| Type |
Details |
Score |
| Protein Domain |
| Type: |
Domain |
| Description: |
Ephexin-1 is a RhoGEF (Rho-type guanine nucleotide exchange factor) that activates RhoA, Tac1, and Cdc42 by exchanging bound GDP for free GTP []. It is expressed mainly in the brain in a region associated with movement control. It regulates the stability of postsynaptic acetylcholine receptor (AChR) clusters and thus plays a critical role in the maturation and neurotransmission of neuromuscular junctions []. Ephexin-1 directly interacts with the ephrin receptor EphA4 and their coexpression enhances the ability of ephexin-1 to activate RhoA []. It is required for normal axon growth and EphA-induced growth cone collapse []. Ephexin-1 contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH) and SH3 domains. This entry represents the SH3 domain. |
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•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
This entry represents the SH3 domain found in srGAP proteins 1, 2 and 3. srGAP1 (also called ARHGAP13) is a key GTPase activating protein (GAP) downstream of Slit-Robo pathway, and has been shown to inhibit neuronal migration and glioma cell invasion by reducing the activation of Cdc42 []. srGAP2 (ARHGAP34) regulates neuronal morphogenesis through the ability of its F-BAR domain to regulate membrane deformation and induce filopodia formation []. srGAP3 (ARHGAP14) interacts with lamellipodin at the cell membrane and regulates Rac-dependent cellular protrusions []. The SLIT-ROBO Rho GTPase-activating protein (srGAP) family consists of four members: srGAP1, -2, -3 and -4. They contain F-BAR, RhoGAP and SH3 domains. Their RhoGAP domain is involved in negative regulation of Rho GTPase activities important for cytoskeleton rearrangement []. The srGAP family members have an "inverse F-BAR"or IF-BAR domain that is distinct from other F-BAR domains such as FBP17. They are multifunctional adaptor proteins involved in various aspects of neuronal development []. |
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•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
This entry represents the SH3 domain of srGAP4. srGAP4 is highly expressed in hematopoietic cells and may play a role in lymphocyte differentiation []. It is able to stimulate the GTPase activity of three members of Rho GTPases, Rac1, Cdc42 and RhoA. In the nervous system, srGAP4 has been detected in differentiating neurites and may be involved in axon and dendritic growth [].The SLIT-ROBO Rho GTPase-activating protein (srGAP) family consists of four members: srGAP1, -2, -3 and -4. They contain F-BAR, RhoGAP and SH3 domains. Their RhoGAP domain is involved in negative regulation of Rho GTPase activities important for cytoskeleton rearrangement []. The srGAP family members have an "inverse F-BAR"or IF-BAR domain that is distinct from other F-BAR domains such as FBP17. They are multifunctional adaptor proteins involved in various aspects of neuronal development []. |
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•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
VAV2 is widely expressed and functions as a guanine nucleotide exchange factor (GEF) for RhoA, RhoB and RhoG and also activates Rac1 and Cdc42 []. It is implicated in many cellular and physiological functions including blood pressure control, eye development, neurite outgrowth and branching, EGFR endocytosis and degradation, and cell cluster morphology, among others [, , , , ]. It has been reported to associate with Nek3. VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. The SH3 domain of VAV is involved in the localization of proteins to specific sites within the cell, by interacting with proline-rich sequences within target proteins [, , ].This entry represents the second SH3 domain of VAV2. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
VAV2 is widely expressed and functions as a guanine nucleotide exchange factor (GEF) for RhoA, RhoB and RhoG and also activates Rac1 and Cdc42 []. It is implicated in many cellular and physiological functions including blood pressure control, eye development, neurite outgrowth and branching, EGFR endocytosis and degradation, and cell cluster morphology, among others [, , , , ]. It has been reported to associate with Nek3. VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. The SH3 domain of VAV is involved in the localization of proteins to specific sites within the cell, by interacting with proline-rich sequences within target proteins [, , ].This entry represents the first SH3 domain of VAV2. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
