity. 1
Mutagenesisi308S → A: Elevated Ca(2+)-calmodulin binding and Ca(2+)-calmodulin-independent kinase activity. Increases apoptotic activity. 1 Publication1
Mutagenesisi308S → D: Reduced Ca(2+)-calmodulin binding and Ca(2+)-calmodulin-independent kinase activity. Decreases apoptotic activity. 1 Publication1
Mutagenesisi313S → A: Minimal effect on activity. 1 Publication1

Organism-specific databases

DisGeNET

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DisGeNETi
1612

Open Targets

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OpenTargetsi
ENSG00000196730

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA27142

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL2558

Drug and drug target database

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DrugBanki
DB04395 Phosphoaminophosphonic Acid-Adenylate Ester

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2002

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
DAPK1

Domain mapping of disease mutations (DMDM)

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DMDMi
317373595

<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_00000859101 – 1430Death-associated protein kinase 1Add BLAST1430

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 residuei289Phosphoserine; by RPS6KA1 and RPS6KA31 Publication1
Modified residuei308Phosphoserine; by autocatalysis3 Publications1
Modified residuei319PhosphoserineCombined sources1
Modified residuei333PhosphoserineCombined sources1
Modified residuei734Phosphoserine; by MAPK11 Publication1
Modified residuei1115PhosphoserineBy 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

Ubiquitinated by the BCR(KLHL20) E3 ubiquitin ligase complex, leading to its degradation by the proteasome.1 Publication
Removal of the C-terminal tail of isoform 2 (corresponding to amino acids 296-337 of isoform 2) by proteolytic cleavage stimulates maximally its membrane-blebbing function.1 Publication
In response to mitogenic stimulation (PMA or EGF), phosphorylated at Ser-289; phosphorylation suppresses DAPK1 pro-apoptotic function. Autophosphorylation at Ser-308 inhibits its catalytic activity. Phosphorylation at Ser-734 by MAPK1 increases its catalytic activity and promotes cytoplasmic retention of MAPK1. Endoplasmic-stress can cause dephosphorylation at Ser-308.5 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P53355

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P53355

MaxQB - The MaxQuant DataBase

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MaxQBi
P53355

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

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PaxDbi
P53355

PeptideAtlas

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PeptideAtlasi
P53355

PRoteomics IDEntifications database

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PRIDEi
P53355

ProteomicsDB human proteome resource

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ProteomicsDBi
56570
56571 [P53355-2]
56572 [P53355-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P53355

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

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PhosphoSitePlusi
P53355

<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

Isoform 2 is expressed in normal intestinal tissue as well as in colorectal carcinomas.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

Up-regulated following treatment with IFNG/IFN-gamma.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000196730 Expressed in 212 organ(s), highest expression level in amniotic fluid

CleanEx database of gene expression profiles

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CleanExi
HS_DAPK1

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P53355 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P53355 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB037302
HPA040472
HPA048436

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

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

Interacts with KLHL20. Interacts (via death domain) with MAPK1 and MAPK3. Interacts with MAP1B (via N-terminus). Interacts (via death domain) with UNC5B (via death domain). Interacts with PRKD1 in an oxidative stress-regulated manner. Interacts with PIN1, PDCD6, BECN1, GRINB, TSC2 and STX1A. Interacts (via kinase domain) with DAPK3 (via kinase domain).15 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
107982, 52 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-102 DAPK1 - calmodulin complex

Protein interaction database and analysis system

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IntActi
P53355, 119 interactors

Molecular INTeraction database

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MINTi
P53355

STRING: functional protein association networks

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STRINGi
9606.ENSP00000350785

