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DAPK2 (death-associated protein kinase 2)

Written2016-04Mafalda Pinto, Valdemar Máximo
IPATIMUP Institute of Molecular Pathology and Immunology of the University of Porto, (MP, VM); I3S Institute for Innovation and Health Research, University of Porto (MP, VM); Department of Pathology and Oncology, Medical Faculty of the University of Porto, Porto, Portugal (VM) mafaldap@ipatimup.pt; vmaximo@ipatimup.pt

Abstract Short communication on DAPK2, with data on DNA and on the protein encoded.

Keywords DAPK2; DRP1; DRP-1; calcium/calmodulin; serine/threonine; kinase; apoptosis

(Note : for Links provided by Atlas : click)

Identity

Alias_symbol (synonym)DRP-1
MGC119312
Other aliasDRP1
DAP-kinase 2
DAP-kinase-related protein 1
DAP-kinase-related Protein 1 Beta Isoform
EC 2.7.11.1
HGNC (Hugo) DAPK2
LocusID (NCBI) 23604
Atlas_Id 40263
Location 15q22.31  [Link to chromosome band 15q22]
Location_base_pair Starts at 64199235 and ends at 64338521 bp from pter ( according to hg19-Feb_2009)  [Mapping DAPK2.png]

DNA/RNA

Note DAPK2 is a gene that codes for a protein that belongs to the serine/threonine protein kinase family.
 
  Blue highlighting indicates alternating exons; Red highlighting indicates amino acids encoded across a splice junction.
Transcription DPAK2 has 13 transcripts (3 coding), 75 orthologues and 11 paralogues (MYLK4, MYLK3, STK17A, DAPK3, DAPK1, OBSCN, SPEG, TTN, MYLK, STK17B, MYKL2) (ENSG00000035664).

Protein

 
  Schematic diagram of DAPK2 protein structure. The 42 KDa DAPK2 protein kinase bears three domain structures. A kinase domain on its N-terminal region determines specificity and allows for homodimerization through its basic loop. It is followed by a calcium/calmodulin (CaM)-regulated Serine/Threonine binding domain, which dictates kinase catalytic activity by unblocking substrate access when bound to Ca2+/CaM. Autophosphorylation of S308 decreases DAPK2 activity. The C-terminal dimerization domain allows for homodimerization. (Kawai T et al., 1999; Inbal B et al., 2000)
Description DAPK2 encodes a 42 KDa protein kinase (Inbal B., 2000) that belongs to the serine/threonine protein family of five proapoptotic proteins with tumor suppressor activity. DAPK2 is soluble and cytosolic (Inbal B., 2000). It contains highly-conserved N-terminal kinase catalytic domain, followed by a conserved calcium/calmodulin regulatory binding domain and a C-terminal homodimerization domain encompassing the last 40 aminoacids, predicted to form two helices, which has no sequence homology to known protein sequences.
Autophosphorylation restrains the apoptotic activity of DAPK2 kinase by controlling dimerization and calmodulin binding (Shani G et al., 2001).
DAPK2 is a monomer in its activated state and a homodimer when inhibited by autophosphorylation at Ser-308 (Shani G et al., 2001). The dimers of DAPK2 are formed through the association of two opposed catalytic domains (Patel AK et al., 2001). DAPK2 is negatively regulated by the autoinhibitory CaM-binding domain and this inhibition is removed by the binding of Ca2+/CaM (Inbal B et al., 2000). That is, DAPK2 is activated by CaM in response to Ca2+ stimuli, and regulated by a double locking mechanism. DAPK2 is dephosphorylated at Ser-308 in response to activated Fas and TNF-alpha receptors.
UniProtKB: Q9UIK4
 
  Translation (370 aa)
Expression Widespread expression. Strong expression in heart, lung and skeletal muscle, but also expressed in colon, breast, spleen tissue and leukocytes (Kawai T et al., 1999; Inbal B et al., 2000). In mouse, DAPK2 is strongly and specifically expressed in interstitial cells of the kidney cortex (Guay JA et al., 2014).
Localisation Cytoplasm (Inbal B et al., 2000), cytoplasmic vesicles, inside autophagic vesicles (Inbal B et al., 2002).
Function DAPK2 is a regulator of apoptosis, autophagy and inflammation (Geering B 2015).

