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DOCK1 (Dedicator of cytokinesis 1)

Written2015-03Ping Li, Fung Zhao, Annie N. Cheung
Departments of Pathology, the University of Hong Kong Shenzhen Hospital, Shenzhen (PL, ANC),, The University of Hong Kong, Hong Kong (FZ, AC), China

Abstract Dedicator of cytokinesis (DOCK) is a family of proteins with 11 members in mammal which can regulate cell motility, phagocytosis, myoblast fusion, tumor suppression, neuronal polarization and adhesion. They are classified into four subfamilies A to D. Dock1 (Dock180), the founding member of the family, is a large protein which includes an N-terminal SH3 domain and a flanking helical bundle that are vital to the formation of a functioning complex Dock1-ELMO1 (Gumienny et al.,2001; Grimsley et al.,2004; Komander et al., 2008). Genetic and biochemical studies show that DOCK1 acts as a guanine-nucleotide exchange factor (GEF) for the small GTPase Rac1 (Diyokawa et al., 1998; Nolan et al., 1998). Rac1 is a small GTPase required for myoblast fusion in organisms such as fruit flies, zebrafish and mice (Rochlin et al., 1998). In addition to playing an important role in a broad spectrum of biological processes, numerous studies have demonstrated contributions of DOCK members to the development of cancer. Deciphering the detailed mechanisms by which DOCK proteins participate in tumorigenesis will shed light on the design of new treatment strategies.

Keywords DOCK1

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Identity

Alias_namesdedicator of cyto-kinesis 1
Alias_symbol (synonym)DOCK180
ced5
Other aliasDOCK 180
HGNC (Hugo) DOCK1
LocusID (NCBI) 1793
Atlas_Id 40354
Location 10q26.13-q26.3  [Link to chromosome band 10q26]
Location_base_pair Starts at 126905409 and ends at 127452517 bp from pter ( according to hg19-Feb_2009)  [Mapping DOCK1.png]
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
C3 (19p13.3) / DOCK1 (10q26.2)DOCK1 (10q26.2) / APBA1 (9q21.11)DOCK1 (10q26.2) / APBA1 (9q21.12)
DOCK1 (10q26.2) / DOCK1 (10q26.2)DOCK1 (10q26.2) / DPCD (10q24.32)DOCK1 (10q26.2) / MGMT (10q26.3)
DOCK1 (10q26.2) / PCDH15 (10q21.1)DOCK1 (10q26.2) / PLPP4 (10q26.12)DOCK1 (10q26.2) / TFDP2 (3q23)
FUOM (10q26.3) / DOCK1 (10q26.2)GALNT16 (14q24.1) / DOCK1 (10q26.2)TTC21B (2q24.3) / DOCK1 (10q26.2)

DNA/RNA

Description The DOCK1 gene is 6797 base pairs in length encoding a large protein (about 180kDa).
Transcription Variant (1) represents the longer transcript and encodes the longer isoform (1). Variant (2) uses an alternate splice site at an internal exon, compared to variant 1. The encoded isoform (2) is shorter, compared to isoform 1.

