Type |
Details |
Score |
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1402
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
2057
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1280
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
428
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
2776
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
985
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1255
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1171
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
595
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
920
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
802
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1345
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
428
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
913
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1077
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
946
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
648
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
439
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1501
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
814
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1944
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
2089
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1107
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1167
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
284
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
526
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
859
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1581
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1543
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
628
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
618
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1149
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
529
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
983
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1650
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
763
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
210
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
2114
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1031
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1552
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
868
 |
Fragment?: |
false |
|
•
•
•
•
•
|
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. |
|
•
•
•
•
•
|
Publication |
First Author: |
Krause-Gruszczynska M |
Year: |
2011 |
Journal: |
Cell Commun Signal |
Title: |
The signaling pathway of Campylobacter jejuni-induced Cdc42 activation: Role of fibronectin, integrin beta1, tyrosine kinases and guanine exchange factor Vav2. |
Volume: |
9 |
|
Pages: |
32 |
|
•
•
•
•
•
|
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 |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
103
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
745
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1388
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1354
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1499
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Arthur WT |
Year: |
2002 |
Journal: |
J Biol Chem |
Title: |
XPLN, a guanine nucleotide exchange factor for RhoA and RhoB, but not RhoC. |
Volume: |
277 |
Issue: |
45 |
Pages: |
42964-72 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner []. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity []. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane []. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes [].ARHGEF3 (also known as XPLN) is a guanine nucleotide exchange factor (GEF) for RhoA and RhoB GTPases []. It contains a tandem Dbl homology and a PH domain. This entry represents the PH domain. |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
178
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Wang Z |
Year: |
2009 |
Journal: |
J Biol Chem |
Title: |
Regulation of immature dendritic cell migration by RhoA guanine nucleotide exchange factor Arhgef5. |
Volume: |
284 |
Issue: |
42 |
Pages: |
28599-606 |
|
•
•
•
•
•
|
Publication |
First Author: |
Albright CF |
Year: |
1993 |
Journal: |
EMBO J |
Title: |
Characterization of a guanine nucleotide dissociation stimulator for a ras-related GTPase. |
Volume: |
12 |
Issue: |
1 |
Pages: |
339-47 |
|
•
•
•
•
•
|
Publication |
First Author: |
Dottori M |
Year: |
2001 |
Journal: |
Development |