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P53355

<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

11430
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
1IG1X-ray1.80A2-285[»]
1JKKX-ray2.40A2-285[»]
1JKLX-ray1.62A2-285[»]
1JKSX-ray1.50A2-285[»]
1JKTX-ray3.50A/B2-285[»]
1P4FX-ray1.90A2-285[»]
1WVWX-ray2.40A1-278[»]
1WVXX-ray2.60A1-278[»]
1WVYX-ray2.80A1-278[»]
1YR5X-ray1.70B302-320[»]
2W4JX-ray1.30A1-277[»]
2W4KX-ray1.90A1-302[»]
2X0GX-ray2.20A1-334[»]
2XUUX-ray1.80A1-334[»]
2XZSX-ray2.00A/B2-312[»]
2Y0AX-ray2.60A2-304[»]
2Y4PX-ray2.65A/B/C/D1-285[»]
2Y4VX-ray1.80B302-320[»]
2YAKX-ray2.20A1-285[»]
3DFCX-ray1.90B1-285[»]
3DGKX-ray1.70A1-285[»]
3EH9X-ray1.70A2-285[»]
3EHAX-ray1.60A2-285[»]
3F5GX-ray1.85A2-285[»]
3F5UX-ray2.00A1-285[»]
3GU4X-ray1.35A1-285[»]
3GU5X-ray1.65A1-285[»]
3GU6X-ray1.49A1-285[»]
3GU7X-ray1.90A1-285[»]
3GU8X-ray1.60A1-285[»]
3GUBX-ray1.71A1-285[»]
3ZXTX-ray2.65A/B/C/D1-285[»]
4B4LX-ray1.75A1-334[»]
4PF4X-ray1.13A1-277[»]
4TL0X-ray2.70A1-334[»]
4TXCX-ray1.95A1-285[»]
4UV0X-ray2.49A1-321[»]
4YO4X-ray1.60A2-285[»]
4YPDX-ray1.40A2-285[»]
5AUTX-ray1.70A1-285[»]
5AUUX-ray1.70A1-285[»]
5AUVX-ray1.50A1-285[»]
5AUWX-ray1.50A1-285[»]
5AUXX-ray1.50A1-285[»]
5AUYX-ray2.00A1-285[»]
5AUZX-ray1.60A1-285[»]
5AV0X-ray1.85A1-285[»]
5AV1X-ray1.50A1-285[»]
5AV2X-ray1.50A1-285[»]
5AV3X-ray1.90A1-285[»]
5AV4X-ray1.40A1-285[»]
6GY5X-ray1.09U1334-1344[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P53355

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

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SMRi
P53355

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
P53355

<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
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati378 – 407ANK 1Add BLAST30
Repeati411 – 440ANK 2Add BLAST30
Repeati444 – 473ANK 3Add BLAST30
Repeati477 – 506ANK 4Add BLAST30
Repeati510 – 539ANK 5Add BLAST30
Repeati543 – 572ANK 6Add BLAST30
Repeati576 – 605ANK 7Add BLAST30
Repeati609 – 638ANK 8Add BLAST30
Domaini681 – 955RocPROSITE-ProRule annotationAdd BLAST275
Repeati875 – 904ANK 9Add BLAST30
Repeati1162 – 1196ANK 10Add BLAST35
Domaini1312 – 1396DeathPROSITE-ProRule annotationAdd BLAST85

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>Regioni267 – 334Calmodulin-bindingAdd BLAST68
Regioni292 – 301Autoinhibitory domainBy similarity10

<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 autoinhibitory domain sterically blocks the substrate peptide-binding site by making both hydrophobic and electrostatic contacts with the kinase core.