Protein

 
  "This research was originally published in Journal of Biological Chemistry. Premkumar L, et al. Structural basis of membrane targeting by the DOCK180 family of Rho family guanine exchange factors (Rho-GEFs). J Biol Chem. 2010, 23; 285(17):13211-22. copyright the American Society for Biochemistry and Molecular Biology." (Premkumar L et al., 2010)
Description Dock1 is a 180 kDa protein and largely responsible for regulating Rac-mediated polarization, migration, phagocytosis of apoptotic cells, myoblasts fusion and macrophages in vitro (Cte etal., 2005; Grimsley etal., 2004; Pajcini et al., 2008) DOCK1 and its homologues in Drosophila (Myoblast city) and C.elegans (CED-5) represent an evolutionarily conserved family of proteins which is called CDM (CED-5, DOCK180, MBC)-family (Wu and Horvitz, 1998). DOCK1 has 6 splice variants with two protein-coding transcripts generating products consisting of 1865 and 1886 amino acids respectively. The others are non-protein-coding transcripts. An SH3 domain at the A- terminus and two domain CRK-binding sequences at the carboxyl end have been identified in Dock1 (Hideki Hasegawa et al, 1996). There are two high sequence homology named DHR-1 and DHR-2 among Dock family members (Jean Francois Cote and Kristiina Vuori, 2002). DHR1 domain is 200-250 amino acids long that binds phospholipids, whereas DHR2 domain of 450-550 amino acids is responsible for the guanine nucleotide exchange activity (25022758). DHR domain DOCK1 and its homologues in Drosophila (Myoblast city) and C.elegans (CED-5) represent an evolutionarily conserved family of proteins which is called CDM (CED-5, DOCK180, MBC)-family(Wu and Horvitz, 1998). This family is one of the GEFs being identified as activators of Rho GTPases (Takai etal., 1996; Hasegawa et al., 1996; Erickson and Cerione, 2004). The other family is Db1 family (Hart et al., 1991) and all their members contain the Db1 Homology (DH) and the Pleckstrin Homology (PH) domains (Klinger et al., 2004; Srivastava et al., 1986; Worthylake te al., 2004; Feng et al.,2002; Baird et al., 2005). While DH domains directly catalyze GDP-GTP exchange, PH domains target proteins to membranes and mediate protein-protein interactions. DOCK 180-related proteins can catalyze nucleotide exchange without homology to DH/PH domains, which are characterized by two protein domains named DOCK homology regions 1 and 2 (DHR-1 and DHR-2, respectively) (Brugnera et al., 2002; Cote and Vuori, 2002). DOCK1 contains 1864 amino acids, a Src-homology 3 (SH3) domain at the amino terminus, a few proline-rich motifs at the carboxyl terminus and a potential phosphatidylinositol trisphosphate (PtdInsP3)-interacting motif near its C terminus (Hasegawa et al.m 1996; Kobayashi et al 2001). Inactivation of the DHR-2 (also known as CZH2 or DOCKER) in DOCK1 can inhibit Rac activation, cell migration and clearance of apoptotic cells. This demonstrates the necessity and sufficiency of DHR-2 to promote GDP/GTP exchange on various GTPases. DHR-2 has been suggested to consist of about 500 residues (Brugnera et al., 2002; Cote and Vuori, 2002). DHR-2 domains of these family members have been shown to interact with the nucleotide-free form of Rho GTPase leading to the exchange of GDP for GTP(Meller et al., 2004; Lin et al., 2006; Miyamoto et al., 2006; Nishikimi et al 2005). DHR-1 domain (also known as CZH1) is located upstream of DHR-2 domain (Meller et al., 2002) and is a novel PtdIns (3,4,5)P3-binding module which directly interacts with phosphoinositides (PI),playing an important role in Rac-mediated cell polarity and migration including myoblast fusion(Cote and Vuori, 2002).
