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Search results 7501 to 7600 out of 8321 for Src

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0.035s

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Hits by Strain

Type Details Score
Protein
A0A0A0MQK6
Organism: Mus musculus/domesticus
Length: 481  
Fragment?: true
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Protein
A0A0N4SW29
Organism: Mus musculus/domesticus
Length: 51  
Fragment?: true
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Protein
A0A2X0SZ21
Organism: Mus musculus/domesticus
Length: 724  
Fragment?: true
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Protein
A0A3Q4EBR8
Organism: Mus musculus/domesticus
Length: 120  
Fragment?: true
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Protein
Q8R2S3
Organism: Mus musculus/domesticus
Length: 220  
Fragment?: false
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Protein
E9PWH2
Organism: Mus musculus/domesticus
Length: 1175  
Fragment?: false
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Protein
Q3ULD8
Organism: Mus musculus/domesticus
Length: 618  
Fragment?: true
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Protein
A0A1Y7VKQ1
Organism: Mus musculus/domesticus
Length: 461  
Fragment?: false
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Protein
G3UY70
Organism: Mus musculus/domesticus
Length: 739  
Fragment?: false
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Protein
A0A2I3BPX6
Organism: Mus musculus/domesticus
Length: 820  
Fragment?: false
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Protein
Q5NC75
Organism: Mus musculus/domesticus
Length: 433  
Fragment?: false
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Protein
Q3V090
Organism: Mus musculus/domesticus
Length: 742  
Fragment?: false
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Protein
A2ASX2
Organism: Mus musculus/domesticus
Length: 538  
Fragment?: false
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Protein
Q80XB1
Organism: Mus musculus/domesticus
Length: 713  
Fragment?: false
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Protein
Q8BH99
Organism: Mus musculus/domesticus
Length: 313  
Fragment?: false
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Protein
Q80XB0
Organism: Mus musculus/domesticus
Length: 393  
Fragment?: false
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Protein
Q53YU5
Organism: Mus musculus/domesticus
Length: 220  
Fragment?: false
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Publication
15335710 | -
First Author: Pawson T
Year: 1993
Journal: Curr Biol
Title: SH2 and SH3 domains.
Volume: 3
Issue: 7
Pages: 434-42
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Publication
7531822 | -
First Author: Pawson T
Year: 1995
Journal: Nature
Title: Protein modules and signalling networks.
Volume: 373
Issue: 6515
Pages: 573-80
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Publication
14731533 | -
First Author: Mayer BJ
Year: 1993
Journal: Trends Cell Biol
Title: Signalling through SH2 and SH3 domains.
Volume: 3
Issue: 1
Pages: 8-13
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Publication
21664272 | -
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
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Publication
15187089 | -
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
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Publication
20971703 | -
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
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Publication
11684018 | -
First Author: Bravo J
Year: 2001
Journal: Mol Cell
Title: The crystal structure of the PX domain from p40(phox) bound to phosphatidylinositol 3-phosphate.
Volume: 8
Issue: 4
Pages: 829-39
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Publication
19549836 | -
First Author: Wang Q
Year: 2009
Journal: Proc Natl Acad Sci U S A
Title: Molecular mechanism of membrane constriction and tubulation mediated by the F-BAR protein Pacsin/Syndapin.