<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

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0032 Eukaryota
ENOG410XRMJ LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000153424

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000082489

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG051296

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P53355

KEGG Orthology (KO)

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KOi
K08803

Identification of Orthologs from Complete Genome Data

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OMAi
NTMGGYR

Database of Orthologous Groups

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OrthoDBi
981551at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P53355

TreeFam database of animal gene trees

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TreeFami
TF314166

Family and domain databases

Conserved Domains Database

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CDDi
cd00204 ANK, 3 hits

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.25.40.20, 2 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR002110 Ankyrin_rpt
IPR020683 Ankyrin_rpt-contain_dom
IPR036770 Ankyrin_rpt-contain_sf
IPR020676 DAPK1
IPR011029 DEATH-like_dom_sf
IPR000488 Death_domain
IPR011009 Kinase-like_dom_sf
IPR027417 P-loop_NTPase
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR020859 ROC_dom
IPR008271 Ser/Thr_kinase_AS

The PANTHER Classification System

More...
PANTHERi
PTHR44619 PTHR44619, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00023 Ank, 1 hit
PF12796 Ank_2, 2 hits
PF00531 Death, 1 hit
PF00069 Pkinase, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01415 ANKYRIN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00248 ANK, 9 hits
SM00005 DEATH, 1 hit
SM00220 S_TKc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47986 SSF47986, 1 hit
SSF48403 SSF48403, 1 hit
SSF52540 SSF52540, 1 hit
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50297 ANK_REP_REGION, 1 hit
PS50088 ANK_REPEAT, 7 hits
PS50017 DEATH_DOMAIN, 1 hit
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit
PS51424 ROC, 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 (4+)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 4 <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 4 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: P53355-1) [UniParc]FASTAAdd to basket
Also known as: Alpha