SH3 domains src-homology3 (SH3) domains are protein-protein interaction modules in intracellular signal transduction. DOCK1 contains an SH3 domain at its N-terminus. SH3 domains have been reported to bind to a proline-finch motif at the C-terminus of ELMO (gumienny et al., 2001) which will be regulating the activation status of DOCK1. In DOCK1, SH3 domain interacts with DHR-2 domain directly which is dependent on a proline-rich region in DHR-2 domain, but inhibits some functions of the DHR-2 domain, such as binding to nucleotide-free Rac and facilitating GTP loading(Lu et al., 2005).
Interaction with ELMO ELMO is an evolutionarily conserved upstream regulator of Rac that takes effect at the same step as DOCK 1 in phagocytosis of apoptotic cells and cell migration (Gumienny et al., 2001). DOCK2-5 and DOCK 1 have an amino-terminal Src homology (SH)-3 domain which can interact with ELMO proteins and cooperate to activate Rac (Grimsley et al., 2004; Hiramoto et al., 2006). Other Dock-related proteins such as DOCK 6-8 and DOCK9-11 cannot physically interact with ELMO proteins due to the lack of a recognizable SH3 domain. Some studies showed that deletion mutants of DOCK 180 that fail to bind to ELMO could not efficiently activate Rac even when over-expressed in cells (Grimsley et al., 2004). Other studies suggested that owing to auto-inhibition, the isolated DHR-2 appears to have much higher GEF activity than total DOCK 180 (Lu et al., 2005; Cote et al., 2007). Co-expression of ELMO is required to relieve the auto-inhibited state (Lu et al., 2004; Santy et al., 2005). The ELMO-DOCK1 complex is located in the cytoplasm and will be translocated to the cell membrane, which is the key step for DOCK1 to activate Rac (Debakker et al., 2004; Katoh and Negishi et al., 2003; Hasegawa et al., 1996; Katoh et al., 2006). All three mammalian ELMO 1-3 proteins have no obvious catalytic activity. They have three recognizable features including armadillo repeats at the N-terminus, an atypical PH domain and a complex prolin-rich region at the C-terminus. In fact, the functions of ELMO proteins in mediating Rac signaling remain largely unknown, and the interaction between ELMO and DOCK is still unclear. Some data indicate that there are two contact regions between DOCK1 and ELMO1. The atypical ELMO1 PH domain and an uncharacterized region between the SH3 and DHR-1 domains primarily interact with each other. This interaction is sufficient to promote complex formation. N-terminal SH3 domain of DOCK1 and the C-terminal PxxP motifs of ELMO1 are involved in the second contact (Komander et al., 2008). The PH domain and proline-rich motifs are implicated in binding to DOCK protein (Manishha et al., 2011). It has been documented that the SH3 domain of DOCK1 binds to a proline-rich (pro-rich) motif at the C-terminus of ELMO, and this in turn would activate DOCK 1. This is the second interaction. So when either of these motifs is mutated, the interaction of ELMO and DOCK1 is completely interrupted (Gumienny et al., 2011; Lu et al., 2005). The PH domain of ELMO stabilizes the DOCK1-nucleotide-free Rac complex through binding "in trans" instead of interacting directly with either Rac or DOCK 180 (Lu et al, 2004). The atypical PH domain of ELMO plays a crucial role in increasing the catalytic activity of DOCK 180 towards Rac. ELMO1 or ELMO2, could coexpress with DOCK1, and overexpression of ELMO1 together with DOCK1 synergistically enhances phagocytosis(Zhou et al., 2001). ELMO PH domain could slightly enhance the catalytic activity of DOCK 1 toward Rac by about twofold in vitro. But this effect could be efficient in vivo because the Ced-12 PH domain mutations let Ced-12-null worms failed to rescue the migration defects (Lu et al., 2004). Therefore, the mechanism of action of Elmo remains inconclusive. Further studies are required to clarify the controversies.
