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Search results 101 to 200 out of 216 for Dock1

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Type Details Score
Publication
- | J:85000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2003
Title: MGI Sequence Curation Reference
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Publication
16141072 | J:99680
First Author: Carninci P
Year: 2005
Journal: Science
Title: The transcriptional landscape of the mammalian genome.
Volume: 309
Issue: 5740
Pages: 1559-63
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Publication
11217851 | J:65060
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
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Publication
- | J:141210
     
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
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Publication
14610273 | J:86696
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
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Publication
- | J:293217
       
First Author: GemPharmatech
Year: 2020
Title: GemPharmatech Website.
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Publication
- | J:60000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2000
Title: Gene Ontology Annotation by electronic association of SwissProt Keywords with GO terms
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Publication
- | J:342587
       
First Author: AgBase, BHF-UCL, Parkinson's UK-UCL, dictyBase, HGNC, Roslin Institute, FlyBase and UniProtKB curators
Year: 2011
Title: Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
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Publication
- | J:68900
     
First Author: The Jackson Laboratory Mouse Radiation Hybrid Database
Year: 2004
Journal: Database Release
Title: Mouse T31 Radiation Hybrid Data Load
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Publication
12466851 | J:80000
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
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Publication
- | J:164563
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Title: Human to Mouse ISO GO annotation transfer
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Publication
21267068 | J:153498
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
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Publication
- | J:157972
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome U74 Array Platform (A, B, C v2).
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Publication
- | J:75000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
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Publication
- | J:161428
       
First Author: Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year: 2010
Title: Annotation inferences using phylogenetic trees
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Publication
- | J:53168
     
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
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Publication
- | J:91388
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
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Publication
- | J:90438
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
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Publication
- | J:155721
     
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
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Publication
- | J:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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Publication
- | J:63103
     
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
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Publication
- | J:262123
     
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
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Publication
- | J:144086
     
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
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Publication
- | J:85324
     
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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Publication
- | J:144087
     
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
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GXD Expression
GXD Expression
 
Probe: MGI:5635579
Assay Type: Immunohistochemistry
Annotation Date: 2015-05-13
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1657020
Pattern: Not Specified
Stage: TS20
Assay Id: MGI:5635647
Age: embryonic day 12.5
Note: There was co-localization of expression with Dock1 in the vascular endothelial cell lineage.
Specimen Label: Online VIA
Detected: true
Specimen Num: 4
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GXD Expression
GXD Expression
 