Intersectin-2 (ITSN2) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction []. It plays a role in clathrin-coated pit (CCP) formation []. It binds to many proteins through its multidomain structure and facilitates the assembly of multimeric complexes. ITSN2 also functions as a specific GEF for Cdc42 activation in epithelial morphogenesis, and is required in mitotic spindle orientation []. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. This entry represents the first SH3 domain of ITSN2. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
Intersectin-2 (ITSN2) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction []. It plays a role in clathrin-coated pit(CCP) formation []. It binds to many proteins through its multidomain structure and facilitates the assembly of multimeric complexes. ITSN2 also functions as a specific GEF for Cdc42 activation in epithelial morphogenesis, and is required in mitotic spindle orientation []. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. This entry represents the second SH3 domain of ITSN2. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
Intersectin-2 (ITSN2) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction []. It plays a role in clathrin-coated pit (CCP) formation []. It binds to many proteins through its multidomain structure and facilitates the assembly of multimeric complexes. ITSN2 also functions as a specific GEF for Cdc42 activation in epithelial morphogenesis, and is required in mitotic spindle orientation []. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. This entry represents the third SH3 domain of ITSN2. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
Intersectin-2 (ITSN2) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction []. It plays a role in clathrin-coated pit (CCP) formation []. It binds to many proteins through its multidomain structure and facilitates the assembly of multimeric complexes. ITSN2 also functions as a specific GEF for Cdc42 activation in epithelial morphogenesis, and is required in mitotic spindle orientation []. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. This entry represents the fourth SH3 domain of ITSN2. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
Intersectin-2 (ITSN2) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction []. It plays a role in clathrin-coated pit (CCP) formation []. It binds to many proteins through its multidomain structure and facilitates the assembly of multimeric complexes. ITSN2 also functions as a specific GEF for Cdc42 activation in epithelial morphogenesis, and is required in mitotic spindle orientation []. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. This entry represents the fifth SH3 domain of ITSN2. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
Beta-PIX, also called Rho guanine nucleotide exchange factor 7 (ARHGEF7) or Cool (Cloned out of Library)-1, activates small GTPases by exchanging bound GDP for free GTP. It acts as a GEF for both Cdc42 and Rac1 [], and plays important roles in regulating neuroendocrine exocytosis, focal adhesion maturation, cell migration, synaptic vesicle localization, and insulin secretion [, , , ].PIX proteins contain an N-terminal SH3 domain followed by RhoGEF (also called Dbl-homologous or DH) and Pleckstrin Homology (PH) domains, and a C-terminal leucine-zipper domain for dimerization. The SH3 domain of PIX binds to an atypical PxxxPR motif in p21-activated kinases (PAKs) with high affinity. The binding of PAKs to PIX facilitate the localization of PAKs to focal complexes and also localizes PAKs to PIX targets Cdc43 and Rac, leading to the activation of PAKs [, ].This entry represents the SH3 domain of beta-PIX. |
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•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
PAK2 plays a role in pro-apoptotic signaling. It is cleaved and activated by caspases leading to morphological changes during apoptosis []. PAK2 is also activated in response to a variety of stresses including DNA damage, hyperosmolarity, serum starvation, and contact inhibition, and may play a role in coordinating the stress response []. PAK2 also contributes to cancer cell invasion through a mechanism distinct from that of PAK1 []. PAK2 belongs to the group I PAKs.Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac []. |
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•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