Volume: 106
Issue: 31
Pages: 12700-5
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Protein Domain
IPR001837 | Adenylate_cyclase-assoc_CAP
Type: Family
Description: Cyclase-associated proteins (CAPs) are highly conserved actin-binding proteins present in a wide range of organisms including yeast, fly, plants, and mammals. CAPs are multifunctional proteins that contain several structural domains. CAP is involved in species-specific signalling pathways [, , , ]. In Drosophila, CAP functions in Hedgehog-mediated eye development and in establishing oocyte polarity. In Dictyostelium (slim mold), CAP is involved in microfilament reorganisation near the plasma membrane in a PIP2-regulated manner and is required to perpetuate the cAMP relay signal to organise fruitbody formation. In plants, CAP is involved in plant signalling pathways required for co-ordinated organ expansion. In yeast, CAP is involved in adenylate cyclase activation, as well as in vesicle trafficking and endocytosis. In both yeast and mammals, CAPs appear to be involved in recycling G-actin monomers from ADF/cofilins for subsequent rounds of filament assembly [, ]. In mammals, there are two different CAPs (CAP1 and CAP2) that share 64% amino acid identity. All CAPs appear to contain a C-terminal actin-binding domain that regulates actin remodelling in response to cellular signals and is required for normal cellular morphology, cell division, growth and locomotion in eukaryotes. CAP directly regulates actin filament dynamics and has been implicated in a number of complex developmental and morphological processes, including mRNA localisation and the establishment of cell polarity. Actin exists both as globular (G) (monomeric) actin subunits and assembled into filamentous (F) actin. In cells, actin cycles between these two forms. Proteins that bind F-actin often regulate F-actin assembly and its interaction with other proteins, while proteins that interact with G-actin often control the availability of unpolymerised actin. CAPs bind G-actin. In addition to actin-binding, CAPs can have additional roles, and may act as bifunctional proteins. In Saccharomyces cerevisiae (Baker's yeast), CAP is a component of the adenylyl cyclase complex (Cyr1p) that serves as an effector of Ras during normal cell signalling. S. cerevisiae CAP functions to expose adenylate cyclase binding sites to Ras, thereby enabling adenylate cyclase to be activated by Ras regulatory signals. In Schizosaccharomyces pombe (Fission yeast), CAP is also required for adenylate cyclase activity, but not through the Ras pathway. In both organisms, the N-terminal domain is responsible for adenylate cyclase activation, but the S cerevisiae and S. pombe N-termini cannot complement one another. Yeast CAPs are unique among the CAP family of proteins, because they are the only ones to directly interact with and activate adenylate cyclase []. S. cerevisiae CAP has four major domains. In addition to the N-terminal adenylate cyclase-interacting domain, and the C-terminal actin-binding domain, it possesses two other domains: a proline-rich domain that interacts with Src homology 3 (SH3) domains of specific proteins, and a domain that is responsible for CAP oligomerisation to form multimeric complexes (although oligomerisation appears to involve the N- and C-terminal domains as well). The proline-rich domain interacts with profilin, a protein that catalyses nucleotide exchange on G-actin monomers and promotes addition to barbed ends of filamentous F-actin []. Since CAP can bind profilin via a proline-rich domain, and G-actin via a C-terminal domain, it has been suggested that a ternary G-actin/CAP/profilin complex could be formed.This entry represents CAP proteins from various organisms.
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Protein Domain
IPR036223 | CAP_C_sf
Type: Homologous_superfamily
Description: Cyclase-associated proteins (CAPs) are highly conserved actin-binding proteins present in a wide range of organisms including yeast, fly, plants, and mammals. CAPs are multifunctional proteins that contain several structural domains. CAP is involved in species-specific signalling pathways [, , , ]. In Drosophila, CAP functions in Hedgehog-mediated eye development and in establishing oocyte polarity. In Dictyostelium (slim mold), CAP is involved in microfilament reorganisation near the plasma membrane in a PIP2-regulated manner and is required to perpetuate the cAMP relay signal to organise fruitbody formation. In plants, CAP is involved in plant signalling pathways required for co-ordinated organ expansion. In yeast, CAP is involved in adenylate cyclase activation, as well as in vesicle trafficking and endocytosis. In both yeast and mammals, CAPs appear to be involved in recycling G-actin monomers from ADF/cofilins for subsequent rounds of filament assembly [, ]. In mammals, there are two different CAPs (CAP1 and CAP2) that share 64% amino acid identity. All CAPs appear to contain a C-terminal actin-binding domain that regulates actin remodelling in response to cellular signals and is required for normal cellular morphology, cell division, growth and locomotion in eukaryotes. CAP directly regulates actin filament dynamics and has been implicated in a number of complex developmental and morphological processes, including mRNA localisation and the establishment of cell polarity. Actin exists both as globular (G) (monomeric) actin subunits and assembled into filamentous (F) actin. In cells, actin cycles between these two forms. Proteins that bind F-actin often regulate F-actin assembly and its interaction with other proteins, while proteins that interact with G-actin often control the availability of unpolymerised actin. CAPs