Apoptosis
DAPK2 overexpression induces cell apoptosis in 50 to 60% (Inbal B et al., 2000). Depletion of the C-terminal tail of DAPK2 abolishes its apoptotic activity, while further truncation of the CaM-regulatory domain strongly enhances its apoptotic effect (Inbal B et al., 2000).
DAPK2 is a modulator of TRAIL signaling and TRAIL-induced apoptosis. Genetic ablation of DAPK2 causes phosphorylation of NF-KB and its transcriptional activity in several cancer cell lines, leading to the induction of several proapoptotic proteins (TNFRSF10A (DR4) and TNFRSF10B (DR5)) (Schlegel CR et al., 2014).

Autophagy
DAPK2 modulates MTOR activity by directly interacting and phosphorylating mTORC1. This way it suppresses mTOR activity to promote autophagy induction and autophagy levels under stress and steady-state conditions (Ber Y et al., 2015).
Expression of DAPK2 in its activated form triggers autophagy in a caspase independent way. DAPK2 mediates the formation of autophagic vesicles during apoptosis (Inbal B et al., 2002). Expression of dominant negative mutant of DAPK2 reduces autophagy (Inbal B et al., 2002).

Protein serine/threonine kinase activity
In vitro kinase assays, using myosin light chain (MLC) as substrate, have shown both MLC phosphorylation and DAPK2 autophosphorylation (Kawai T et al., 1999; Inbal B et al., 2000). DAPK2 functions in vitro as a kinase that is capable of phosphorylating itself and an external substrate (Kawai T et al., 1999; Inbal B et al., 2000).

Calmodulin binding
The addition of Ca2+/CaM to in vitro kinase assays using myosin light chain (MLC) as substrate, lead to an increased amount of phosphorylated MLC, suggesting that DPK2 is regulated by binding to CaM (Kawai T et al., 1999; Inbal B et al., 2000). DPAK2 is negatively regulated by the autoinhibitory CaM-binding domain and this inhibition is removed by the binding of Ca2+/CaM (Inbal B et al., 2000).
Truncation of the CaM-regulatory region of DAPK2 enhances the apoptotic effect (Inbal B et al., 2000). Oxidative stress regulation
DAPK2 regulates oxidative stress in cancer cells by preserving mitochondrial function. Depletion of DAPK2 leads to an increased production of mitochondrial superoxide anions and increased oxidative stress (Schlegel CR et al., 2015).

Cellular metabolism
DAPK2 kinase domain in important to maintain mitochondrial integrity and thus metabolism. Depletion of DPAK2 leads to metabolic alterations, decreased rate of oxidative phosphorylation and destabilized mitochondrial membrane potential (Schlegel CR et al., 2015). Membrane blebbing
Interaction of DAPK2 with ACTA1 (α-actin-1) at the plasma membrane leads to massive membrane blebbing (Geering B et al., 2015). Expression of DAPK2 in its activated form triggers membrane blebbing and this process is caspase independent (Inbal B et al., 2002). Dominant negative mutants of DAPK2 reduce membrane blebbing during the p55/TRAF1 (TNF-receptor 1)-induced apoptosis (Inbal B et al., 2002).

Motility
Interaction of DAPK2 with α-actin-1 leads to reduced cellular motility (Geering B et al., 2015).

Intracellular signaling transduction
Depletion of DAPK2 leads to the activation of classical stress-activated kinases, such as ERK, JNK and p38 (Schlegel CR et al., 2015).

Positive regulation of eosinophil and neutrophil chemotaxis, and granulocyte maturation
DPAK2 inhibition blocks recruitment of neutrophils to the site of inflammation in a peritonitis mouse model. DAPK2 functions in a signaling pathway that mediates motility in neutrophils and eosinophils in response to intermediary chemoattractants, but not to end-target chemoattractants (Geering B et al., 2014).
DPAK2 regulates granulocytic motility by controlling cell spreading and polarization (Geering B et al., 2014) and may play a role in granulocyte maturation (Rizzi M et al., 2007).

Regulation of erythropoiesis
Among hematopoietic lineages, DPAK2 is expressed predominantly in erythroid cells. DPAK2 is substantially up-modulated during late erythropoiesis (Fang J et al., 2008). In UT7epo cells, siRNA knock-down of DAPK2 enhanced survival due to cytokine withdrawal, and DAPK2's phosphorylation and kinase activity also were erythropoietin (EPO)-modulated. DAPK2 therefore comprises a new candidate attenuator of stress erythropoiesis (Fang J et al., 2008).

The physiological substrate of DAPK2 is unknown although it is known to phosphorylate the myosin light chain in vitro (Inbal B et al., 2000).

