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Search results 301 to 338 out of 338 for Vav2

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Type Details Score
Publication
17855053 | -
First Author: Lazer G
Year: 2007
Journal: Cell Signal
Title: The association of Sam68 with Vav1 contributes to tumorigenesis.
Volume: 19
Issue: 12
Pages: 2479-86
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Protein Domain
IPR035879 | VAV1_SH2
Type: Domain
Description: This entry represents the SH2 domain of VAV1 from vertebrates.VAV1 (also known as proto-oncogene vav) is expressed predominantly in the hematopoietic system and it plays an important role in the development and activation of B and T cells [, , ]. It is activated by tyrosine phosphorylation to function as a guanine nucleotide exchange factor (GEF) for Rho GTPases following cell surface receptor activation, triggering various effects such as cytoskeletal reorganization, transcription regulation, cell cycle progression, and calcium mobilization [, ]. It also serves as a scaffold protein and has been shown to interact with Ku70, Socs1, Janus kinase 2, SIAH2, S100B, Abl gene, ZAP-70, SLP76, and Syk, among others []. The VAV protein family members are multiple domain proteins, including Vav from flies and VAV1/2/3 from mammals. VAV1 predominates in hematopoietic cells, whereas VAV2 and VAV3 are more broadly expressed. They have a calponin homology (CH) domain, an acidic domain (AC), a Dbl homology (DH) domain, a pleckstrin homology (PH) domain, a cysteine-rich (CR) domain containing a zinc finger, and a complex region with SH2 and SH3 domains. Therefore they may participate in the activity of several pathways [, ]. They are signal transducer proteins that couple tyrosine kinase signals with the activation of the Rho/Rac GTPases, [, , ].
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Protein Domain
IPR035729 | VAV1_SH3_2
Type: Domain
Description: VAV1 (also known as proto-oncogene vav) is expressed predominantly in the hematopoietic system and it plays an important role in the development and activation of B and T cells [, , ]. It is activated by tyrosine phosphorylation to function as a guanine nucleotide exchange factor (GEF) for Rho GTPases following cell surface receptor activation, triggering various effects such as cytoskeletal reorganization, transcription regulation, cell cycle progression, and calcium mobilization [, ]. It also serves as a scaffold protein and has been shown to interact with Ku70, Socs1, Janus kinase 2, SIAH2, S100B, Abl gene, ZAP-70, SLP76, and Syk, among others []. The VAV protein family members are multiple domain proteins, including Vav from flies and VAV1/2/3 from mammals. VAV1 predominates in hematopoietic cells, whereas VAV2 and VAV3 are more broadly expressed. They have a calponin homology (CH) domain, an acidic domain (AC), a Dbl homology (DH) domain, a pleckstrin homology (PH) domain, a cysteine-rich (CR) domain containing a zinc finger, and a complex region with SH2 and SH3 domains. Therefore they may participate in the activity of several pathways [, ]. They are signal transducer proteins that couple tyrosine kinase signals with the activation of the Rho/Rac GTPases, [, , ]. This entry represents the second SH3 domain of VAV1. This domain interacts with a wide variety of proteins including cytoskeletal regulators (zyxin), RNA-binding proteins (Sam68), transcriptional regulators, viral proteins, and dynamin 2 [].
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Protein Domain
IPR035730 | VAV1_SH3_1
Type: Domain
Description: VAV1 (also known as proto-oncogene vav) is expressed predominantly in the hematopoietic system and it plays an important role in the development and activation of B and T cells [, , ]. It is activated by tyrosine phosphorylation to function as a guanine nucleotide exchange factor (GEF) for Rho GTPases following cell surface receptor activation, triggering various effects such as cytoskeletal reorganization, transcription regulation, cell cycle progression, and calcium mobilization [, ]. It also serves as a scaffold protein and has been shown to interact with Ku70, Socs1, Janus kinase 2, SIAH2, S100B, Abl gene, ZAP-70, SLP76, and Syk, among others []. The VAV protein family members are multiple domain proteins, including Vav from flies and VAV1/2/3 from mammals. VAV1 predominates in hematopoietic cells, whereas VAV2 and VAV3 are more broadly expressed. They have a calponin homology (CH) domain, an acidic domain (AC), a Dbl homology (DH) domain, a pleckstrin homology (PH) domain, a cysteine-rich (CR) domain containing a zinc finger, and a complex region with SH2 and SH3 domains. Therefore they may participate in the activity of several pathways [, ]. They are signal transducer proteins that couple tyrosine kinase signals with the activation of the Rho/Rac GTPases, [, , ]. This entry represents the first SH3 domain of VAV1.
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Publication
15767666 | J:97576
First Author: Brachmann SM
Year: 2005
Journal: Mol Cell Biol
Title: Role of phosphoinositide 3-kinase regulatory isoforms in development and actin rearrangement.
Volume: 25
Issue: 7
Pages: 2593-606
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Publication
10938113 | J:63932
First Author: Moores SL
Year: 2000
Journal: Mol Cell Biol
Title: Vav family proteins couple to diverse cell surface receptors.
Volume: 20
Issue: 17
Pages: 6364-73
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Publication
23940720 | J:225189
First Author: Xu M
Year: 2013
Journal: PLoS One
Title: Contribution of NADPH oxidase to membrane CD38 internalization and activation in coronary arterial myocytes.
Volume: 8
Issue: 8
Pages: e71212
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Publication
31300985 | J:295491
First Author: Mohammad G
Year: 2019
Journal: Mol Neurobiol
Title: Functional Regulation of an Oxidative Stress Mediator, Rac1, in Diabetic Retinopathy.
Volume: 56
Issue: 12
Pages: 8643-8655
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Publication
12405184 | -
 