PAK6 may play a role in stress responses through its activation by the mitogen-activated protein kinase (MAPK) p38 and MAPK kinase 6 (MKK6) pathway []. PAK6 is highly expressed in the brain. It is not required for viability, but together with PAK5, it is required for normal levels of locomotion and activity, and for learning and memory []. Increased expression of PAK6 is found in primary and metastatic prostate cancer [].PAK6 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites []. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Abr (active breakpoint cluster region-related protein) and Bcr (breakpoint cluster region protein) are homologous proteins containing a C-terminal domain with GTPase-activating protein (GAP) activity specific for Rac. They control multiple cellular functions of murine macrophages []. They contain several domains, including tandem DH-PH, C2 and GAP domains. Bcr has an extra N-terminal oligomerization domain []. Bcr has been shown to fused to Abl tyrosine kinase in leukemia. The fusion of Bcr to Abl deregulates the tyrosine kinase activity of Abl []. The N-terminal oligomerization domain is thought to be the most critical component that allows the formation of homo-tetramer Bcr/Abl complexes and deregulates the Abl tyrosine kinase [, ]. The GTPase-activating activity of Bcr has been shown to be regulated by transglutaminase 2 (TG2), a multifunctional protein that has been implicated in numerous pathologies including that of neurodegeneration and celiac disease [, ].Abr is a critical regulator of Rho and Cdc42 during the single cell wound healing []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
Rho GTPase-activating protein 26 (ARHGAP26), also known as GTPase regulator associated with focal adhesion kinase (GRAF), is a GTPase-activating protein for the small GTPases of the Rho family RhoA and CDC42 [, ]. GRAF influences cytoskeletal changes mediated by Rho proteins []. It is recognised as a tumor suppressor []. GRAF contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, a Rho GAP domain, and a C-terminal SH3 domain. The SH3 domain of GRAF binds PKNbeta, a target of the small GTPase Rho [].This entry represents the BAR domain of GRAF. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The BAR domain of GRAF directly interacts with its Rho GAP domain and inhibits its activity. Autoinhibited GRAF is capable of binding membranes and tubulating liposomes, showing that the membrane-tubulation and GAP-inhibitory functions of the BAR domain can occur simultaneously []. |
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•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
NDE-like 1 (NDEL1/NUDEL) and its paralogue, NDE, are involved in mitosis and neurodevelopment that have been implicated in psychiatric and neurodevelopmental disorders. NDEL1 contains the N-terminal LIS1-binding domain that stimulates the movement of dynein and the C-terminal domain that causes dynein-microtubule dissociation [, , ]. It can also bind the motor domain of dynein in its heavy-chain []. It has been shown to affect many aspects of dynein function, such as transport along the microtubule network of vesicles and lysosomes, with effects on the correct structure of the Golgi apparatus, as well as on the transport of intermediate filament proteins, short microtubules and viral glycoproteins. Its phosphorilation by Aurora-A kinase is essential for centrosomal separation and mitotic entry []. It also facilitates neurofilament polymerization, promotes axonal regeneration, regulates Cdc42 at the leading edge of migrating neurons and the GTPase activity of the microtubule remodeling protein Dynamin 2, etc [, ]. |
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•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
167
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
174
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
92
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
181
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
188
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
249
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
254
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Bokoch GM |
| Year: |
1998 |
| Journal: |
Cell Death Differ |
| Title: |
Caspase-mediated activation of PAK2 during apoptosis: proteolytic kinase activation as a general mechanism of apoptotic signal transduction? |
| Volume: |
5 |
| Issue: |
8 |
| Pages: |
637-45 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Roig J |
| Year: |
2001 |
| Journal: |
Vitam Horm |
| Title: |
Cytostatic p21 G protein-activated protein kinase gamma-PAK. |
| Volume: |
62 |
|
| Pages: |
167-98 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Coniglio SJ |