Probe: MGI:5635579
Assay Type: Immunohistochemistry
Annotation Date: 2015-05-13
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1669620
Pattern: Not Specified
Stage: TS20
Assay Id: MGI:5635647
Age: embryonic day 12.5
Note: There was co-localization of expression with Dock1 in the cardiac cell lineage.
Specimen Label: Online VIB
Detected: true
Specimen Num: 5
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Publication
19004829 | -
First Author: Sanders MA
Year: 2009
Journal: J Biol Chem
Title: DOCK5 and DOCK1 regulate Caco-2 intestinal epithelial cell spreading and migration on collagen IV.
Volume: 284
Issue: 1
Pages: 27-35
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Publication
11950595 | -
First Author: Goicoechea SM
Year: 2002
Journal: Int J Biochem Cell Biol
Title: Nck-2 interacts with focal adhesion kinase and modulates cell motility.
Volume: 34
Issue: 7
Pages: 791-805
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Publication
9843575 | -
First Author: Tu Y
Year: 1998
Journal: Mol Biol Cell
Title: Nck-2, a novel Src homology2/3-containing adaptor protein that interacts with the LIM-only protein PINCH and components of growth factor receptor kinase-signaling pathways.
Volume: 9
Issue: 12
Pages: 3367-82
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Protein Domain
IPR028524 | NCK2
Type: Family
Description: Cytoplasmic protein NCK2 (NCK2) is a non-enzymatic adaptor protein composed of three SH3 (Src homology 3) domains and a C-terminal SH2 domain. There are two vertebrate NCK proteins, NCK1 and NCK2. NCK2 mediates Slit-induced cortical neurite outgrowth []. NCK2 interacts with focal adhesion kinase (FAK) and this interaction suggests a role of NCK2 in the modulation of cell motility []. It also interacts with DOCK1 [], LIMS1 [].
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Protein Domain
IPR006816 | ELMO_dom
Type: Domain
Description: This entry represents the ELMO (EnguLfment and Cell MOtility) domain, which is found in a number of eukaryotic proteins involved in the cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility, including CED-12, ELMO-1 and ELMO-2. ELMO-1 and ELMO-2 are components of signalling pathways that regulate phagocytosis and cell migration and are mammalian orthologues of the Caenorhabditis elegans gene, ced-12 that is required for the engulfment of dying cells and cell migration. ELMO-1/2 act in association with DOCK1 and CRK. ELMO-1/2 interact with the SH3-domain of DOCK1 via an SH3-binding site to enhance the guanine nucleotide exchange factor (GEF) activity of DOCK1. ELMO-1/2 could be part of a complex with DOCK1 and Rac1 that could be required to activate Rac Rho small GTPases. Regulatory GTPases in the Ras superfamily employ a cycle of alternating GTP binding and hydrolysis, controlled by guanine nucleotide exchange factors and GTPase-activating proteins (GAPs), as essential features of their actions in cells. Within the Ras superfamily, the Arf family is composed of 30 members, including 22 Arf-like (Arl) proteins. The ELMO domain has been proposed to be a GAP domain for ARL2 and other members of the Arf family [].
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Protein
Q3V1U8
Organism: Mus musculus/domesticus
Length: 326  
Fragment?: false
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Protein
Q8BGF6
Organism: Mus musculus/domesticus
Length: 293  
Fragment?: false
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Protein
Q91YP6
Organism: Mus musculus/domesticus
Length: 381  
Fragment?: false
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Protein
Q3TPW1
Organism: Mus musculus/domesticus
Length: 164  
Fragment?: true
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Protein
Q8BHN8
Organism: Mus musculus/domesticus
Length: 216  
Fragment?: false
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Protein
B7ZN22
Organism: Mus musculus/domesticus
Length: 269  
Fragment?: false
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Protein
B7ZN20
Organism: Mus musculus/domesticus
Length: 295  
Fragment?: true
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Protein
A0A0U1RPA9
Organism: Mus musculus/domesticus
Length: 213  
Fragment?: true
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Protein
E9Q0K9
Organism: Mus musculus/domesticus
Length: 326  
Fragment?: false
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Protein
Q0P556
Organism: Mus musculus/domesticus
Length: 295  
Fragment?: true
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Protein
A0A1B0GRZ8
Organism: Mus musculus/domesticus
Length: 189  
Fragment?: true
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Protein
Q8BHP4
Organism: Mus musculus/domesticus
Length: 164  
Fragment?: false
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Publication
20844538 | J:164662
First Author: Elliott MR
Year: 2010
Journal: Nature
Title: Unexpected requirement for ELMO1 in clearance of apoptotic germ cells in vivo.
Volume: 467
Issue: 7313
Pages: 333-7
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Protein
A0A1Y7VIX9
Organism: Mus musculus/domesticus
Length: 193  
Fragment?: true
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Publication
19796679 | -
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
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Publication
19803396 | -
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
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Protein
Q5GMG0
Organism: Mus musculus/domesticus
Length: 122  
Fragment?: true
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Protein
F6YXR3
Organism: Mus musculus/domesticus
Length: 290  
Fragment?: true
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Protein
A2A5A7
Organism: Mus musculus/domesticus
Length: 41  
Fragment?: true
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Protein
D6RHT3
Organism: Mus musculus/domesticus
Length: 63  
Fragment?: false
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Publication
25452388 | -
First Author: Toret CP
Year: 2014
Journal: J Cell Biol
Title: An Elmo-Dock complex locally controls Rho GTPases and actin remodeling during cadherin-mediated adhesion.
Volume: 207
Issue: 5
Pages: 577-87
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Publication
25332238 | -
First Author: Abu-Thuraia A
Year: 2015
Journal: Mol Cell Biol
Title: Axl phosphorylates Elmo scaffold proteins to promote Rac activation and cell invasion.
Volume: 35
Issue: 1
Pages: 76-87
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Protein Domain
IPR037808 | C2_Dock-C
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) [, , ].
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Protein Domain
IPR037809 | C2_Dock-D
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 [, , ].
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Protein Domain
IPR037811 | C2_Dock-B
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)[, , ].
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Protein Domain
IPR030713 | ELMO2
Type: Family
