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Search results 1 to 100 out of 121 for Dock4

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0.021s
Type Details Score
Gene
Type: gene
Organism: Homo sapiens
Gene
Type: gene
Organism: Danio rerio
Gene
Type: gene
Organism: Rattus norvegicus
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus musculus
Protein Domain
Type: Family
Description: DOCK family members are evolutionarily conserved guanine nucleotide exchange factors (GEFs) for Rho-family GTPases []. DOCK proteins are required during several cellular processes, such as cell motility and phagocytosis. The N-terminal SH3 domain of the DOCK proteins functions as an inhibitor of GEF, which can be relieved upon its binding to the ELMO1-3 adaptor proteins, after their binding to active RhoG at the plasma membrane [, ]. DOCK family proteins are categorised into four subfamilies based on their sequence homology: DOCK-A subfamily (DOCK1/180, 2, 5), DOCK-B subfamily (DOCK3, 4), DOCK-C subfamily (DOCK6, 7, 8), DOCK-D subfamily (DOCK9, 10, 11) []. This entry represents DOCK4. DOCK4 plays a critical role in mediating TGF-beta's prometastatic effects in lung cancer [].
Gene
Type: gene
Organism: Homo sapiens
Publication
First Author: Huang L
Year: 2019
Journal: Nature
Title: SR-B1 drives endothelial cell LDL transcytosis via DOCK4 to promote atherosclerosis.
Volume: 569
Issue: 7757
Pages: 565-569
Publication
First Author: Yu JR
Year: 2015
Journal: Genes Dev
Title: TGF-β/Smad signaling through DOCK4 facilitates lung adenocarcinoma metastasis.
Volume: 29
Issue: 3
Pages: 250-61
Publication
First Author: Yan D
Year: 2006
Journal: J Mol Biol
Title: An isoform of GTPase regulator DOCK4 localizes to the stereocilia in the inner ear and binds to harmonin (USH1C).
Volume: 357
Issue: 3
Pages: 755-64
Protein
Organism: Mus musculus
Length: 235  
Fragment?: true
Publication
First Author: Lu M
Year: 2005
Journal: Curr Biol
Title: A Steric-inhibition model for regulation of nucleotide exchange via the Dock180 family of GEFs.
Volume: 15
Issue: 4
Pages: 371-7
Publication
First Author: Gadea G
Year: 2014
Journal: Eur J Cell Biol
Title: Dock-family exchange factors in cell migration and disease.
Volume: 93
Issue: 10-12
Pages: 466-77
Publication
First Author: Côté JF
Year: 2002
Journal: J Cell Sci
Title: Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity.
Volume: 115
Issue: Pt 24
Pages: 4901-13
Protein
Organism: Mus musculus
Length: 1134  
Fragment?: false
Protein
Organism: Mus musculus
Length: 1978  
Fragment?: false
Protein
Organism: Mus musculus
Length: 1940  
Fragment?: false
Protein
Organism: Mus musculus
Length: 557  
Fragment?: true
Publication  
First Author: Abraham S
Year: 2015
Journal: Nat Commun
Title: A Rac/Cdc42 exchange factor complex promotes formation of lateral filopodia and blood vessel lumen morphogenesis.