Title: |
The winged-helix transcription factor Foxd3 suppresses interneuron differentiation and promotes neural crest cell fate. |
Volume: |
128 |
Issue: |
21 |
Pages: |
4127-38 |
|
•
•
•
•
•
|
Publication |
First Author: |
Parikh VN |
Year: |
2012 |
Journal: |
Circulation |
Title: |
MicroRNA-21 integrates pathogenic signaling to control pulmonary hypertension: results of a network bioinformatics approach. |
Volume: |
125 |
Issue: |
12 |
Pages: |
1520-32 |
|
•
•
•
•
•
|
Publication |
First Author: |
Stankiewicz TR |
Year: |
2020 |
Journal: |
Neurobiol Dis |
Title: |
Dysregulation of Rac or Rho elicits death of motor neurons and activation of these GTPases is altered in the G93A mutant hSOD1 mouse model of amyotrophic lateral sclerosis. |
Volume: |
136 |
|
Pages: |
104743 |
|
•
•
•
•
•
|
Publication |
First Author: |
Jackson B |
Year: |
2011 |
Journal: |
Mol Biol Cell |
Title: |
RhoA is dispensable for skin development, but crucial for contraction and directed migration of keratinocytes. |
Volume: |
22 |
Issue: |
5 |
Pages: |
593-605 |
|
•
•
•
•
•
|
Publication |
First Author: |
Behrends J |
Year: |
2005 |
Journal: |
Mol Cell Biol |
Title: |
Normal thyroid structure and function in rhophilin 2-deficient mice. |
Volume: |
25 |
Issue: |
7 |
Pages: |
2846-52 |
|
•
•
•
•
•
|
Publication |
First Author: |
Melendez J |
Year: |
2011 |
Journal: |
J Biol Chem |
Title: |
RhoA GTPase is dispensable for actomyosin regulation but is essential for mitosis in primary mouse embryonic fibroblasts. |
Volume: |
286 |
Issue: |
17 |
Pages: |
15132-7 |
|
•
•
•
•
•
|
Publication |
First Author: |
Reichova A |
Year: |
2020 |
Journal: |
Mol Cell Endocrinol |
Title: |
Abnormal neuronal morphology and altered synaptic proteins are restored by oxytocin in autism-related SHANK3 deficient model. |
Volume: |
518 |
|
Pages: |
110924 |
|
•
•
•
•
•
|
Publication |
First Author: |
Krzyzosiak WJ |
Year: |
1992 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
Isolation of genes specifically expressed in flat revertant cells derived from activated ras-transformed NIH 3T3 cells by treatment with azatyrosine. |
Volume: |
89 |
Issue: |
11 |
Pages: |
4879-83 |
|
•
•
•
•
•
|
Publication |
First Author: |
Miura Y |
Year: |
1993 |
Journal: |
J Biol Chem |
Title: |
Regulation of morphology by rho p21 and its inhibitory GDP/GTP exchange protein (rho GDI) in Swiss 3T3 cells. |
Volume: |
268 |
Issue: |
1 |
Pages: |
510-5 |
|
•
•
•
•
•
|
Publication |
First Author: |
del Peso L |
Year: |
1997 |
Journal: |
Oncogene |
Title: |
Rho proteins induce metastatic properties in vivo. |
Volume: |
15 |
Issue: |
25 |
Pages: |
3047-57 |
|
•
•
•
•
•
|
Publication |
First Author: |
Huang GX |
Year: |
2017 |
Journal: |
Cancer Lett |
Title: |
Up-regulation of Rho-associated kinase 1/2 by glucocorticoids promotes migration, invasion and metastasis of melanoma. |
Volume: |
410 |
|
Pages: |
1-11 |
|
•
•
•
•
•
|
Publication |
First Author: |
Du J |
Year: |
2017 |
Journal: |
Int J Dev Neurosci |
Title: |
MiR-194 is involved in morphogenesis of spiral ganglion neurons in inner ear by rearranging actin cytoskeleton via targeting RhoB. |
Volume: |
63 |
|
Pages: |
16-26 |
|
•
•
•
•
•
|
Publication |
First Author: |
Müller FU |
Year: |
2005 |
Journal: |
J Biol Chem |
Title: |
Heart-directed expression of a human cardiac isoform of cAMP-response element modulator in transgenic mice. |
Volume: |
280 |
Issue: |
8 |
Pages: |
6906-14 |
|
•
•
•
•
•
|
Publication |
First Author: |
Romero F |
Year: |
1996 |
Journal: |
Cell Signal |
Title: |
Structure and function of vav. |
Volume: |
8 |
Issue: |
8 |
Pages: |
545-53 |
|
•
•
•
•
•
|
Publication |
First Author: |
DuHadaway JB |
Year: |
2003 |
Journal: |
Oncogene |
Title: |
Transformation-selective apoptotic program triggered by farnesyltransferase inhibitors requires Bin1. |
Volume: |
22 |
Issue: |
23 |
Pages: |
3578-88 |
|
•
•
•
•
•
|
Publication |
First Author: |
Shi C |
Year: |
2013 |
Journal: |
PLoS One |
Title: |
MicroRNA-21 knockout improve the survival rate in DSS induced fatal colitis through protecting against inflammation and tissue injury. |
Volume: |
8 |
Issue: |
6 |
Pages: |
e66814 |
|
•
•
•
•
•
|
Publication |
First Author: |
Johnston DGW |
Year: |
2017 |
Journal: |
Front Cell Infect Microbiol |
Title: |
MicroRNA-21 Limits Uptake of Listeria monocytogenes by Macrophages to Reduce the Intracellular Niche and Control Infection. |
Volume: |
7 |
|
Pages: |
201 |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
722
 |
Fragment?: |
false |
|
•
•
•
•
•
|