bind G-actin. In addition to actin-binding, CAPs can have additional roles, and may act as bifunctional proteins. In Saccharomyces cerevisiae (Baker's yeast), CAP is a component of the adenylyl cyclase complex (Cyr1p) that serves as an effector of Ras during normal cell signalling. S. cerevisiae CAP functions to expose adenylate cyclase binding sites to Ras, thereby enabling adenylate cyclase to be activated by Ras regulatory signals. In Schizosaccharomyces pombe (Fission yeast), CAP is also required for adenylate cyclase activity, but not through the Ras pathway. In both organisms, the N-terminal domain is responsible for adenylate cyclase activation, but the S cerevisiae and S. pombe N-termini cannot complement one another. Yeast CAPs are unique among the CAP family of proteins, because they are the only ones to directly interact with and activate adenylate cyclase []. S. cerevisiae CAP has four major domains. In addition to the N-terminal adenylate cyclase-interacting domain, and the C-terminal actin-binding domain, it possesses two other domains: a proline-rich domain that interacts with Src homology 3 (SH3) domains of specific proteins, and a domain that is responsible for CAP oligomerisation to form multimeric complexes (although oligomerisation appears to involve the N- and C-terminal domains as well). The proline-rich domain interacts with profilin, a protein that catalyses nucleotide exchange on G-actin monomers and promotes addition to barbed ends of filamentous F-actin []. Since CAP can bind profilin via a proline-rich domain, and G-actin via a C-terminal domain, it has been suggested that a ternary G-actin/CAP/profilin complex could be formed.This entry represents the C-terminal domain of CAP proteins, which is responsible for G-actin-binding. This domain has a superhelical structure, where the superhelix turns are made of two β-strands each [].
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Protein Domain
IPR036222 | CAP_N_sf
Type: Homologous_superfamily
Description: Cyclase-associated proteins (CAPs) are highly conserved actin-binding proteins present in a wide range of organisms including yeast, fly, plants, and mammals. CAPs are multifunctional proteins that contain several structural domains. CAP is involved in species-specific signalling pathways [, , , ]. In Drosophila, CAP functions in Hedgehog-mediated eye development and in establishing oocyte polarity. In Dictyostelium (slim mold), CAP is involved in microfilament reorganisation near the plasma membrane in a PIP2-regulated manner and is required to perpetuate the cAMP relay signal to organise fruitbody formation. In plants, CAP is involved in plant signalling pathways required for co-ordinated organ expansion. In yeast, CAP is involved in adenylate cyclase activation, as well as in vesicle trafficking and endocytosis. In both yeast and mammals, CAPs appear to be involved in recycling G-actin monomers from ADF/cofilins for subsequent rounds of filament assembly [, ]. In mammals, there are two different CAPs (CAP1 and CAP2) that share 64% amino acid identity. All CAPs appear to contain a C-terminal actin-binding domain that regulates actin remodelling in response to cellular signals and is required for normal cellular morphology, cell division, growth and locomotion in eukaryotes. CAP directly regulates actin filament dynamics and has been implicated in a number of complex developmental and morphological processes, including mRNA localisation and the establishment of cell polarity. Actin exists both as globular (G) (monomeric) actin subunits and assembled into filamentous (F) actin. In cells, actin cycles between these two forms. Proteins that bind F-actin often regulate F-actin assembly and its interaction with other proteins, while proteins that interact with G-actin often control the availability of unpolymerised actin. CAPs bind G-actin. In addition to actin-binding, CAPs can have additional roles, and may act as bifunctional proteins. In Saccharomyces cerevisiae (Baker's yeast), CAP is a component of the adenylyl cyclase complex (Cyr1p) that serves as an effector of Ras during normal cell signalling. S. cerevisiae CAP functions to expose adenylate cyclase binding sites to Ras, thereby enabling adenylate cyclase to be activated by Ras regulatory signals. In Schizosaccharomyces pombe (Fission yeast), CAP is also required for adenylate cyclase activity, but not through the Ras pathway. In both organisms, the N-terminal domain is responsible for adenylate cyclase activation, but the S cerevisiae and S. pombe N-termini cannot complement one another. Yeast CAPs are unique among the CAP family of proteins, because they are the only ones to directly interact with and activate adenylate cyclase []. S. cerevisiae CAP has four major domains. In addition to the N-terminal adenylate cyclase-interacting domain, and the C-terminal actin-binding domain, it possesses two other domains: a proline-rich domain that interacts with Src homology 3 (SH3) domains of specific proteins, and a domain that is responsible for CAP oligomerisation to form multimeric complexes (although oligomerisation appears to involve the N- and C-terminal domains as well). The proline-rich domain interacts with profilin, a protein that catalyses nucleotide exchange on G-actin monomers and promotes addition to barbed ends of filamentous F-actin []. Since CAP can bind profilin via a proline-rich domain, and G-actin via a C-terminal domain, it has been suggested that a ternary G-actin/CAP/profilin complex could be formed.This entry represents the N-terminal domain of CAP proteins. This domain has an all-alpha structure consisting of six helices in a bundle with a left-handed twist and an up-and-down topology [].