Binding to Crk Crk is an adaptor protein consisting mostly of SH2 and SH3 domains which is also involved in signaling processes, such as cell adhesions, differentiation, migration, proliferation, and phagocytosis of apoptotic cells (Clark and Brugge, 1995; Juliano and Haskill, 1993; Richardson and Parsons, 1995). Crk gene can be translated into two proteins, Crk-I and Crk-II which are primarily isolated as oncogenic products (Mayer etal., 1988; Matsuda et al., 1992). DOCK180/DOCK1 can bind with the SH3 of the Crk through PxxP region in its C-termini (Matsuda et al., 1996). It has been shown that DOCK 1 has two C-terminal CRK-binding sequences. DOCK1 binds with Crk on the basis of a biochemical interaction. The complex will be transiently translocated to the membrane resulting in changes in cell morphology (Hasegawa et al., 1996).
Essential for myoblast fusion Mammalian myogenesis arises from the fusion of mononucleated myoblasts. Myogenic cells fuse with each other to form multinucleated myotubes (Horsley and Pavlath, 2004). Myoblast fusion is responsible for development during embryogenesis and postnatal maintenance, growth, and helps regenerate injured tissue (Cerletti et al.m 2008; Rudnicki et al., 2008). Proper regulation of myoblast fusion events determines myofiber length, appropriate contractile capacity and muscle function(Allen et al., 1999). In fact, the understanding of myoblast fusion of higher vertebrates remains poor. Current knowledge is largely derived from genetic analyses performed in Drosophila(Chen and Olson, 2004; Taylor, 2003) and in vivo experiments in vertebrates (Cote and Vuori, 2007). In Drosophila melanogaster, fusion-competent myoblasts and founder cells regulate the formation of multinucleate muscle fibers. At cellular level, the processes of myoblast fusion include alignment, actin cytoskeleton rearrangement at the contact sites and membrane fusion (Knudsen and Horwitz, 1977; Wakelam, 1985; Peckham, 2008; Duan and Gallagher, 2009). CDM superfamily consists of founding members such as MBC, human DOCK1, Caenorhabditis elegans CED-5 (Wu and Horvitz, 1998) and almost 20 additional members (Cote and Vuori, 2002). Myoblast city (mbc) is highly important in Drosophila melanogaster embryo for multinucleate fibers formation. It has been reported that Mbc together with ELMO, function as an atypical bipartite GEF to directly control Rac1 in vivo. Drosophila eye experiments show that Mbc and ELMO interaction will increase the activity of Ras (Gersbrecht et al., 2008).
Expression DOCK1 is predominantly located in the cytoplasm of cells. Nuclear localization of DOCK1 has also been reported (Zhao et al., 2011).
Function This family is one of the GEFs being identified as activators of Rho GTPases (Takai etal., 1996; Hasegawa et al., 1996; Erickson and Cerione, 2004). DOCK1 activates Rho GTPase through facilitating the exchange of bound GDP for GTP. GTPases can regulate actin cytoskeleton and be accountable for crucial biological functions, such as cell phagocytosis, cell migration, cell proliferation, cell survival, cell polarity, axonal guidance, transcription and intracellular trafficking (Iwasato et al., 2007; Schmidt and Hall, 2002). In addition to playing an important role in a broad spectrum of biological processes, numerous studies have demonstrated contribution of DOCK members to the development of cancer.
Homology In mammals, dedicator of cytokinesis (DOCK) represents a new family of proteins comprising 11 members named DOCK1 (also known as Dock180) to Dock11. They are classified into four subfamilies denoted Dock-A, -B, -C, -D. 11 members are classified as following: DOCK-A subfamily (DOCK1, DOCK2 and DOCK5); DOCK-B subfamily (DOCK3 and DOCK4); DOCK-C subfamily (DOCK6, DOCK7 and DOCK8); DOCK-D subfamily (DOCK9, DOCK10 and DOCK11) (Bridget Biersmith et al, 2011).