Volume: 6
Pages: 7286
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus caroli
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus musculus
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus musculus
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus musculus
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus musculus
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus musculus
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus musculus
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus musculus
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus musculus
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus musculus
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus musculus
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus musculus
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus musculus
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus musculus
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus musculus
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus musculus
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus musculus
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus pahari
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus spretus
GXD Expression      
Probe: MGI:6724236
Assay Type: RT-PCR
Annotation Date: 2021-07-20
Strength: Present
Sex: Male
Emaps: EMAPS:1797220
Stage: TS20
Assay Id: MGI:6724317
Age: embryonic day 12.5
Detected: true
Specimen Num: 2
GXD Expression      
Probe: MGI:6724236
Assay Type: RT-PCR
Annotation Date: 2021-07-20
Strength: Present
Sex: Male
Emaps: EMAPS:1797221
Stage: TS21
Assay Id: MGI:6724317
Age: embryonic day 13.5
Detected: true
Specimen Num: 4
GXD Expression      
Probe: MGI:6724236
Assay Type: RT-PCR
Annotation Date: 2021-07-20
Strength: Present
Sex: Female
Emaps: EMAPS:1796220
Stage: TS20
Assay Id: MGI:6724317
Age: embryonic day 12.5
Detected: true
Specimen Num: 1
GXD Expression      
Probe: MGI:6724236
Assay Type: RT-PCR
Annotation Date: 2021-07-20
Strength: Present
Sex: Female
Emaps: EMAPS:1796221
Stage: TS21
Assay Id: MGI:6724317
Age: embryonic day 13.5
Detected: true
Specimen Num: 3
GXD Expression  
Probe: MGI:5776245
Assay Type: Immunohistochemistry
Annotation Date: 2016-06-16
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1620421
Pattern: Not Specified
Stage: TS21
Assay Id: MGI:5776249
Age: embryonic day 13.5
Image: S9c WT
Detected: true
Specimen Num: 1
GXD Expression  
Probe: MGI:5776245
Assay Type: Immunohistochemistry
Annotation Date: 2016-06-16
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1620421
Pattern: Not Specified
Stage: TS21
Assay Id: MGI:5776249
Age: embryonic day 13.5
Image: S9c Het
Detected: true
Specimen Num: 2
Publication
First Author: Davis RC
Year: 2005
Journal: Diabetes
Title: Ultrafine mapping of SNPs from mouse strains C57BL/6J, DBA/2J, and C57BLKS/J for loci contributing to diabetes and atherosclerosis susceptibility.
Volume: 54
Issue: 4
Pages: 1191-9
Publication
First Author: Kawada K
Year: 2009
Journal: Mol Cell Biol
Title: Cell migration is regulated by platelet-derived growth factor receptor endocytosis.
Volume: 29
Issue: 16
Pages: 4508-18
Publication
First Author: Thomas JW
Year: 2000
Journal: Genome Res
Title: Comparative genome mapping in the sequence-based era: early experience with human chromosome 7.
Volume: 10
Issue: 5
Pages: 624-33
Publication
First Author: Bouma GJ
Year: 2010
Journal: Biol Reprod
Title: New candidate genes identified for controlling mouse gonadal sex determination and the early stages of granulosa and Sertoli cell differentiation.
Volume: 82
Issue: 2
Pages: 380-9
Publication
First Author: Munger SC
Year: 2009
Journal: Genes Dev
Title: Elucidation of the transcription network governing mammalian sex determination by exploiting strain-specific susceptibility to sex reversal.
Volume: 23
Issue: 21
Pages: 2521-36
Publication
First Author: Okazaki N
Year: 2003
Journal: DNA Res
Title: Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries.
Volume: 10
Issue: 1
Pages: 35-48
Publication      
First Author: Mammalian Functional Genomics Centre
Year: 2010
Journal: MGI Direct Data Submission
Title: Alleles produced for the NorCOMM project by the Mammalian Functional Genomics Centre (Mfgc), University of Manitoba
Publication      
First Author: MGI and IMPC
Year: 2018
Journal: Database Release
Title: MGI Load of Endonuclease-Mediated Alleles (CRISPR) from the International Mouse Phenotyping Consortium (IMPC)
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: FANTOM2 Data Curation in Mouse Genome Informatics
Publication
First Author: Stryke D
Year: 2003
Journal: Nucleic Acids Res
Title: BayGenomics: a resource of insertional mutations in mouse embryonic stem cells.
Volume: 31
Issue: 1
Pages: 278-81
Publication      
First Author: International Mouse Strain Resource
Year: 2014
Journal: Database Download
Title: MGI download of germline transmission data for alleles from IMSR strain data
Publication      
First Author: Helmholtz Zentrum Muenchen GmbH
Year: 2010
Journal: MGI Direct Data Submission
Title: Alleles produced for the EUCOMM and EUCOMMTools projects by the Helmholtz Zentrum Muenchen GmbH (Hmgu)
Publication
First Author: Magdaleno S
Year: 2006
Journal: PLoS Biol
Title: BGEM: an in situ hybridization database of gene expression in the embryonic and adult mouse nervous system.
Volume: 4
Issue: 4
Pages: e86
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2003
Title: MGI Sequence Curation Reference
Publication
First Author: Carninci P
Year: 2005
Journal: Science
Title: The transcriptional landscape of the mammalian genome.
Volume: 309
Issue: 5740
Pages: 1559-63
Publication
First Author: Okazaki Y
Year: 2002
Journal: Nature
Title: Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs.