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
MTVFRQENVD DYYDTGEELG SGQFAVVKKC REKSTGLQYA AKFIKKRRTK
60 70 80 90 100
SSRRGVSRED IEREVSILKE IQHPNVITLH EVYENKTDVI LILELVAGGE
110 120 130 140 150
LFDFLAEKES LTEEEATEFL KQILNGVYYL HSLQIAHFDL KPENIMLLDR
160 170 180 190 200
NVPKPRIKII DFGLAHKIDF GNEFKNIFGT PEFVAPEIVN YEPLGLEADM
210 220 230 240 250
WSIGVITYIL LSGASPFLGD TKQETLANVS AVNYEFEDEY FSNTSALAKD
260 270 280 290 300
FIRRLLVKDP KKRMTIQDSL QHPWIKPKDT QQALSRKASA VNMEKFKKFA
310 320 330 340 350
ARKKWKQSVR LISLCQRLSR SFLSRSNMSV ARSDDTLDEE DSFVMKAIIH
360 370 380 390 400
AINDDNVPGL QHLLGSLSNY DVNQPNKHGT PPLLIAAGCG NIQILQLLIK
410 420 430 440 450
RGSRIDVQDK GGSNAVYWAA RHGHVDTLKF LSENKCPLDV KDKSGEMALH
460 470 480 490 500
VAARYGHADV AQLLCSFGSN PNIQDKEEET PLHCAAWHGY YSVAKALCEA
510 520 530 540 550
GCNVNIKNRE GETPLLTASA RGYHDIVECL AEHGADLNAC DKDGHIALHL
560 570 580 590 600
AVRRCQMEVI KTLLSQGCFV DYQDRHGNTP LHVACKDGNM PIVVALCEAN
610 620 630 640 650
CNLDISNKYG RTPLHLAANN GILDVVRYLC LMGASVEALT TDGKTAEDLA
660 670 680 690 700
RSEQHEHVAG LLARLRKDTH RGLFIQQLRP TQNLQPRIKL KLFGHSGSGK
710 720 730 740 750
TTLVESLKCG LLRSFFRRRR PRLSSTNSSR FPPSPLASKP TVSVSINNLY
760 770 780 790 800
PGCENVSVRS RSMMFEPGLT KGMLEVFVAP THHPHCSADD QSTKAIDIQN
810 820 830 840 850
AYLNGVGDFS VWEFSGNPVY FCCYDYFAAN DPTSIHVVVF SLEEPYEIQL
860 870 880 890 900
NQVIFWLSFL KSLVPVEEPI AFGGKLKNPL QVVLVATHAD IMNVPRPAGG
910 920 930 940 950
EFGYDKDTSL LKEIRNRFGN DLHISNKLFV LDAGASGSKD MKVLRNHLQE
960 970 980 990 1000
IRSQIVSVCP PMTHLCEKII STLPSWRKLN GPNQLMSLQQ FVYDVQDQLN
1010 1020 1030 1040 1050
PLASEEDLRR IAQQLHSTGE INIMQSETVQ DVLLLDPRWL CTNVLGKLLS
1060 1070 1080 1090 1100
VETPRALHHY RGRYTVEDIQ RLVPDSDVEE LLQILDAMDI CARDLSSGTM
1110 1120 1130 1140 1150
VDVPALIKTD NLHRSWADEE DEVMVYGGVR IVPVEHLTPF PCGIFHKVQV
1160 1170 1180 1190 1200
NLCRWIHQQS TEGDADIRLW VNGCKLANRG AELLVLLVNH GQGIEVQVRG
1210 1220 1230 1240 1250
LETEKIKCCL LLDSVCSTIE NVMATTLPGL LTVKHYLSPQ QLREHHEPVM
1260 1270 1280 1290 1300
IYQPRDFFRA QTLKETSLTN TMGGYKESFS SIMCFGCHDV YSQASLGMDI
1310 1320 1330 1340 1350
HASDLNLLTR RKLSRLLDPP DPLGKDWCLL AMNLGLPDLV AKYNTSNGAP
1360 1370 1380 1390 1400
KDFLPSPLHA LLREWTTYPE STVGTLMSKL RELGRRDAAD FLLKASSVFK
1410 1420 1430
INLDGNGQEA YASSCNSGTS YNSISSVVSR
Length:1,430
Mass (Da):160,046
Last modified:January 11, 2011 - v6
<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:iE2C4246E7C78A6D2
GO
Isoform 2 (identifier: P53355-2) [UniParc]FASTAAdd to basket
Also known as: s-DAPK-1