| Year: |
2008 |
| Journal: |
Mol Cell Biol |
| Title: |
Pak1 and Pak2 mediate tumor cell invasion through distinct signaling mechanisms. |
| Volume: |
28 |
| Issue: |
12 |
| Pages: |
4162-72 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Moon MS |
| Year: |
2010 |
| Journal: |
Mol Cell Neurosci |
| Title: |
Balanced Vav2 GEF activity regulates neurite outgrowth and branching in vitro and in vivo. |
| Volume: |
44 |
| Issue: |
2 |
| Pages: |
118-28 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Thalappilly S |
| Year: |
2010 |
| Journal: |
Oncogene |
| Title: |
VAV2 regulates epidermal growth factor receptor endocytosis and degradation. |
| Volume: |
29 |
| Issue: |
17 |
| Pages: |
2528-39 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Sauzeau V |
| Year: |
2010 |
| Journal: |
J Clin Invest |
| Title: |
The Rho/Rac exchange factor Vav2 controls nitric oxide-dependent responses in mouse vascular smooth muscle cells. |
| Volume: |
120 |
| Issue: |
1 |
| Pages: |
315-30 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Holthusen K |
| Year: |
2009 |
| Journal: |
Am J Ther |
| Title: |
Guanine exchange factor Vav2: a novel potential target for the development of drugs effective in the prevention of papillomavirus infection and disease. |
| Volume: |
16 |
| Issue: |
6 |
| Pages: |
496-507 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Arora PD |
| Year: |
2008 |
| Journal: |
Am J Physiol Cell Physiol |
| Title: |
Collagen phagocytosis is regulated by the guanine nucleotide exchange factor Vav2. |
| Volume: |
295 |
| Issue: |
1 |
| Pages: |
C130-7 |
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•
•
•
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| Publication |
| First Author: |
Nie J |
| Year: |
2012 |
| Journal: |
J Biol Chem |
| Title: |
Synapses of amphids defective (SAD-A) kinase promotes glucose-stimulated insulin secretion through activation of p21-activated kinase (PAK1) in pancreatic β-Cells. |
| Volume: |
287 |
| Issue: |
31 |
| Pages: |
26435-44 |
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•
•
•
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| Publication |
| First Author: |
Bagrodia S |
| Year: |
1999 |
| Journal: |
J Biol Chem |
| Title: |
A tyrosine-phosphorylated protein that binds to an important regulatory region on the cool family of p21-activated kinase-binding proteins. |
| Volume: |
274 |
| Issue: |
32 |
| Pages: |
22393-400 |
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•
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| Publication |
| First Author: |
Kuroiwa M |
| Year: |
2011 |
| Journal: |
J Cell Sci |
| Title: |
The guanine nucleotide exchange factor Arhgef5 plays crucial roles in Src-induced podosome formation. |
| Volume: |
124 |
| Issue: |
Pt 10 |
| Pages: |
1726-38 |
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•
•
•
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| Publication |
| First Author: |
Sakai H |
| Year: |
2006 |
| Journal: |
Bone |
| Title: |
Activated c-Fms recruits Vav and Rac during CSF-1-induced cytoskeletal remodeling and spreading in osteoclasts. |
| Volume: |
39 |
| Issue: |
6 |
| Pages: |
1290-301 |
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•
•
•
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| Publication |
| First Author: |
Sampaio NG |
| Year: |
2011 |
| Journal: |
J Cell Sci |
| Title: |
Phosphorylation of CSF-1R Y721 mediates its association with PI3K to regulate macrophage motility and enhancement of tumor cell invasion. |
| Volume: |
124 |
| Issue: |
Pt 12 |
| Pages: |
2021-31 |
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•
•
•
•
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| Publication |
| First Author: |
Neudauer CL |
| Year: |
2001 |
| Journal: |
Biochem Biophys Res Commun |
| Title: |
PIST: a novel PDZ/coiled-coil domain binding partner for the rho-family GTPase TC10. |
| Volume: |
280 |
| Issue: |
2 |
| Pages: |
541-7 |
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•
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| Publication |
| First Author: |
Yamaguchi A |
| Year: |
1997 |
| Journal: |
J Biol Chem |
| Title: |
An Eps homology (EH) domain protein that binds to the Ral-GTPase target, RalBP1. |
| Volume: |
272 |
| Issue: |
50 |
| Pages: |
31230-4 |
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•
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| First Author: |
Jenna S |
| Year: |
2002 |
| Journal: |
J Biol Chem |
| Title: |
The activity of the GTPase-activating protein CdGAP is regulated by the endocytic protein intersectin. |