Description: This entry represents engulfment and cell motility protein 2 (ELMO2) from vertebrates. ELMO2 is a scaffolding component of the Elmo-DOCK complex. Elmo2 and DOCK1 are essential for the rapid recruitment and spreading of E-cadherin, actin reorganisation, localised Rac and Rho GTPase activities, and the development of strong cell-cell adhesion []. ELMO2 interacts with Axl, a receptor tyrosine kinase, and this interaction contributes to cancer cell invasion and proliferation [].ELMO 1-3 are orthologues of the Caenorhabditis elegans ced-12, which is required for the engulfment of dying cells and cell migration []. They are cytoplasmic adaptor proteins that interact with DOCK family guanine nucleotide exchange factors (GEFs) to promote activation of the small GTPase Rac []. ELMO proteins interact with the SH3-domain of DOCKs via an SH3-binding site to enhance the GEF activity of DOCKs. Regulatory GTPases in the Ras superfamily employ a cycle of alternating GTP binding and hydrolysis, controlled by GEFs and GTPase-activating proteins (GAPs), as essential features of their actions in cells [, ].
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Protein
Q8BHL5
Organism: Mus musculus/domesticus
Length: 732  
Fragment?: false
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Publication
17452337 | -
First Author: Bowzard JB
Year: 2007
Journal: J Biol Chem
Title: ELMOD2 is an Arl2 GTPase-activating protein that also acts on Arfs.
Volume: 282
Issue: 24
Pages: 17568-80
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Protein
Q05D34
Organism: Mus musculus/domesticus
Length: 590  
Fragment?: false
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Protein
Q3TZG4
Organism: Mus musculus/domesticus
Length: 506  
Fragment?: false
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Protein
Q8BYZ7
Organism: Mus musculus/domesticus
Length: 720  
Fragment?: false
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Protein
Q8BPU7
Organism: Mus musculus/domesticus
Length: 727  
Fragment?: false
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Protein
Q571D6
Organism: Mus musculus/domesticus
Length: 741  
Fragment?: true
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Protein
A0A1D5RMK9
Organism: Mus musculus/domesticus
Length: 703  
Fragment?: false
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Publication
20167601 | -
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
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Publication
15723800 | -
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
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Publication
25022758 | -
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
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Publication
11595183 | J:72091
First Author: Gumienny TL
Year: 2001
Journal: Cell
Title: CED-12/ELMO, a novel member of the CrkII/Dock180/Rac pathway, is required for phagocytosis and cell migration.
Volume: 107
Issue: 1
Pages: 27-41
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Protein
F6XD63
Organism: Mus musculus/domesticus
Length: 194  
Fragment?: true
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Publication
24821968 | J:244219
First Author: Stevenson C
Year: 2014
Journal: J Immunol
Title: Essential role of Elmo1 in Dock2-dependent lymphocyte migration.
Volume: 192
Issue: 12
Pages: 6062-70
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Protein
A0A0J9YUK4
Organism: Mus musculus/domesticus
Length: 142  
Fragment?: true
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Protein
A0A0U1RNY4
Organism: Mus musculus/domesticus
Length: 811  
Fragment?: true
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Protein
A0A1L1STJ1
Organism: Mus musculus/domesticus
Length: 477  
Fragment?: true
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Publication
11240126 | -
First Author: Tu Y
Year: 2001
Journal: FEBS Lett
Title: Identification and kinetic analysis of the interaction between Nck-2 and DOCK180.
Volume: 491
Issue: 3
Pages: 193-9
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Publication
12432077 | -
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
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Protein
Q8VDR9
Organism: Mus musculus/domesticus
Length: 2080  
Fragment?: false
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Protein
Q8R1A4
Organism: Mus musculus/domesticus
Length: 2130  
Fragment?: false
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Protein
A0A1L1SQR4
Organism: Mus musculus/domesticus
Length: 2111  
Fragment?: false
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Protein
Q6ZPS1
Organism: Mus musculus/domesticus
Length: 1909  
Fragment?: true
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Protein
A0A0R4J2B7
Organism: Mus musculus/domesticus
Length: 1816  
Fragment?: true
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Protein
A0A0U1RNK7
Organism: Mus musculus/domesticus
Length: 2098  
Fragment?: false
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Protein
A2A9M5
Organism: Mus musculus/domesticus
Length: 2128  
Fragment?: false
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Protein
E9PX48
Organism: Mus musculus/domesticus
Length: 2100  
Fragment?: false
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Protein
A2A9M4
Organism: Mus musculus/domesticus
Length: 2130  
Fragment?: false
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Publication
21600986 | J:178048
First Author: Round JE
Year: 2011
Journal: Mol Cell Neurosci
Title: The adaptor protein Nck2 mediates Slit1-induced changes in cortical neuron morphology.
Volume: 47
Issue: 4
Pages: 265-73
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Protein
O55033
Organism: Mus musculus/domesticus
Length: 380  
Fragment?: false
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Protein
Q8BZN6
Organism: Mus musculus/domesticus
Length: 2150  
Fragment?: false
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Protein
A2AF47
Organism: Mus musculus/domesticus
Length: 2073  
Fragment?: false
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Protein
Q8C147
Organism: Mus musculus/domesticus
Length: 2100  
Fragment?: false
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Protein
Q8BIK4
Organism: Mus musculus/domesticus
Length: 2055  
Fragment?: false
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Protein
F8VPN7
Organism: Mus musculus/domesticus
Length: 2113  
Fragment?: false
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Protein
A0A2X0U4P8
Organism: Mus musculus/domesticus
Length: 1942  
Fragment?: true
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Protein
B2RY79
Organism: Mus musculus/domesticus
Length: 2058  
Fragment?: false
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Protein
A0A2X0U2I4
Organism: Mus musculus/domesticus
Length: 2008  
Fragment?: false
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Protein
Q3UHH9
Organism: Mus musculus/domesticus
Length: 1601  
Fragment?: true
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Protein
B9EJ70
Organism: Mus musculus/domesticus
Length: 2100  
Fragment?: false
•
•
•
•
•
Protein
Q7TN11
Organism: Mus musculus/domesticus
Length: 1920  
Fragment?: true
•
•
•
•
•
Protein
A0A1D5RMM1
Organism: Mus musculus/domesticus
Length: 2088  
Fragment?: false
•
•
•
•
•




MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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