Implicated in

Note
  
Entity Breast cancer
Note Expression of DOCK1 correlates with poor survival for HER2+ and basal breast cancer patients (Eckhardt et al., 2012; Perou et al., 2000). Dock1 protein interacts with HER2 and enhances HER2-induced Rac activation and cell migration (Laurin et al., 2013).
  
  
Entity Glioblastoma
Note EGFR8, a constitutively active EGFR mutant, promotes glioma tumorigenesis and invasion through protein kinase A-dependent phosphorylation of DOCK1 (Feng H et al, 2014).
  
  
Entity Ovarian cancer
Note Correlation of high Dock1 expression with poor survival for patients has been reported. Dock1 overexpression contributes to enhanced ovarian cancer cell migration and invasion (Zhao F et al, 2011).
  
  
Entity Lung cancer
Note Dock1 can upregulate PTTG which could play a role in actin cytoskeleton remodeling, cell migration and induction of epithelial mesenchymal transition in lung cancer. The integrin alpha(V)beta(3)-FAK (focal adhesion kinase) signaling pathway is involved. (Shah PP et al, 2012).
  
  
Entity Gastric cancer
Note Among genes involved in extracellular signal-regulated kinase (ERK) downstream signaling pathways activated by Cytotoxin-associated antigen (CagA), a H. pylori immunoprotein, single nucleotide polymorphism of Dock1 was found to be significantly associated with risk of developing gastric cancer with marginal gene dose effects. (Yang JJ et al, 2011).
  

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Structure 2004 Jun;12(6):1078-86
PMID 15274927
 
C
Wu YC, Horvitz HR
elegans phagocytosis and cell-migration protein CED-5 is similar to human DOCK180 Nature
PMID 9548255
 
DOCK4, a GTPase activator, is disrupted during tumorigenesis
Yajnik V, Paulding C, Sordella R, McClatchey AI, Saito M, Wahrer DC, Reynolds P, Bell DW, Lake R, van den Heuvel S, Settleman J, Haber DA
Cell 2003 Mar 7;112(5):673-84
PMID 12628187
 
Oncogenic CagA promotes gastric cancer risk via activating ERK signaling pathways: a nested case-control study
Yang JJ, Cho LY, Ma SH, Ko KP, Shin A, Choi BY, Han DS, Song KS, Kim YS, Chang SH, Shin HR, Kang D, Yoo KY, Park SK
PLoS One 2011;6(6):e21155
PMID 21698158
 
Overexpression of dedicator of cytokinesis I (Dock180) in ovarian cancer correlated with aggressive phenotype and poor patient survival
Zhao F, Siu MK, Jiang L, Tam KF, Ngan HY, Le XF, Wong OG, Wong ES, Chan HY, Cheung AN
Histopathology 2011 Dec;59(6):1163-72
PMID 22175896
 
The C
Zhou Z, Caron E, Hartwieg E, Hall A, Horvitz HR
elegans PH domain protein CED-12 regulates cytoskeletal reorganization via a Rho/Rac GTPase signaling pathway Dev Cell
PMID 11703939
 
Phagocytosis of apoptotic cells is regulated by a UNC-73/TRIO-MIG-2/RhoG signaling module and armadillo repeats of CED-12/ELMO
deBakker CD, Haney LB, Kinchen JM, Grimsley C, Lu M, Klingele D, Hsu PK, Chou BK, Cheng LC, Blangy A, Sondek J, Hengartner MO, Wu YC, Ravichandran KS
Curr Biol 2004 Dec 29;14(24):2208-16
PMID 15620647
 

Citation

This paper should be referenced as such :
Ping Li, Fung Zhao, Annie N Cheung
DOCK1 (Dedicator of cytokinesis 1)
Atlas Genet Cytogenet Oncol Haematol. 2016;20(3):115-120.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/DOCK1ID40354ch10q26.html


Other Leukemias implicated (Data extracted from papers in the Atlas) [ 1 ]
  t(3;11)(p25;p15) ANKRD28/NUP98