The sequence of this isoform differs from the canonical sequence as follows:
     1-446: Missing.
     742-783: VSVSINNLYP...LEVFVAPTHH → GRNLHAGPVS...SLGLYWTLWP
     784-1430: Missing.

Show »
Length:337
Mass (Da):36,765
Checksum:i3BA58BA79D87E0C6
GO
Isoform 3 (identifier: P53355-3) [UniParc]FASTAAdd to basket
Also known as: Beta

The sequence of this isoform differs from the canonical sequence as follows:
     1430-1430: R → RRNSHVWNPTV

Show »
Length:1,440
Mass (Da):161,237
Checksum:iD43BB6B6A3F0ABF9
GO
Isoform 4 (identifier: P53355-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     805-870: Missing.

Note: No experimental confirmation available.
Show »
Length:1,364
Mass (Da):152,467
Checksum:i60E285E6A32348CB
GO

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

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F8WCQ3F8WCQ3_HUMAN
Death-associated protein kinase 1
DAPK1
188Annotation 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 AAP35581 differs from that shown. Contaminating sequence. Sequence of unknown origin in the C-terminal part.Curated
The sequence CAA53712 differs from that shown. Reason: Frameshift at positions 462 and 464.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti490Y → H in BAC87163 (PubMed:14702039).Curated1
Sequence conflicti1217S → G in CAH18690 (PubMed:17974005).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_033235416V → I1 PublicationCorresponds to variant dbSNP:rs12343465Ensembl.1
Natural variantiVAR_040420461A → S1 Publication1
Natural variantiVAR_040421519S → A1 Publication1
Natural variantiVAR_040422540C → Y1 PublicationCorresponds to variant dbSNP:rs56327474Ensembl.1
Natural variantiVAR_060693591P → L1 PublicationCorresponds to variant dbSNP:rs36214022Ensembl.1
Natural variantiVAR_060694622I → M1 PublicationCorresponds to variant dbSNP:rs36215047Ensembl.1
Natural variantiVAR_040423941M → T1 Publication1
Natural variantiVAR_040424977R → W1 Publication1
Natural variantiVAR_040425978K → N1 Publication1
Natural variantiVAR_040426993Y → C1 Publication1
Natural variantiVAR_040427994D → E1 Publication1
Natural variantiVAR_0404281005E → Q1 Publication1
Natural variantiVAR_0404291007D → Y1 Publication1
Natural variantiVAR_0404301008L → P1 Publication1
Natural variantiVAR_0404311010R → C1 PublicationCorresponds to variant dbSNP:rs371784492Ensembl.1
Natural variantiVAR_0404321018T → A1 Publication1
Natural variantiVAR_0404331272M → I1 PublicationCorresponds to variant dbSNP:rs56169226Ensembl.1
Natural variantiVAR_0404341346S → N5 PublicationsCorresponds to variant dbSNP:rs1056719Ensembl.1
Natural variantiVAR_0404351405G → V2 PublicationsCorresponds to variant dbSNP:rs36220450Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. 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_0420531 – 446Missing in isoform 2. 1 PublicationAdd BLAST446
Alternative sequenceiVSP_042054742 – 783VSVSI…APTHH → GRNLHAGPVSPAGVGFRTLS FQGLGGKGVVFGSLGLYWTL WP in isoform 2. 1 PublicationAdd BLAST42
Alternative sequenceiVSP_042055784 – 1430Missing in isoform 2. 1 PublicationAdd BLAST647
Alternative sequenceiVSP_054478805 – 870Missing in isoform 4. 1 PublicationAdd BLAST66
Alternative sequenceiVSP_0420561430R → RRNSHVWNPTV in isoform 3. Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X76104 mRNA Translation: CAA53712.1 Frameshift.
AK127855 mRNA Translation: BAC87163.1
CR749834 mRNA Translation: CAH18690.1
DQ436495 Genomic DNA Translation: ABD96827.1
AL160279 Genomic DNA No translation available.
AL161787 Genomic DNA No translation available.
AL591852 Genomic DNA No translation available.
CH471089 Genomic DNA Translation: EAW62727.1
BC113660 mRNA Translation: AAI13661.1
BC143733 mRNA Translation: AAI43734.1
BC143759 mRNA Translation: AAI43760.1
BT006935 mRNA Translation: AAP35581.1 Sequence problems.

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS43842.1 [P53355-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
I37275

NCBI Reference Sequences

More...
RefSeqi
NP_001275658.1, NM_001288729.1 [P53355-1]
NP_001275659.1, NM_001288730.1 [P53355-1]
NP_001275660.1, NM_001288731.1 [P53355-1]
NP_004929.2, NM_004938.3 [P53355-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.380277
Hs.693441

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000358077; ENSP00000350785; ENSG00000196730 [P53355-1]
ENST00000408954; ENSP00000386135; ENSG00000196730 [P53355-1]
ENST00000469640; ENSP00000418885; ENSG00000196730 [P53355-4]
ENST00000472284; ENSP00000417076; ENSG00000196730 [P53355-1]
ENST00000491893; ENSP00000419026; ENSG00000196730 [P53355-4]
ENST00000622514; ENSP00000484267; ENSG00000196730 [P53355-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
1612

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:1612

UCSC genome browser

More...
UCSCi
uc004apc.5 human [P53355-1]

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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

