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Search results 201 to 257 out of 257 for Nck1

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Type Details Score
Publication        
First Author: Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year: 2010
Title: Annotation inferences using phylogenetic trees
Publication      
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
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 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 (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
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: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
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: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
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
UniProt Feature
Begin: 2
Description: Cytoplasmic protein NCK1
Type: chain
End: 377
Publication
First Author: He B
Year: 2013
Journal: PLoS One
Title: A remote cis-acting variant at 3q links glomerular NCK1 to diabetic nephropathy.
Volume: 8
Issue: 2
Pages: e56414
Publication
First Author: Kefalas G
Year: 2018
Journal: J Biol Chem
Title: Peptide-based sequestration of the adaptor protein Nck1 in pancreatic β cells enhances insulin biogenesis and protects against diabetogenic stresses.
Volume: 293
Issue: 32
Pages: 12516-12524
Publication
First Author: Mukherjee C
Year: 2014
Journal: PLoS Biol
Title: The cytoplasmic capping complex assembles on adapter protein nck1 bound to the proline-rich C-terminus of Mammalian capping enzyme.
Volume: 12
Issue: 8
Pages: e1001933
Allele
Name: non-catalytic region of tyrosine kinase adaptor protein 1; endonuclease-mediated mutation 2, Shanghai Model Organisms Center
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
Publication
First Author: Ger M
Year: 2011
Journal: Cell Signal
Title: Adaptor protein Nck1 interacts with p120 Ras GTPase-activating protein and regulates its activity.
Volume: 23
Issue: 10
Pages: 1651-8
Publication
First Author: Miyamoto Y
Year: 2004
Journal: J Biol Chem
Title: The adaptor protein Nck1 mediates endothelin A receptor-regulated cell migration through the Cdc42-dependent c-Jun N-terminal kinase pathway.
Volume: 279
Issue: 33
Pages: 34336-42
Strain
Attribute String: coisogenic, mutant strain, endonuclease-mediated mutation
Allele
Name: non-catalytic region of tyrosine kinase adaptor protein 1; endonuclease-mediated mutation 1, Shanghai Model Organisms Center
Allele Type: Endonuclease-mediated
Attribute String: Conditional ready, No functional change
Publication
First Author: Ito N
Year: 1998
Journal: J Biol Chem
Title: Identification of vascular endothelial growth factor receptor-1 tyrosine phosphorylation sites and binding of SH2 domain-containing molecules.
Volume: 273
Issue: 36
Pages: 23410-8
Protein Domain
Type: Domain
Description: Cytoplasmic proteins Nck are non-enzymatic adaptor proteins composed of three SH3 (Src homology 3) domains and a C-terminal SH2 domain []. They regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates []. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics []. They associate with tyrosine-phosphorylated growth factor receptors or their cellular substrates [, ]. There are two vertebrate Nck proteins, Nck1 and Nck2. Nck1 (also called Nck-alpha) plays a crucial role in connecting signaling pathways of tyrosine kinase receptors and important effectors in actin dynamics and cytoskeletal remodeling []. It binds and activates RasGAP, resulting in the downregulation of Ras []. It is also involved in the signaling of endothilin-mediated inhibition of cell migration [].This entry represents the SH2 domain of Nck1.
Publication
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
Publication
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
Protein Domain
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 [].
Protein Domain
Type: Family
Description: Cytoplasmic proteins Nck are non-enzymatic adaptor proteins composed of three SH3 (Src homology 3) domains and a C-terminal SH2 domain []. They regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates []. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics []. They associate with tyrosine-phosphorylated growth factor receptors or their cellular substrates [, ]. There are two vertebrate Nck proteins, Nck1 and Nck2.
Protein Domain
Type: Domain
Description: Cytoplasmic proteins Nck are non-enzymatic adaptor proteins composed of three SH3 (Src homology 3) domains and a C-terminal SH2 domain []. They regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates []. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics []. They associate with tyrosine-phosphorylated growth factor receptors or their cellular substrates [, ]. There are two vertebrate Nck proteins, Nck1 and Nck2. This entry represents the SH2 domain of Nck2.
Publication
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
Publication
First Author: Oser M
Year: 2010
Journal: J Cell Sci
Title: Specific tyrosine phosphorylation sites on cortactin regulate Nck1-dependent actin polymerization in invadopodia.
Volume: 123
Issue: Pt 21
Pages: 3662-73
Publication
First Author: Matuoka K
Year: 1997
Journal: Biochem Biophys Res Commun
Title: A novel ligand for an SH3 domain of the adaptor protein Nck bears an SH2 domain and nuclear signaling motifs.