Volume: 420
Issue: 6915
Pages: 563-73
Publication
First Author: Kawai J
Year: 2001
Journal: Nature
Title: Functional annotation of a full-length mouse cDNA collection.
Volume: 409
Issue: 6821
Pages: 685-90
Publication
First Author: Zambrowicz BP
Year: 2003
Journal: Proc Natl Acad Sci U S A
Title: Wnk1 kinase deficiency lowers blood pressure in mice: a gene-trap screen to identify potential targets for therapeutic intervention.
Volume: 100
Issue: 24
Pages: 14109-14
Publication      
First Author: Mouse Genome Informatics (MGI) and National Center for Biotechnology Information (NCBI)
Year: 2008
Journal: Database Download
Title: Mouse Gene Trap Data Load from dbGSS
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2001
Title: Gene Ontology Annotation by the MGI Curatorial Staff
Publication      
First Author: MGI Genome Annotation Group and UniGene Staff
Year: 2015
Journal: Database Download
Title: MGI-UniGene Interconnection Effort
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Title: Human to Mouse ISO GO annotation transfer
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2000
Title: Gene Ontology Annotation by electronic association of SwissProt Keywords with GO terms
Publication
First Author: Diez-Roux G
Year: 2011
Journal: PLoS Biol
Title: A high-resolution anatomical atlas of the transcriptome in the mouse embryo.
Volume: 9
Issue: 1
Pages: e1000582
Publication      
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
Publication      
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
Publication      
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
Publication      
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
Publication      
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
Publication      
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
Publication
First Author: Ueda S
Year: 2013
Journal: Mol Biol Cell
Title: Rac GEF Dock4 interacts with cortactin to regulate dendritic spine formation.
Volume: 24
Issue: 10
Pages: 1602-13
Protein Domain
Type: Domain
Description: DOCK family members are evolutionarily conserved guanine nucleotide exchange factors (GEFs) for Rho-family GTPases []. DOCK proteins are required during several cellular processes, such as cell motility and phagocytosis. The N-terminal SH3 domain of the DOCK proteins functions as an inhibitor of GEF, which can be relieved upon its binding to the ELMO1-3 adaptor proteins, after their binding to active RhoG at the plasma membrane [, ]. DOCK family proteins are categorised into four subfamilies based on their sequence homology: DOCK-A subfamily (DOCK1/180, 2, 5), DOCK-B subfamily (DOCK3, 4), DOCK-C subfamily (DOCK6, 7, 8), DOCK-D subfamily (DOCK9, 10, 11) []. This entry represents the C2 domain of the Dock-B members. Most of these members have been shown to be GEFs specific for Rac, although Dock4 has also been shown to interact indirectly with the Ras family GTPase Rap1, probably through Rap regulatory proteins. In addition to the C2 domain (also known as DHR-1 domain) and the DHR-2 domain, Dock-B members contain a SH3 domain upstream of the C2 domain and a proline-rich region downstream. DHR-2 has the catalytic activity for Rac and/or Cdc42, but is structurally unrelated to the DH domain. The C2/DHR-1 domains of Dock1 (also known as Dock180) and Dock4 have been shown to bind phosphatidylinositol-3, 4, 5-triphosphate (PtdIns(3,4,5)P3)[, , ].
Publication
First Author: Miyamoto Y
Year: 2010
Journal: Cell Signal
Title: Cellular signaling of Dock family proteins in neural function.
Volume: 22
Issue: 2
Pages: 175-82
Publication
First Author: Katoh H
Year: 2009
Journal: Seikagaku
Title: [Regulation of cell morphology and motility by Dock family proteins].
Volume: 81
Issue: 8
Pages: 711-6
Protein Domain
Type: Domain
Description: DOCK family members are evolutionarily conserved guanine nucleotide exchange factors (GEFs) for Rho-family GTPases []. DOCK proteins are required during several cellular processes, such as cell motility and phagocytosis. The N-terminal SH3 domain of the DOCK proteins functions as an inhibitor of GEF, which can be relieved upon its binding to the ELMO1-3 adaptor proteins, after their binding to active RhoG at the plasma membrane [, ]. DOCK family proteins are categorised into four subfamilies based on their sequence homology: DOCK-A subfamily (DOCK1/180, 2, 5), DOCK-B subfamily (DOCK3, 4), DOCK-C subfamily (DOCK6, 7, 8), DOCK-D subfamily (DOCK9, 10, 11) []. This entry represents the SH3 domain found in DOCK4. DOCK4 regulates dendritic spine formation and has been linked to autism, dyslexia, and schizophrenia []. It also plays a critical role in mediating TGF-beta's prometastatic effects in lung cancer [].