NIEHS-SNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76104 mRNA Translation: CAA53712.1 Frameshift.
AK127855 mRNA Translation: BAC87163.1
CR749834 mRNA Translation: CAH18690.1
DQ436495 Genomic DNA Translation: ABD96827.1
AL160279 Genomic DNA No translation available.
AL161787 Genomic DNA No translation available.
AL591852 Genomic DNA No translation available.
CH471089 Genomic DNA Translation: EAW62727.1
BC113660 mRNA Translation: AAI13661.1
BC143733 mRNA Translation: AAI43734.1
BC143759 mRNA Translation: AAI43760.1
BT006935 mRNA Translation: AAP35581.1 Sequence problems.
CCDSiCCDS43842.1 [P53355-1]
PIRiI37275
RefSeqiNP_001275658.1, NM_001288729.1 [P53355-1]
NP_001275659.1, NM_001288730.1 [P53355-1]
NP_001275660.1, NM_001288731.1 [P53355-1]
NP_004929.2, NM_004938.3 [P53355-1]
UniGeneiHs.380277
Hs.693441

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IG1X-ray1.80A2-285[»]
1JKKX-ray2.40A2-285[»]
1JKLX-ray1.62A2-285[»]
1JKSX-ray1.50A2-285[»]
1JKTX-ray3.50A/B2-285[»]
1P4FX-ray1.90A2-285[»]
1WVWX-ray2.40A1-278[»]
1WVXX-ray2.60A1-278[»]
1WVYX-ray2.80A1-278[»]
1YR5X-ray1.70B302-320[»]
2W4JX-ray1.30A1-277[»]
2W4KX-ray1.90A1-302[»]
2X0GX-ray2.20A1-334[»]
2XUUX-ray1.80A1-334[»]
2XZSX-ray2.00A/B2-312[»]
2Y0AX-ray2.60A2-304[»]
2Y4PX-ray2.65A/B/C/D1-285[»]
2Y4VX-ray1.80B302-320[»]
2YAKX-ray2.20A1-285[»]
3DFCX-ray1.90B1-285[»]
3DGKX-ray1.70A1-285[»]
3EH9X-ray1.70A2-285[»]
3EHAX-ray1.60A2-285[»]
3F5GX-ray1.85A2-285[»]
3F5UX-ray2.00A1-285[»]
3GU4X-ray1.35A1-285[»]
3GU5X-ray1.65A1-285[»]
3GU6X-ray1.49A1-285[»]
3GU7X-ray1.90A1-285[»]
3GU8X-ray1.60A1-285[»]
3GUBX-ray1.71A1-285[»]
3ZXTX-ray2.65A/B/C/D1-285[»]
4B4LX-ray1.75A1-334[»]
4PF4X-ray1.13A1-277[»]
4TL0X-ray2.70A1-334[»]
4TXCX-ray1.95A1-285[»]
4UV0X-ray2.49A1-321[»]
4YO4X-ray1.60A2-285[»]
4YPDX-ray1.40A2-285[»]
5AUTX-ray1.70A1-285[»]
5AUUX-ray1.70A1-285[»]
5AUVX-ray1.50A1-285[»]
5AUWX-ray1.50A1-285[»]
5AUXX-ray1.50A1-285[»]
5AUYX-ray2.00A1-285[»]
5AUZX-ray1.60A1-285[»]
5AV0X-ray1.85A1-285[»]
5AV1X-ray1.50A1-285[»]
5AV2X-ray1.50A1-285[»]
5AV3X-ray1.90A1-285[»]
5AV4X-ray1.40A1-285[»]
6GY5X-ray1.09U1334-1344[»]
ProteinModelPortaliP53355
SMRiP53355
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107982, 52 interactors
ComplexPortaliCPX-102 DAPK1 - calmodulin complex
IntActiP53355, 119 interactors
MINTiP53355
STRINGi9606.ENSP00000350785

Chemistry databases

BindingDBiP53355
ChEMBLiCHEMBL2558
DrugBankiDB04395 Phosphoaminophosphonic Acid-Adenylate Ester
GuidetoPHARMACOLOGYi2002