INTERACTION
YWHAB (14-3-3-β) (Yuasa K et al., 2015) and α-actinin-1 are novel DAPK2 binding partners (Geering B et al., 2015). The interaction of DAPK2 with α-actinin-1 is localized to the plasma membrane, resulting in massive membrane blebbing and reduced cellular motility, whereas the interaction of DAPK2 with 14-3-3- β is localized to the cytoplasm, with no impact on blebbing, motility, or viability (Geering B et al 2015). 14-3-3- proteins inhibit DAPK2 activity and its apoptotic effects (Yuasa K et al., 2015).
DAPK2 also interacts with RAD1, MAPK1 and MLC1 (Steinmann S et al., 2015).

Homology DAPK3/ZIPK/DLK (Death-related protein 1); STK17A (DRAK1/STK17B (DRAK2) (DAPK-related apoptosis inducing protein kinases 1 and 2) (Shobat G et al., 2002)

Mutations

Germinal No germline or somatic mutations have been described for DAPK2 gene. There are 4 structural variants are described for DPAK2 gene: nsv1567 and nsv1569 leading to loss (PubMed ID 18451855), and nsv1568 and esv1414761 leading to insertions (PubMed IDs 18451855 and 17803354, respectively) (Database of Genomic Variants).
Somatic Hypermethylation of the promoter region downregulates DAPK2 expression.

Implicated in

Note
  
Entity Hematological malignancies
Note DAPK2 is a tumor suppressor gene. Promoter region hypermethylation is one mechanism of DAPK2 inactivation in Hodgkin lymphoma-derived tumor cell lines (Tur MK et al., 2009).
DAPK2 is up-regulated during normal myeloid differentiation and enhances neutrophil maturation in myeloid leukemic cells (Rizzi M et al., 2007).
Acute promyelocytic leukemia (APL) patients have particularly low levels of DAPK2, where the predominant lesion causing its transcriptional repression isPML-RARA. and SPI1 (PU.1) bind to binding sites in the DAPK2 promoter. Restoring DAPK2 expression can rescue neutrophil differentiation (Humbert M. et al., 2014).
Low DAPK2 expression is associated with CEBPA-mutated AML patients and Humbert et al have found that DAPK2 is induced by the myeloid transcription factors PU.1 and CEBPA during granulocyte differentiation but repressed by PML-RARA in APL patients (Humbert M. et al., 2014).
CEBPA-dependent regulation of DAPK2 during APL differentiation (Humbert M. et al., 2014).
  
  
Entity
Note DAPK2 expression is regulated by MIR520H in breast cancer cells (Su CM. et al., 2016).
  
  
Entity Obesity
Note DAPK2 regulates obesity-related attenuated autophagy in adipocytes – DAPK2 downregulation associates with attenuated adipocyte autophagic clearance in human obesity (Soussi H et al., 2015).
  

Bibliography

DAPK2 is a novel regulator of mTORC1 activity and autophagy
Ber Y, Shiloh R, Gilad Y, Degani N, Bialik S, Kimchi A
Cell Death Differ 2015 Mar;22(3):465-75
PMID 25361081
 
Attenuation of EPO-dependent erythroblast formation by death-associated protein kinase-2
Fang J, Menon M, Zhang D, Torbett B, Oxburgh L, Tschan M, Houde E, Wojchowski DM
Blood 2008 Aug 1;112(3):886-90
PMID 18535204
 
Death-associated protein kinase 2: Regulator of apoptosis, autophagy and inflammation
Geering B
Int J Biochem Cell Biol 2015 Aug;65:151-4
PMID 26055515
 
DAPK2 positively regulates motility of neutrophils and eosinophils in response to intermediary chemoattractants
Geering B, Stoeckle C, Rozman S, Oberson K, Benarafa C, Simon HU
J Leukoc Biol 2014 Feb;95(2):293-303
PMID 24163421
 
Identification of Novel Death-Associated Protein Kinase 2 Interaction Partners by Proteomic Screening Coupled with Bimolecular Fluorescence Complementation
Geering B, Zokouri Z, Hürlemann S, Gerrits B, Ausländer D, Britschgi A, Tschan MP, Simon HU, Fussenegger M
Mol Cell Biol 2015 Oct 19;36(1):132-43
PMID 26483415
 