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Protein Domain
IPR013912 | Adenylate_cyclase-assoc_CAP_C
Type: Domain
Description: Cyclase-associated proteins (CAPs) are highly conserved actin-binding proteins present in a wide range of organisms including yeast, fly, plants, and mammals. CAPs are multifunctional proteins that contain several structural domains. CAP is involved in species-specific signalling pathways [, , , ]. In Drosophila, CAP functions in Hedgehog-mediated eye development and in establishing oocyte polarity. In Dictyostelium (slim mold), CAP is involved in microfilament reorganisation near the plasma membrane in a PIP2-regulated manner and is required to perpetuate the cAMP relay signal to organise fruitbody formation. In plants, CAP is involved in plant signalling pathways required for co-ordinated organ expansion. In yeast, CAP is involved in adenylate cyclase activation, as well as in vesicle trafficking and endocytosis. In both yeast and mammals, CAPs appear to be involved in recycling G-actin monomers from ADF/cofilins for subsequent rounds of filament assembly [, ]. In mammals, there are two different CAPs (CAP1 and CAP2) that share 64% amino acid identity. All CAPs appear to contain a C-terminal actin-binding domain that regulates actin remodelling in response to cellular signals and is required for normal cellular morphology, cell division, growth and locomotion in eukaryotes. CAP directly regulates actin filament dynamics and has been implicated in a number of complex developmental and morphological processes, including mRNA localisation and the establishment of cell polarity. Actin exists both as globular (G) (monomeric) actin subunits and assembled into filamentous (F) actin. In cells, actin cycles between these two forms. Proteins that bind F-actin often regulate F-actin assembly and its interaction with other proteins, while proteins that interact with G-actin often control the availability of unpolymerised actin. CAPs bind G-actin. In addition to actin-binding, CAPs can have additional roles, and may act as bifunctional proteins. In Saccharomyces cerevisiae (Baker's yeast), CAP is a component of the adenylyl cyclase complex (Cyr1p) that serves as an effector of Ras during normal cell signalling. S. cerevisiae CAP functions to expose adenylate cyclase binding sites to Ras, thereby enabling adenylate cyclase to be activated by Ras regulatory signals. In Schizosaccharomyces pombe (Fission yeast), CAP is also required for adenylate cyclase activity, but not through the Ras pathway. In both organisms, the N-terminal domain is responsible for adenylate cyclase activation, but the S cerevisiae and S. pombe N-termini cannot complement one another. Yeast CAPs are unique among the CAP family of proteins, because they are the only ones to directly interact with and activate adenylate cyclase []. S. cerevisiae CAP has four major domains. In addition to the N-terminal adenylate cyclase-interacting domain, and the C-terminal actin-binding domain, it possesses two other domains: a proline-rich domain that interacts with Src homology 3 (SH3) domains of specific proteins, and a domain that is responsible for CAP oligomerisation to form multimeric complexes (although oligomerisation appears to involve the N- and C-terminal domains as well). The proline-rich domain interacts with profilin, a protein that catalyses nucleotide exchange on G-actin monomers and promotes addition to barbed ends of filamentous F-actin []. Since CAP can bind profilin via a proline-rich domain, and G-actin via a C-terminal domain, it has been suggested that a ternary G-actin/CAP/profilin complex could be formed.This entry represents the C-terminal domain of CAP proteins, which is responsible for G-actin-binding. This domain has a superhelical structure, where the superhelix turns are made of two β-strands each [].