| Volume: |
277 |
| Issue: |
8 |
| Pages: |
6366-73 |
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•
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| First Author: |
Kurogane Y |
| Year: |
2012 |
| Journal: |
Arterioscler Thromb Vasc Biol |
| Title: |
FGD5 mediates proangiogenic action of vascular endothelial growth factor in human vascular endothelial cells. |
| Volume: |
32 |
| Issue: |
4 |
| Pages: |
988-96 |
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•
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| First Author: |
Holland PM |
| Year: |
1997 |
| Journal: |
J Biol Chem |
| Title: |
MKK7 is a stress-activated mitogen-activated protein kinase kinase functionally related to hemipterous. |
| Volume: |
272 |
| Issue: |
40 |
| Pages: |
24994-8 |
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•
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•
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| First Author: |
Foltz IN |
| Year: |
1998 |
| Journal: |
J Biol Chem |
| Title: |
Human mitogen-activated protein kinase kinase 7 (MKK7) is a highly conserved c-Jun N-terminal kinase/stress-activated protein kinase (JNK/SAPK) activated by environmental stresses and physiological stimuli. |
| Volume: |
273 |
| Issue: |
15 |
| Pages: |
9344-51 |
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| First Author: |
Yuan Z |
| Year: |
2019 |
| Journal: |
Cells |
| Title: |
Agenesis and Hypomyelination of Corpus Callosum in Mice Lacking Nsun5, an RNA Methyltransferase. |
| Volume: |
8 |
| Issue: |
6 |
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| First Author: |
Kreis P |
| Year: |
2007 |
| Journal: |
J Biol Chem |
| Title: |
The p21-activated kinase 3 implicated in mental retardation regulates spine morphogenesis through a Cdc42-dependent pathway. |
| Volume: |
282 |
| Issue: |
29 |
| Pages: |
21497-506 |
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| First Author: |
Shaheen R |
| Year: |
2011 |
| Journal: |
Am J Hum Genet |
| Title: |
Recessive mutations in DOCK6, encoding the guanidine nucleotide exchange factor DOCK6, lead to abnormal actin cytoskeleton organization and Adams-Oliver syndrome. |
| Volume: |
89 |
| Issue: |
2 |
| Pages: |
328-33 |
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•
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| First Author: |
Ikeda W |
| Year: |
2001 |
| Journal: |
Biochem Biophys Res Commun |
| Title: |
Identification of splicing variants of Frabin with partly different functions and tissue distribution. |
| Volume: |
286 |
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5 |
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1066-72 |
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| First Author: |
Bryan BA |
| Year: |
2005 |
| Journal: |
Mol Cell Biol |
| Title: |
Modulation of muscle regeneration, myogenesis, and adipogenesis by the Rho family guanine nucleotide exchange factor GEFT. |
| Volume: |
25 |
| Issue: |
24 |
| Pages: |
11089-101 |
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| First Author: |
Gerwins P |
| Year: |
1997 |
| Journal: |
J Biol Chem |
| Title: |
Cloning of a novel mitogen-activated protein kinase kinase kinase, MEKK4, that selectively regulates the c-Jun amino terminal kinase pathway. |
| Volume: |
272 |
| Issue: |
13 |
| Pages: |
8288-95 |
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•
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| First Author: |
Himmel KL |
| Year: |
2002 |
| Journal: |
J Biol Chem |
| Title: |
Activation of clg, a novel dbl family guanine nucleotide exchange factor gene, by proviral insertion at evi24, a common integration site in B cell and myeloid leukemias. |
| Volume: |
277 |
| Issue: |
16 |
| Pages: |
13463-72 |
|
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•
•
•
•
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| Publication |
| First Author: |
Quilliam LA |
| Year: |
1996 |
| Journal: |
J Biol Chem |
| Title: |
Isolation of a NCK-associated kinase, PRK2, an SH3-binding protein and potential effector of Rho protein signaling. |
| Volume: |
271 |
| Issue: |
46 |
| Pages: |
28772-6 |
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•
•
•
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| First Author: |
Benesch S |
| Year: |
2002 |
| Journal: |
J Biol Chem |
| Title: |
Phosphatidylinositol 4,5-biphosphate (PIP2)-induced vesicle movement depends on N-WASP and involves Nck, WIP, and Grb2. |
| Volume: |
277 |
| Issue: |
40 |
| Pages: |
37771-6 |
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