PTM databases

iPTMnetiP53355
PhosphoSitePlusiP53355

Polymorphism and mutation databases

BioMutaiDAPK1
DMDMi317373595

Proteomic databases

EPDiP53355
jPOSTiP53355
MaxQBiP53355
PaxDbiP53355
PeptideAtlasiP53355
PRIDEiP53355
ProteomicsDBi56570
56571 [P53355-2]
56572 [P53355-3]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
1612
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000358077; ENSP00000350785; ENSG00000196730 [P53355-1]
ENST00000408954; ENSP00000386135; ENSG00000196730 [P53355-1]
ENST00000469640; ENSP00000418885; ENSG00000196730 [P53355-4]
ENST00000472284; ENSP00000417076; ENSG00000196730 [P53355-1]
ENST00000491893; ENSP00000419026; ENSG00000196730 [P53355-4]
ENST00000622514; ENSP00000484267; ENSG00000196730 [P53355-1]
GeneIDi1612
KEGGihsa:1612
UCSCiuc004apc.5 human [P53355-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1612
DisGeNETi1612
EuPathDBiHostDB:ENSG00000196730.12

GeneCards: human genes, protein and diseases

More...
GeneCardsi
DAPK1
HGNCiHGNC:2674 DAPK1
HPAiCAB037302
HPA040472
HPA048436
MIMi600831 gene
neXtProtiNX_P53355
OpenTargetsiENSG00000196730
PharmGKBiPA27142

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0032 Eukaryota
ENOG410XRMJ LUCA
GeneTreeiENSGT00940000153424
HOGENOMiHOG000082489
HOVERGENiHBG051296
InParanoidiP53355
KOiK08803
OMAiNTMGGYR
OrthoDBi981551at2759
PhylomeDBiP53355
TreeFamiTF314166

Enzyme and pathway databases

BRENDAi2.7.11.1 2681
ReactomeiR-HSA-418889 Caspase activation via Dependence Receptors in the absence of ligand
SignaLinkiP53355
SIGNORiP53355

Miscellaneous databases

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

More...
ChiTaRSi
DAPK1 human
EvolutionaryTraceiP53355

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
DAPK1

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

More...
GenomeRNAii
1612

Protein Ontology

More...
PROi
PR:P53355

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000196730 Expressed in 212 organ(s), highest expression level in amniotic fluid
CleanExiHS_DAPK1
ExpressionAtlasiP53355 baseline and differential
GenevisibleiP53355 HS

Family and domain databases

CDDicd00204 ANK, 3 hits
Gene3Di1.25.40.20, 2 hits
InterProiView protein in InterPro
IPR002110 Ankyrin_rpt
IPR020683 Ankyrin_rpt-contain_dom
IPR036770 Ankyrin_rpt-contain_sf
IPR020676 DAPK1
IPR011029 DEATH-like_dom_sf
IPR000488 Death_domain
IPR011009 Kinase-like_dom_sf
IPR027417 P-loop_NTPase
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR020859 ROC_dom
IPR008271 Ser/Thr_kinase_AS
PANTHERiPTHR44619 PTHR44619, 1 hit
PfamiView protein in Pfam
PF00023 Ank, 1 hit
PF12796 Ank_2, 2 hits
PF00531 Death, 1 hit
PF00069 Pkinase, 1 hit
PRINTSiPR01415 ANKYRIN
SMARTiView protein in SMART
SM00248 ANK, 9 hits
SM00005 DEATH, 1 hit
SM00220 S_TKc, 1 hit
SUPFAMiSSF47986 SSF47986, 1 hit
SSF48403 SSF48403, 1 hit
SSF52540 SSF52540, 1 hit
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS50297 ANK_REP_REGION, 1 hit
PS50088 ANK_REPEAT, 7 hits
PS50017 DEATH_DOMAIN, 1 hit
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit
PS51424 ROC, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiDAPK1_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: P53355
Secondary accession number(s): B7ZLD2
, B7ZLE7, Q14CQ7, Q1W5W0, Q68CP8, Q6ZRZ3, Q9BTL8
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 11, 2011
Last modified: January 16, 2019
This is version 205 of the entry and version 6 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 chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  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 entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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