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Protein Domain
IPR013992 | Adenylate_cyclase-assoc_CAP_N
Type: Domain
Description: Cyclase-associated proteins (CAPs) are highly conserved actin-binding proteins present in a wide range of organisms including yeast, fly, plants, and mammals. CAPs are multifunctional proteins that contain several structural domains. CAP is involved in species-specific signalling pathways [, , , ]. In Drosophila, CAP functions in Hedgehog-mediated eye development and in establishing oocyte polarity. In Dictyostelium (slim mold), CAP is involved in microfilament reorganisation near the plasma membrane in a PIP2-regulated manner and is required to perpetuate the cAMP relay signal to organise fruitbody formation. In plants, CAP is involved in plant signalling pathways required for co-ordinated organ expansion. In yeast, CAP is involved in adenylate cyclase activation, as well as in vesicle trafficking and endocytosis. In both yeast and mammals, CAPs appear to be involved in recycling G-actin monomers from ADF/cofilins for subsequent rounds of filament assembly [, ]. In mammals, there are two different CAPs (CAP1 and CAP2) that share 64% amino acid identity. All CAPs appear to contain a C-terminal actin-binding domain that regulates actin remodelling in response to cellular signals and is required for normal cellular morphology, cell division, growth and locomotion in eukaryotes. CAP directly regulates actin filament dynamics and has been implicated in a number of complex developmental and morphological processes, including mRNA localisation and the establishment of cell polarity. Actin exists both as globular (G) (monomeric) actin subunits and assembled into filamentous (F) actin. In cells, actin cycles between these two forms. Proteins that bind F-actin often regulate F-actin assembly and its interaction with other proteins, while proteins that interact with G-actin often control the availability of unpolymerised actin. CAPs bind G-actin. In addition to actin-binding, CAPs can have additional roles, and may act as bifunctional proteins. In Saccharomyces cerevisiae (Baker's yeast), CAP is a component of the adenylyl cyclase complex (Cyr1p) that serves as an effector of Ras during normal cell signalling. S. cerevisiae CAP functions to expose adenylate cyclase binding sites to Ras, thereby enabling adenylate cyclase to be activated by Ras regulatory signals. In Schizosaccharomyces pombe (Fission yeast), CAP is also required for adenylate cyclase activity, but not through the Ras pathway. In both organisms, the N-terminal domain is responsible for adenylate cyclase activation, but the S cerevisiae and S. pombe N-termini cannot complement one another. Yeast CAPs are unique among the CAP family of proteins, because they are the only ones to directly interact with and activate adenylate cyclase []. S. cerevisiae CAP has four major domains. In addition to the N-terminal adenylate cyclase-interacting domain, and the C-terminal actin-binding domain, it possesses two other domains: a proline-rich domain that interacts with Src homology 3 (SH3) domains of specific proteins, and a domain that is responsible for CAP oligomerisation to form multimeric complexes (although oligomerisation appears to involve the N- and C-terminal domains as well). The proline-rich domain interacts with profilin, a protein that catalyses nucleotide exchange on G-actin monomers and promotes addition to barbed ends of filamentous F-actin []. Since CAP can bind profilin via a proline-rich domain, and G-actin via a C-terminal domain, it has been suggested that a ternary G-actin/CAP/profilin complex could be formed.This entry represents the N-terminal domain of CAP proteins. This domain has an all-alpha structure consisting of six helices in a bundle with a left-handed twist and an up-and-down topology [].
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Protein
Q80TM9
Organism: Mus musculus/domesticus
Length: 1593  
Fragment?: false
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Protein
Q8VCM2
Organism: Mus musculus/domesticus
Length: 349  
Fragment?: false
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Protein
Q923U0
Organism: Mus musculus/domesticus
Length: 474  
Fragment?: false
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Protein
Q9WV80
Organism: Mus musculus/domesticus
Length: 522  
Fragment?: false
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Protein
Q811P8
Organism: Mus musculus/domesticus
Length: 2089  
Fragment?: false
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Protein
Q9D8U8
Organism: Mus musculus/domesticus
Length: 404  
Fragment?: false
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Protein
Q8CFD4
Organism: Mus musculus/domesticus
Length: 459  
Fragment?: false
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Protein
Q6P8X1
Organism: Mus musculus/domesticus
Length: 406  
Fragment?: false
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Protein
Q8BVL3
Organism: Mus musculus/domesticus
Length: 470  
Fragment?: false
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Protein
P59729
Organism: Mus musculus/domesticus
Length: 980  
Fragment?: false
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Protein