External links

Nomenclature
HGNC (Hugo)DOCK1   2987
Cards
AtlasDOCK1ID40354ch10q26
Entrez_Gene (NCBI)DOCK1  1793  dedicator of cytokinesis 1
AliasesDOCK180; ced5
GeneCards (Weizmann)DOCK1
Ensembl hg19 (Hinxton)ENSG00000150760 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000150760 [Gene_View]  chr10:126905409-127452517 [Contig_View]  DOCK1 [Vega]
ICGC DataPortalENSG00000150760
TCGA cBioPortalDOCK1
AceView (NCBI)DOCK1
Genatlas (Paris)DOCK1
WikiGenes1793
SOURCE (Princeton)DOCK1
Genetics Home Reference (NIH)DOCK1
Genomic and cartography
GoldenPath hg38 (UCSC)DOCK1  -     chr10:126905409-127452517 +  10q26.2   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)DOCK1  -     10q26.2   [Description]    (hg19-Feb_2009)
EnsemblDOCK1 - 10q26.2 [CytoView hg19]  DOCK1 - 10q26.2 [CytoView hg38]
Mapping of homologs : NCBIDOCK1 [Mapview hg19]  DOCK1 [Mapview hg38]
OMIM601403   
Gene and transcription
Genbank (Entrez)AI951513 AK091673 AL157538 AW298149 BC084559
RefSeq transcript (Entrez)NM_001290223 NM_001380
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)DOCK1
Cluster EST : UnigeneHs.159195 [ NCBI ]
CGAP (NCI)Hs.159195
Alternative Splicing GalleryENSG00000150760
Gene ExpressionDOCK1 [ NCBI-GEO ]   DOCK1 [ EBI - ARRAY_EXPRESS ]   DOCK1 [ SEEK ]   DOCK1 [ MEM ]
Gene Expression Viewer (FireBrowse)DOCK1 [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevestigatorExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)1793
GTEX Portal (Tissue expression)DOCK1
Human Protein AtlasENSG00000150760-DOCK1 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ14185   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ14185  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ14185
Splice isoforms : SwissVarQ14185
PhosPhoSitePlusQ14185
Domaine pattern : Prosite (Expaxy)DHR_1 (PS51650)    DHR_2 (PS51651)    SH3 (PS50002)   
Domains : Interpro (EBI)ARM-type_fold    DHR-1_domain    DHR-2    DOCK    DOCK1    DOCK_C    DOCK_N    SH3_domain   
Domain families : Pfam (Sanger)DHR-2 (PF06920)    DOCK-C2 (PF14429)    DOCK_N (PF16172)    SH3_9 (PF14604)   
Domain families : Pfam (NCBI)pfam06920    pfam14429    pfam16172    pfam14604   
Domain families : Smart (EMBL)SH3 (SM00326)  
Conserved Domain (NCBI)DOCK1
DMDM Disease mutations1793
Blocks (Seattle)DOCK1
PDB (SRS)3L4C   
PDB (PDBSum)3L4C   
PDB (IMB)3L4C   
PDB (RSDB)3L4C   
Structural Biology KnowledgeBase3L4C   
SCOP (Structural Classification of Proteins)3L4C   
CATH (Classification of proteins structures)3L4C   
SuperfamilyQ14185
Human Protein Atlas [tissue]ENSG00000150760-DOCK1 [tissue]
Peptide AtlasQ14185
HPRD03240
IPIIPI00015286   IPI00872808   
Protein Interaction databases
DIP (DOE-UCLA)Q14185
IntAct (EBI)Q14185
FunCoupENSG00000150760
BioGRIDDOCK1
STRING (EMBL)DOCK1
ZODIACDOCK1
Ontologies - Pathways
QuickGOQ14185
Ontology : AmiGOguanyl-nucleotide exchange factor activity  Rho guanyl-nucleotide exchange factor activity  GTPase activator activity  protein binding  cytoplasm  cytosol  phagocytosis, engulfment  apoptotic process  cytoskeleton organization  signal transduction  integrin-mediated signaling pathway  small GTPase mediated signal transduction  blood coagulation  positive regulation of epithelial cell migration  membrane  cell migration  SH3 domain binding  guanyl-nucleotide exchange factor complex  Fc-gamma receptor signaling pathway involved in phagocytosis  positive regulation of GTPase activity  vascular endothelial growth factor receptor signaling pathway  positive regulation of substrate adhesion-dependent cell spreading  