Protein Domain
Type: Domain
Description: DOCK family members are evolutionarily conserved guanine nucleotide exchange factors (GEFs) for Rho-family GTPases []. DOCK proteins are required during several cellular processes, such as cell motility and phagocytosis. The N-terminal SH3 domain of the DOCK proteins functions as an inhibitor of GEF, which can be relieved upon its binding to the ELMO1-3 adaptor proteins, after their binding to active RhoG at the plasma membrane [, ]. DOCK family proteins are categorised into four subfamilies based on their sequence homology: DOCK-A subfamily (DOCK1/180, 2, 5), DOCK-B subfamily (DOCK3, 4), DOCK-C subfamily (DOCK6, 7, 8), DOCK-D subfamily (DOCK9, 10, 11) []. This entry represents the C2 domain found in the Dock-C members. In addition to the C2 domain (also known as DHR-1 domain) and the DHR-2 domain, Dock-C members contain a functionally uncharacterised domain upstream of the C2 domain. DHR-2 has the catalytic activity for Rac and/or Cdc42, but is structurally unrelated to the DH domain. The C2/DHR-1 domains of Dock1 (also known as Dock180) and Dock4 have been shown to bind phosphatidylinositol-3, 4, 5-triphosphate (PtdIns(3,4,5)P3) [, , ].
Protein Domain
Type: Domain
Description: DOCK family members are evolutionarily conserved guanine nucleotide exchange factors (GEFs) for Rho-family GTPases []. DOCK proteins are required during several cellular processes, such as cell motility and phagocytosis. The N-terminal SH3 domain of the DOCK proteins functions as an inhibitor of GEF, which can be relieved upon its binding to the ELMO1-3 adaptor proteins, after their binding to active RhoG at the plasma membrane [, ]. DOCK family proteins are categorised into four subfamilies based on their sequence homology: DOCK-A subfamily (DOCK1/180, 2, 5), DOCK-B subfamily (DOCK3, 4), DOCK-C subfamily (DOCK6, 7, 8), DOCK-D subfamily (DOCK9, 10, 11) []. This entry represents the C2 domain of the Dock-D members. In addition to the C2 domain (also known as the DHR-1 domain) and the DHR-2, Dock-D members contain a functionally uncharacterised domain and a PH domain upstream of the C2 domain. DHR-2 has the catalytic activity for Rac and/or Cdc42, but is structurally unrelated to the DH domain. The C2/DHR-1 domains of Dock1 (also known as Dock180) and Dock4 have been shown to bind phosphatidylinositol-3, 4, 5-triphosphate (PtdIns(3,4,5)P3). The PH domain broadly binds to phospholipids and is thought to be involved in targeting the plasma membrane [, , ].
Publication
First Author: Premkumar L
Year: 2010
Journal: J Biol Chem
Title: Structural basis of membrane targeting by the Dock180 family of Rho family guanine exchange factors (Rho-GEFs).
Volume: 285
Issue: 17
Pages: 13211-22
Protein
Organism: Mus musculus
Length: 1601  
Fragment?: true
Protein
Organism: Mus musculus
Length: 811  
Fragment?: true
Protein
Organism: Mus musculus
Length: 477  
Fragment?: true
Protein
Organism: Mus musculus
Length: 2027  
Fragment?: false
Protein
Organism: Mus musculus
Length: 2030  
Fragment?: false
Protein
Organism: Mus musculus
Length: 2130  
Fragment?: false
Protein
Organism: Mus musculus
Length: 2080  
Fragment?: false
Protein
Organism: Mus musculus
Length: 2128  
Fragment?: false
Protein
Organism: Mus musculus
Length: 2098  
Fragment?: false
Protein
Organism: Mus musculus
Length: 2130  
Fragment?: false
Protein
Organism: Mus musculus
Length: 2111  
Fragment?: false
Protein
Organism: Mus musculus
Length: 1816  
Fragment?: true
Protein
Organism: Mus musculus
Length: 1909  
Fragment?: true
Protein
Organism: Mus musculus
Length: 2100  
Fragment?: false