Volume: 239
Issue: 2
Pages: 488-92
Publication
First Author: Buday L
Year: 2002
Journal: Cell Signal
Title: The Nck family of adapter proteins: regulators of actin cytoskeleton.
Volume: 14
Issue: 9
Pages: 723-31
Publication
First Author: Dubrac A
Year: 2018
Journal: Nat Commun
Title: NCK-dependent pericyte migration promotes pathological neovascularization in ischemic retinopathy.
Volume: 9
Issue: 1
Pages: 3463
Publication
First Author: Magalhaes MA
Year: 2011
Journal: J Cell Biol
Title: Cortactin phosphorylation regulates cell invasion through a pH-dependent pathway.
Volume: 195
Issue: 5
Pages: 903-20
Publication    
First Author: Jiang H
Year: 2019
Journal: Elife
Title: Entry by multiple picornaviruses is dependent on a pathway that includes TNK2, WASL, and NCK1.
Volume: 8
Publication
First Author: Xu NJ
Year: 2009
Journal: Nat Neurosci
Title: Ephrin-B3 reverse signaling through Grb4 and cytoskeletal regulators mediates axon pruning.
Volume: 12
Issue: 3
Pages: 268-76
Protein Domain
Type: Domain
Description: This entry represent the first SH3 domain of Nck2. It binds the PxxDY sequence in the CD3e cytoplasmic tail; this binding inhibits phosphorylation by Src kinases, resulting in the downregulation of TCR surface expression []. Nck2 (also known as Grb4) is a member of the Nck family. It plays a crucial role in connecting signaling pathways of tyrosine kinase receptors and important effectors in actin dynamics and cytoskeletal remodeling []. It binds neuronal signaling proteins such as ephrinB []. Cytoplasmic proteins Nck are non-enzymatic adaptor proteins composed of three SH3 (Src homology 3) domains and a C-terminal SH2 domain []. They regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates []. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics []. They associate with tyrosine-phosphorylated growth factor receptors or their cellular substrates [, ]. There are two vertebrate Nck proteins, Nck1 and Nck2.
Protein Domain
Type: Domain
Description: This entry represent the second SH3 domain of Nck2. The second SH3 domain of Nck appears to prefer ligands containing the APxxPxR motif []. Nck2 (also known as Grb4) is a member of the Nck family. It plays a crucial role in connecting signaling pathways of tyrosine kinase receptors and important effectors in actin dynamics and cytoskeletal remodeling []. It binds neuronal signaling proteins such as ephrinB []. Cytoplasmic proteins Nck are non-enzymatic adaptor proteins composed of three SH3 (Src homology 3) domains and a C-terminal SH2 domain []. They regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates []. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics []. They associate with tyrosine-phosphorylated growth factor receptors or their cellular substrates [, ]. There are two vertebrate Nck proteins, Nck1 and Nck2.
Protein Domain
Type: Domain
Description: This entry represent the third SH3 domain of Nck2. The third SH3 domain of Nck appears to prefer ligands with a PxAPxR motif [].Nck2 (also known as Grb4) is a member of the Nck family. It plays a crucial role in connecting signaling pathways of tyrosine kinase receptors and important effectors in actin dynamics and cytoskeletal remodeling []. It binds neuronal signaling proteins such as ephrinB []. Cytoplasmic proteins Nck are non-enzymatic adaptor proteins composed of three SH3 (Src homology 3) domains and a C-terminal SH2 domain []. They regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates []. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics []. They associate with tyrosine-phosphorylated growth factor receptors or their cellular substrates [, ]. There are two vertebrate Nck proteins, Nck1 and Nck2.
Protein Domain
Type: Domain
Description: This entry represent the second SH3 domain of Nck1. The second SH3 domain of Nck appears to prefer ligands containing the APxxPxR motif [].Nck1 (also called Nck-alpha) plays a crucial role in connecting signaling pathways of tyrosine kinase receptors and important effectors in actin dynamics and cytoskeletal remodeling []. It binds and activates RasGAP, resulting in the downregulation of Ras []. It is also involved in the signaling of endothilin-mediated inhibition of cell migration [].Cytoplasmic proteins Nck are non-enzymatic adaptor proteins composed of three SH3 (Src homology 3) domains and a C-terminal SH2 domain []. They regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates []. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics []. They associate with tyrosine-phosphorylated growth factor receptors or their cellular substrates [, ]. There are two vertebrate Nck proteins, Nck1 and Nck2.