Q9CWK8
Organism: Mus musculus/domesticus
Length: 519  
Fragment?: false
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Protein
Q91YJ2
Organism: Mus musculus/domesticus
Length: 450  
Fragment?: false
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Protein
Q5SRX1
Organism: Mus musculus/domesticus
Length: 507  
Fragment?: false
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Protein
Q6NZD2
Organism: Mus musculus/domesticus
Length: 521  
Fragment?: false
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Protein
Q7TNI6
Organism: Mus musculus/domesticus
Length: 474  
Fragment?: false
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Protein
Q3U0I9
Organism: Mus musculus/domesticus
Length: 411  
Fragment?: false
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Protein
Q8BZR6
Organism: Mus musculus/domesticus
Length: 397  
Fragment?: false
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Protein
Q91VZ1
Organism: Mus musculus/domesticus
Length: 519  
Fragment?: false
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Protein
Q3TT02
Organism: Mus musculus/domesticus
Length: 411  
Fragment?: false
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Protein
Q3TI63
Organism: Mus musculus/domesticus
Length: 522  
Fragment?: false
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Protein
Q80X54
Organism: Mus musculus/domesticus
Length: 403  
Fragment?: false
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Protein
Q3TJN6
Organism: Mus musculus/domesticus
Length: 404  
Fragment?: false
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Protein
Q8C5E7
Organism: Mus musculus/domesticus
Length: 404  
Fragment?: false
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Protein
Q3U4S1
Organism: Mus musculus/domesticus
Length: 522  
Fragment?: false
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Protein
Q3U5L3
Organism: Mus musculus/domesticus
Length: 519  
Fragment?: false
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Protein
Q80YA2
Organism: Mus musculus/domesticus
Length: 234  
Fragment?: false
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Protein
Q3TM19
Organism: Mus musculus/domesticus
Length: 980  
Fragment?: false
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Protein
Q3UDY9
Organism: Mus musculus/domesticus
Length: 492  
Fragment?: true
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Protein
Q5SXA4
Organism: Mus musculus/domesticus
Length: 462  
Fragment?: false
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Protein
Q3U3Y6
Organism: Mus musculus/domesticus
Length: 980  
Fragment?: false
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Protein
Q5SXA5
Organism: Mus musculus/domesticus
Length: 457  
Fragment?: false
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Protein
Q80WA0
Organism: Mus musculus/domesticus
Length: 980  
Fragment?: false
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Protein
Q0VDT6
Organism: Mus musculus/domesticus
Length: 336  
Fragment?: true
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Protein
Q80ZW1
Organism: Mus musculus/domesticus
Length: 337  
Fragment?: false
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Publication
15311924 | -
First Author: Dodatko T
Year: 2004
Journal: Biochemistry
Title: Crystal structure of the actin binding domain of the cyclase-associated protein.
Volume: 43
Issue: 33
Pages: 10628-41
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Publication
12962635 | -
First Author: Ksiazek D
Year: 2003
Journal: Structure
Title: Structure of the N-terminal domain of the adenylyl cyclase-associated protein (CAP) from Dictyostelium discoideum.
Volume: 11
Issue: 9
Pages: 1171-8
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Publication
9344857 | -
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
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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
12034353 | -
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
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Publication
18765673 | J:142544
First Author: Ruusala A
Year: 2008
Journal: J Biol Chem
Title: Nck adapters are involved in the formation of dorsal ruffles, cell migration, and Rho signaling downstream of the platelet-derived growth factor beta receptor.
Volume: 283
Issue: 44
Pages: 30034-44
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Protein
P97504
Organism: Mus musculus/domesticus
Length: 651  
Fragment?: false
•
•
•
•
•
Protein
P24604
Organism: Mus musculus/domesticus
Length: 630  
Fragment?: false
•
•
•
•
•
Protein
Q3U436
Organism: Mus musculus/domesticus
Length: 630  
Fragment?: false
•
•
•
•
•
Protein
B1AUL5
Organism: Mus musculus/domesticus
Length: 651  
Fragment?: false
•
•
•
•
•
Publication
11034371 | J:118029
First Author: Assarsson E
Year: 2000
Journal: J Immunol
Title: CD8+ T cells rapidly acquire NK1.1 and NK cell-associated molecules upon stimulation in vitro and in vivo.
Volume: 165
Issue: 7
Pages: 3673-9
•
•
•
•
•
Publication
27474268 | J:239186
First Author: Voisinne G
Year: 2016
Journal: Mol Syst Biol
Title: Co-recruitment analysis of the CBL and CBLB signalosomes in primary T cells identifies CD5 as a key regulator of TCR-induced ubiquitylation.