Death associated protein kinase 2 is expressed in cortical interstitial cells of the mouse kidney
Guay JA, Wojchowski DM, Fang J, Oxburgh L
BMC Res Notes 2014 Jun 7;7:345
PMID 24906443
 
The tumor suppressor gene DAPK2 is induced by the myeloid transcription factors PU
Humbert M, Federzoni EA, Britschgi A, Schläfli AM, Valk PJ, Kaufmann T, Haferlach T, Behre G, Simon HU, Torbett BE, Fey MF, Tschan MP
1 and C/EBPα during granulocytic differentiation but repressed by PML-RARα in APL J Leukoc Biol
PMID 24038216
 
DAP kinase and DRP-1 mediate membrane blebbing and the formation of autophagic vesicles during programmed cell death
Inbal B, Bialik S, Sabanay I, Shani G, Kimchi A
J Cell Biol 2002 Apr 29;157(3):455-68
PMID 11980920
 
Death-associated protein kinase-related protein 1, a novel serine/threonine kinase involved in apoptosis
Inbal B, Shani G, Cohen O, Kissil JL, Kimchi A
Mol Cell Biol 2000 Feb;20(3):1044-54
PMID 10629061
 
Death-associated protein kinase 2 is a new calcium/calmodulin-dependent protein kinase that signals apoptosis through its catalytic activity
Kawai T, Nomura F, Hoshino K, Copeland NG, Gilbert DJ, Jenkins NA, Akira S
Oncogene 1999 Jun 10;18(23):3471-80
PMID 10376525
 
Structure of the dimeric autoinhibited conformation of DAPK2, a pro-apoptotic protein kinase
Patel AK, Yadav RP, Majava V, Kursula I, Kursula P
J Mol Biol 2011 Jun 10;409(3):369-83
PMID 21497605
 
The death-associated protein kinase 2 is up-regulated during normal myeloid differentiation and enhances neutrophil maturation in myeloid leukemic cells
Rizzi M, Tschan MP, Britschgi C, Britschgi A, HĂĽgli B, Grob TJ, Leupin N, Mueller BU, Simon HU, Ziemiecki A, Torbett BE, Fey MF, Tobler A
J Leukoc Biol 2007 Jun;81(6):1599-608
PMID 17347302
 
DAPK2 regulates oxidative stress in cancer cells by preserving mitochondrial function
Schlegel CR, Georgiou ML, Misterek MB, Stöcker S, Chater ER, Munro CE, Pardo OE, Seckl MJ, Costa-Pereira AP
Cell Death Dis 2015 Mar 5;6:e1671
PMID 25741596
 
Autophosphorylation restrains the apoptotic activity of DRP-1 kinase by controlling dimerization and calmodulin binding
Shani G, Henis-Korenblit S, Jona G, Gileadi O, Eisenstein M, Ziv T, Admon A, Kimchi A
EMBO J 2001 Mar 1;20(5):1099-113
PMID 11230133
 
The DAP-kinase family of proteins: study of a novel group of calcium-regulated death-promoting kinases
Shohat G, Shani G, Eisenstein M, Kimchi A
Biochim Biophys Acta 2002 Nov 4;1600(1-2):45-50
PMID 12445458
 
DAPK2 Downregulation Associates With Attenuated Adipocyte Autophagic Clearance in Human Obesity
Soussi H, Reggio S, Alili R, Prado C, Mutel S, Pini M, Rouault C, Clément K, Dugail I
Diabetes 2015 Oct;64(10):3452-63
PMID 26038578
 
Death-associated protein kinase: A molecule with functional antagonistic duality and a potential role in inflammatory bowel disease (Review)
Steinmann S, Scheibe K, Erlenbach-Wuensch K, Neufert C, Schneider-Stock R
Int J Oncol 2015 Jul;47(1):5-15
PMID 25963636
 
miR-520h is crucial for DAPK2 regulation and breast cancer progression
Su CM, Wang MY, Hong CC, Chen HA, Su YH, Wu CH, Huang MT, Chang YW, Jiang SS, Sung SY, Chang JY, Chen LT, Chen PS, Su JL
Oncogene 2016 Mar 3;35(9):1134-42
PMID 25982274
 
Targeted restoration of down-regulated DAPK2 tumor suppressor activity induces apoptosis in Hodgkin lymphoma cells
Tur MK, Neef I, Jost E, Galm O, Jäger G, Stöcker M, Ribbert M, Osieka R, Klinge U, Barth S
J Immunother 2009 Jun;32(5):431-41
PMID 19609235
 