Protein Domain
Type: Domain
Description: This entry represent the third SH3 domain of Nck1. The third SH3 domain of Nck appears to prefer ligands with a PxAPxR motif [].Nck1 (also called Nck-alpha) plays a crucial role in connecting signaling pathways of tyrosine kinase receptors and important effectors in actin dynamics and cytoskeletal remodeling []. It binds and activates RasGAP, resulting in the downregulation of Ras []. It is also involved in the signaling of endothilin-mediated inhibition of cell migration [].Cytoplasmic proteins Nck are non-enzymatic adaptor proteins composed of three SH3 (Src homology 3) domains and a C-terminal SH2 domain []. They regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates []. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics []. They associate with tyrosine-phosphorylated growth factor receptors or their cellular substrates [, ]. There are two vertebrate Nck proteins, Nck1 and Nck2.
Publication
First Author: Takeuchi K
Year: 2008
Journal: J Mol Biol
Title: Structural and functional evidence that Nck interaction with CD3epsilon regulates T-cell receptor activity.
Volume: 380
Issue: 4
Pages: 704-16
Publication
First Author: Liu J
Year: 2006
Journal: Biochemistry
Title: Structural insight into the binding diversity between the human Nck2 SH3 domains and proline-rich proteins.
Volume: 45
Issue: 23
Pages: 7171-84
Publication
First Author: Panzhinskiy E
Year: 2013
Journal: PLoS One
Title: Protein tyrosine phosphatase 1B and insulin resistance: role of endoplasmic reticulum stress/reactive oxygen species/nuclear factor kappa B axis.
Volume: 8
Issue: 10
Pages: e77228
Publication
First Author: New LA
Year: 2016
Journal: J Am Soc Nephrol
Title: Nephrin Tyrosine Phosphorylation Is Required to Stabilize and Restore Podocyte Foot Process Architecture.
Volume: 27
Issue: 8
Pages: 2422-35
Protein Domain
Type: Domain
Description: This entry represent the first SH3 domain of Nck1. The first SH3 domain of Nck binds the PxxDY sequence in the CD3e cytoplasmic tail; this binding inhibits phosphorylation by Src kinases, resulting in the downregulation of TCR surface expression [].Nck1 (also called Nck-alpha) plays a crucial role in connecting signaling pathways of tyrosine kinase receptors and important effectors in actin dynamics and cytoskeletal remodeling []. It binds and activates RasGAP, resulting in the downregulation of Ras []. It is also involved in the signaling of endothilin-mediated inhibition of cell migration [].Cytoplasmic proteins Nck are non-enzymatic adaptor proteins composed of three SH3 (Src homology 3) domains and a C-terminal SH2 domain []. They regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates []. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics []. They associate with tyrosine-phosphorylated growth factor receptors or their cellular substrates [, ]. There are two vertebrate Nck proteins, Nck1 and Nck2.
Protein
Organism: Mus musculus/domesticus
Length: 380  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 380  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 142  
Fragment?: true
Publication
First Author: Ballif BA
Year: 2008
Journal: J Proteome Res
Title: Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain.
Volume: 7
Issue: 1
Pages: 311-8
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: Carninci P
Year: 2000
Journal: Genome Res
Title: Normalization and subtraction of cap-trapper-selected cDNAs to prepare full-length cDNA libraries for rapid discovery of new genes.
Volume: 10
Issue: 10
Pages: 1617-30
Publication  
First Author: Carninci P
Year: 1999
Journal: Methods Enzymol
Title: High-efficiency full-length cDNA cloning.
Volume: 303
Pages: 19-44
Publication
First Author: Shibata K
Year: 2000
Journal: Genome Res
Title: RIKEN integrated sequence analysis (RISA) system--384-format sequencing pipeline with 384 multicapillary sequencer.
Volume: 10
Issue: 11
Pages: 1757-71
Publication
First Author: Katayama S
Year: 2005
Journal: Science
Title: Antisense transcription in the mammalian transcriptome.
Volume: 309
Issue: 5740
Pages: 1564-6
Publication
First Author: Gerhard DS
Year: 2004
Journal: Genome Res
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Volume: 14
Issue: 10B
Pages: 2121-7
Publication
First Author: Huttlin EL
Year: 2010
Journal: Cell
Title: A tissue-specific atlas of mouse protein phosphorylation and expression.
Volume: 143
Issue: 7
Pages: 1174-89
Publication
First Author: Church DM
Year: 2009
Journal: PLoS Biol
Title: Lineage-specific biology revealed by a finished genome assembly of the mouse.
Volume: 7
Issue: 5
Pages: e1000112