Ontology : EGO-EBIguanyl-nucleotide exchange factor activity  Rho guanyl-nucleotide exchange factor activity  GTPase activator activity  protein binding  cytoplasm  cytosol  phagocytosis, engulfment  apoptotic process  cytoskeleton organization  signal transduction  integrin-mediated signaling pathway  small GTPase mediated signal transduction  blood coagulation  positive regulation of epithelial cell migration  membrane  cell migration  SH3 domain binding  guanyl-nucleotide exchange factor complex  Fc-gamma receptor signaling pathway involved in phagocytosis  positive regulation of GTPase activity  vascular endothelial growth factor receptor signaling pathway  positive regulation of substrate adhesion-dependent cell spreading  
Pathways : BIOCARTASignaling of Hepatocyte Growth Factor Receptor [Genes]   
Pathways : KEGGFocal adhesion    Regulation of actin cytoskeleton    Bacterial invasion of epithelial cells    Shigellosis   
REACTOMEQ14185 [protein]
REACTOME PathwaysR-HSA-983231 [pathway]   
NDEx NetworkDOCK1
Atlas of Cancer Signalling NetworkDOCK1
Wikipedia pathwaysDOCK1
Orthology - Evolution
OrthoDB1793
GeneTree (enSembl)ENSG00000150760
Phylogenetic Trees/Animal Genes : TreeFamDOCK1
HOVERGENQ14185
HOGENOMQ14185
Homologs : HomoloGeneDOCK1
Homology/Alignments : Family Browser (UCSC)DOCK1
Gene fusions - Rearrangements
Fusion : MitelmanDOCK1/APBA1 [10q26.2/9q21.11]  
Fusion : MitelmanDOCK1/DPCD [10q26.2/10q24.32]  [t(10;10)(q24;q26)]  
Fusion : MitelmanDOCK1/MGMT [10q26.2/10q26.3]  [t(10;10)(q26;q26)]  
Fusion : MitelmanDOCK1/PCDH15 [10q26.2/10q21.1]  [t(10;10)(q21;q26)]  
Fusion : MitelmanDOCK1/PPAPDC1A [10q26.2/10q26.12]  [t(10;10)(q26;q26)]  
Fusion : MitelmanFUOM/DOCK1 [10q26.3/10q26.2]  [t(10;10)(q26;q26)]  
Fusion : MitelmanGALNT16/DOCK1 [14q24.1/10q26.2]  [t(10;14)(q26;q24)]  
Fusion: TCGA_MDACCC10orf125 DOCK1 10q26.2 LUAD
Fusion: TCGA_MDACCDOCK1 10q26.2 APBA1 9q21.11 BRCA
Fusion: TCGA_MDACCDOCK1 10q26.2 DPCD 10q24.32 GBM
Fusion: TCGA_MDACCDOCK1 10q26.2 MGMT 10q26.3 BRCA
Fusion: TCGA_MDACCDOCK1 10q26.2 PCDH15 10q21.1 BRCA
Fusion: TCGA_MDACCDOCK1 10q26.2 PPAPDC1A 10q26.12 BRCA
Fusion: TCGA_MDACCGALNTL1 DOCK1 10q26.2 BRCA
Tumor Fusion PortalDOCK1
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerDOCK1 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)DOCK1
dbVarDOCK1
ClinVarDOCK1
1000_GenomesDOCK1 
Exome Variant ServerDOCK1
ExAC (Exome Aggregation Consortium)ENSG00000150760
GNOMAD BrowserENSG00000150760
Genetic variants : HAPMAP1793
Genomic Variants (DGV)DOCK1 [DGVbeta]
DECIPHERDOCK1 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisDOCK1 
Mutations
ICGC Data PortalDOCK1 
TCGA Data PortalDOCK1 
Broad Tumor PortalDOCK1
OASIS PortalDOCK1 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICDOCK1  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDDOCK1
BioMutasearch DOCK1
DgiDB (Drug Gene Interaction Database)DOCK1
DoCM (Curated mutations)DOCK1 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)DOCK1 (select a term)
intoGenDOCK1
NCG5 (London)DOCK1
Cancer3DDOCK1(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM601403   
Orphanet
DisGeNETDOCK1
MedgenDOCK1
Genetic Testing Registry DOCK1
NextProtQ14185 [Medical]
TSGene1793
GENETestsDOCK1
Target ValidationDOCK1
Huge Navigator DOCK1 [HugePedia]
snp3D : Map Gene to Disease1793
BioCentury BCIQDOCK1
ClinGenDOCK1
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD1793
Chemical/Pharm GKB GenePA27453
Clinical trialDOCK1
Miscellaneous
canSAR (ICR)DOCK1 (select the gene name)
Probes
Litterature
PubMed80 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineDOCK1
EVEXDOCK1
GoPubMedDOCK1
iHOPDOCK1
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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indexed on : Tue Nov 21 14:48:47 CET 2017

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