Suppression of death-associated protein kinase 2 by interaction with 14-3-3 proteins
Yuasa K, Ota R, Matsuda S, Isshiki K, Inoue M, Tsuji A
Biochem Biophys Res Commun 2015 Aug 14;464(1):70-5
PMID 26047703
 

Citation

This paper should be referenced as such :
Pinto M, Máximo V
DAPK2 (death-associated protein kinase 2);
Atlas Genet Cytogenet Oncol Haematol. in press
On line version : http://AtlasGeneticsOncology.org/Genes/DAPK2ID40263ch15q22.html


External links

Nomenclature
HGNC (Hugo)DAPK2   2675
Cards
AtlasDAPK2ID40263ch15q22
Entrez_Gene (NCBI)DAPK2  23604  death-associated protein kinase 2
AliasesDRP-1; DRP1
GeneCards (Weizmann)DAPK2
Ensembl hg19 (Hinxton)ENSG00000035664 [Gene_View]  chr15:64199235-64338521 [Contig_View]  DAPK2 [Vega]
Ensembl hg38 (Hinxton)ENSG00000035664 [Gene_View]  chr15:64199235-64338521 [Contig_View]  DAPK2 [Vega]
ICGC DataPortalENSG00000035664
TCGA cBioPortalDAPK2
AceView (NCBI)DAPK2
Genatlas (Paris)DAPK2
WikiGenes23604
SOURCE (Princeton)DAPK2
Genetics Home Reference (NIH)DAPK2
Genomic and cartography
GoldenPath hg19 (UCSC)DAPK2  -     chr15:64199235-64338521 -  15q22.1   [Description]    (hg19-Feb_2009)
GoldenPath hg38 (UCSC)DAPK2  -     15q22.1   [Description]    (hg38-Dec_2013)
EnsemblDAPK2 - 15q22.1 [CytoView hg19]  DAPK2 - 15q22.1 [CytoView hg38]
Mapping of homologs : NCBIDAPK2 [Mapview hg19]  DAPK2 [Mapview hg38]
OMIM616567   
Gene and transcription
Genbank (Entrez)AB018001 AF052941 AK026801 AK094290 AK310967
RefSeq transcript (Entrez)NM_014326
RefSeq genomic (Entrez)NC_000015 NC_018926 NT_010194 NW_004929398
Consensus coding sequences : CCDS (NCBI)DAPK2
Cluster EST : UnigeneHs.237886 [ NCBI ]
CGAP (NCI)Hs.237886
Alternative Splicing GalleryENSG00000035664
Gene ExpressionDAPK2 [ NCBI-GEO ]   DAPK2 [ EBI - ARRAY_EXPRESS ]   DAPK2 [ SEEK ]   DAPK2 [ MEM ]
Gene Expression Viewer (FireBrowse)DAPK2 [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)23604
GTEX Portal (Tissue expression)DAPK2
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ9UIK4   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ9UIK4  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ9UIK4
Splice isoforms : SwissVarQ9UIK4
PhosPhoSitePlusQ9UIK4
Domaine pattern : Prosite (Expaxy)PROTEIN_KINASE_ATP (PS00107)    PROTEIN_KINASE_DOM (PS50011)    PROTEIN_KINASE_ST (PS00108)   
Domains : Interpro (EBI)Ca/CaM-dep_Ca-dep_prot_Kinase    Kinase-like_dom    Prot_kinase_dom    Protein_kinase_ATP_BS    Ser/Thr_dual-sp_kinase    Ser/Thr_kinase_AS   
Domain families : Pfam (Sanger)Pkinase (PF00069)   
Domain families : Pfam (NCBI)pfam00069   
Domain families : Smart (EMBL)S_TKc (SM00220)  
Conserved Domain (NCBI)DAPK2
DMDM Disease mutations23604
Blocks (Seattle)DAPK2
PDB (SRS)1WMK    1WRZ    1Z9X    1ZUZ    1ZWS    2A27    2A2A    2CKE   
PDB (PDBSum)1WMK    1WRZ    1Z9X    1ZUZ    1ZWS    2A27    2A2A    2CKE   
PDB (IMB)1WMK    1WRZ    1Z9X    1ZUZ    1ZWS    2A27    2A2A    2CKE   
PDB (RSDB)1WMK    1WRZ    1Z9X    1ZUZ    1ZWS    2A27    2A2A    2CKE   
Structural Biology KnowledgeBase1WMK    1WRZ    1Z9X    1ZUZ    1ZWS    2A27    2A2A    2CKE   
SCOP (Structural Classification of Proteins)1WMK    1WRZ    1Z9X    1ZUZ    1ZWS    2A27    2A2A    2CKE   
CATH (Classification of proteins structures)1WMK    1WRZ    1Z9X    1ZUZ    1ZWS    2A27    2A2A    2CKE   
SuperfamilyQ9UIK4
Human Protein AtlasENSG00000035664
Peptide AtlasQ9UIK4
HPRD09905