Volume: 12
Issue: 7
Pages: 876
•
•
•
•
•
Publication
15735648 | J:97609
First Author: Salvador JM
Year: 2005
Journal: Nat Immunol
Title: Alternative p38 activation pathway mediated by T cell receptor-proximal tyrosine kinases.
Volume: 6
Issue: 4
Pages: 390-5
•
•
•
•
•
Publication
19917692 | J:157513
First Author: Salmond RJ
Year: 2009
Journal: J Immunol
Title: MAPK, phosphatidylinositol 3-kinase, and mammalian target of rapamycin pathways converge at the level of ribosomal protein S6 phosphorylation to control metabolic signaling in CD8 T cells.
Volume: 183
Issue: 11
Pages: 7388-97
•
•
•
•
•
Publication
15102471 | J:114108
First Author: Papin J
Year: 2004
Journal: Curr Opin Biotechnol
Title: Bioinformatics and cellular signaling.
Volume: 15
Issue: 1
Pages: 78-81
•
•
•
•
•
Publication
17947660 | -
First Author: Cao L
Year: 2007
Journal: J Immunol
Title: Quantitative time-resolved phosphoproteomic analysis of mast cell signaling.
Volume: 179
Issue: 9
Pages: 5864-76
•
•
•
•
•
Publication
19386638 | J:173286
 
First Author: Long JE
Year: 2009
Journal: Cereb Cortex
Title: Dlx1&2 and Mash1 transcription factors control MGE and CGE patterning and differentiation through parallel and overlapping pathways.
Volume: 19 Suppl 1
Pages: i96-106
•
•
•
•
•
Publication
- | J:58777
     
First Author: Elliott R
Year: 2000
Journal: Personal Communication
Title: Chromosome Locations Based on RH mapping
•
•
•
•
•
Publication
- | J:165964
     
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
•
•
•
•
•
Protein
P14234
Organism: Mus musculus/domesticus
Length: 517  
Fragment?: false
•
•
•
•
•
Protein
P41241
Organism: Mus musculus/domesticus
Length: 450  
Fragment?: false
•
•
•
•
•
Protein
P40124
Organism: Mus musculus/domesticus
Length: 474  
Fragment?: false
•
•
•
•
•
Protein
P41242
Organism: Mus musculus/domesticus
Length: 505  
Fragment?: false
•
•
•
•
•
Protein
Q9CYT6
Organism: Mus musculus/domesticus
Length: 476  
Fragment?: false
•
•
•
•
•
Protein
P42682
Organism: Mus musculus/domesticus
Length: 527  
Fragment?: false
•
•
•
•
•
Protein
Q04736
Organism: Mus musculus/domesticus
Length: 541  
Fragment?: false
•
•
•
•
•
Protein
P43404
Organism: Mus musculus/domesticus
Length: 618  
Fragment?: false
•
•
•
•
•
Protein
Q3TC53
Organism: Mus musculus/domesticus
Length: 474  
Fragment?: false
•
•
•
•
•
Protein
I6L9F0
Organism: Mus musculus/domesticus
Length: 445  
Fragment?: false
•
•
•
•
•
Protein
Q3U0U5
Organism: Mus musculus/domesticus
Length: 474  
Fragment?: false
•
•
•
•
•
Protein
Q9D6H7
Organism: Mus musculus/domesticus
Length: 465  
Fragment?: false
•
•
•
•
•
Protein
Q3UNQ0
Organism: Mus musculus/domesticus
Length: 474  
Fragment?: false
•
•
•
•
•
Protein
Q3TJI7
Organism: Mus musculus/domesticus
Length: 541  
Fragment?: false
•
•
•
•
•
Protein
Q3TH41
Organism: Mus musculus/domesticus
Length: 608  
Fragment?: false
•
•
•
•
•
Protein
Q8CBP1
Organism: Mus musculus/domesticus
Length: 541  
Fragment?: false
•
•
•
•
•
Protein
D3YTR7
Organism: Mus musculus/domesticus
Length: 364  
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.

Copyright © 2017 by The Jackson Laboratory. All Rights Reserved

© 2002 - 2017 Department of Genetics, University of Cambridge, Downing Street,
Cambridge CB2 3EH, United Kingdom