IPIIPI00033388   IPI00746243   
Protein Interaction databases
DIP (DOE-UCLA)Q9UIK4
IntAct (EBI)Q9UIK4
FunCoupENSG00000035664
BioGRIDDAPK2
STRING (EMBL)DAPK2
ZODIACDAPK2
Ontologies - Pathways
QuickGOQ9UIK4
Ontology : AmiGOprotein serine/threonine kinase activity  protein binding  calmodulin binding  ATP binding  cytoplasm  protein phosphorylation  apoptotic process  regulation of autophagy  cytoplasmic vesicle  autophagosome lumen  intracellular signal transduction  identical protein binding  regulation of apoptotic process  anoikis  protein autophosphorylation  positive regulation of neutrophil chemotaxis  neutrophil migration  positive regulation of eosinophil chemotaxis  regulation of intrinsic apoptotic signaling pathway  
Ontology : EGO-EBIprotein serine/threonine kinase activity  protein binding  calmodulin binding  ATP binding  cytoplasm  protein phosphorylation  apoptotic process  regulation of autophagy  cytoplasmic vesicle  autophagosome lumen  intracellular signal transduction  identical protein binding  regulation of apoptotic process  anoikis  protein autophosphorylation  positive regulation of neutrophil chemotaxis  neutrophil migration  positive regulation of eosinophil chemotaxis  regulation of intrinsic apoptotic signaling pathway  
Pathways : KEGGPathways in cancer    Bladder cancer   
REACTOMEQ9UIK4 [protein]
REACTOME Pathways418889 [pathway]   
NDEx NetworkDAPK2
Atlas of Cancer Signalling NetworkDAPK2
Wikipedia pathwaysDAPK2
Orthology - Evolution
OrthoDB23604
GeneTree (enSembl)ENSG00000035664
Phylogenetic Trees/Animal Genes : TreeFamDAPK2
HOVERGENQ9UIK4
HOGENOMQ9UIK4
Homologs : HomoloGeneDAPK2
Homology/Alignments : Family Browser (UCSC)DAPK2
Gene fusions - Rearrangements
Fusion : MitelmanHERC1/DAPK2 [15q22.31/15q22.31]  [t(15;15)(q22;q22)]  
Fusion: TCGAHERC1 15q22.31 DAPK2 15q22.31 BLCA BRCA
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerDAPK2 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)DAPK2
dbVarDAPK2
ClinVarDAPK2
1000_GenomesDAPK2 
Exome Variant ServerDAPK2
ExAC (Exome Aggregation Consortium)DAPK2 (select the gene name)
Genetic variants : HAPMAP23604
Genomic Variants (DGV)DAPK2 [DGVbeta]
DECIPHER (Syndromes)15:64199235-64338521  ENSG00000035664
CONAN: Copy Number AnalysisDAPK2 
Mutations
ICGC Data PortalDAPK2 
TCGA Data PortalDAPK2 
Broad Tumor PortalDAPK2
OASIS PortalDAPK2 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICDAPK2  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDDAPK2
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch DAPK2
DgiDB (Drug Gene Interaction Database)DAPK2
DoCM (Curated mutations)DAPK2 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)DAPK2 (select a term)
intoGenDAPK2
NCG5 (London)DAPK2
Cancer3DDAPK2(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM616567   
Orphanet
MedgenDAPK2
Genetic Testing Registry DAPK2
NextProtQ9UIK4 [Medical]
TSGene23604
GENETestsDAPK2
Huge Navigator DAPK2 [HugePedia]
snp3D : Map Gene to Disease23604
BioCentury BCIQDAPK2
ClinGenDAPK2
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD23604
Chemical/Pharm GKB GenePA27143
Clinical trialDAPK2
Miscellaneous
canSAR (ICR)DAPK2 (select the gene name)
Probes
Litterature
PubMed30 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineDAPK2
EVEXDAPK2
GoPubMedDAPK2
iHOPDAPK2
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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