First Author: Turner M
Year: 2002
Journal: Adv Exp Med Biol
Title: The role of Vav proteins in B cell responses.
Volume: 512
Pages: 29-34
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Publication
14592821 | -
First Author: Katzav S
Year: 2004
Journal: Blood
Title: Vav1: an oncogene that regulates specific transcriptional activation of T cells.
Volume: 103
Issue: 7
Pages: 2443-51
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Publication
17590270 | -
First Author: Katzav S
Year: 2007
Journal: Cancer Lett
Title: Flesh and blood: the story of Vav1, a gene that signals in hematopoietic cells but can be transforming in human malignancies.
Volume: 255
Issue: 2
Pages: 241-54
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Publication
12670394 | -
 
First Author: Tybulewicz VL
Year: 2003
Journal: Immunol Rev
Title: Vav1: a key signal transducer downstream of the TCR.
Volume: 192
Pages: 42-52
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Publication
12165654 | -
First Author: Michel F
Year: 2002
Journal: Sci STKE
Title: CD28 costimulation: a source of Vav-1 for TCR signaling with the help of SLP-76?
Volume: 2002
Issue: 144
Pages: pe35
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Publication
18511940 | -
First Author: Rapley J
Year: 2008
Journal: EMBO Rep
Title: Crucial structural role for the PH and C1 domains of the Vav1 exchange factor.
Volume: 9
Issue: 7
Pages: 655-61
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Publication
20141838 | -
First Author: Yu B
Year: 2010
Journal: Cell
Title: Structural and energetic mechanisms of cooperative autoinhibition and activation of Vav1.
Volume: 140
Issue: 2
Pages: 246-56
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Publication
26353933 | -
First Author: Katzav S
Year: 2015
Journal: Oncotarget
Title: Vav1: A Dr. Jekyll and Mr. Hyde protein--good for the hematopoietic system, bad for cancer.
Volume: 6
Issue: 30
Pages: 28731-42
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Publication
10669724 | -
First Author: Bustelo XR
Year: 2000
Journal: Mol Cell Biol
Title: Regulatory and signaling properties of the Vav family.
Volume: 20
Issue: 5
Pages: 1461-77
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Protein Domain
IPR037832 | PH_Vav
Type: Domain
Description: Vav acts as a guanosine nucleotide exchange factor (GEF) for Rho/Rac proteins. They control processes including T cell activation, phagocytosis, and migration of cells. The Vav subgroup of Dbl GEFs consists of three family members (Vav1, Vav2, and Vav3) in mammals []. Vav1 is preferentially expressed in the hematopoietic system, while Vav2 and Vav3 are described by broader expression patterns []. Mammalian Vav proteins consist of a calponin homology (CH) domain, an acidic region, a catalytic Dbl homology (DH) domain, a PH domain, a zinc finger cysteine rich domain (C1/CRD), and an SH2 domain, flanked by two SH3 domains. In invertebrates such as Drosophila and C. elegans, Vav is missing the N-terminal SH3 domain. The DH domain is involved in RhoGTPase recognition and selectivity and stimulates the reorganization of the switch regions for GDP/GTP exchange []. The PH domain is implicated in directing membrane localization, allosteric regulation of guanine nucleotide exchange activity, and as a phospholipid-dependent regulator of GEF activity []. Vavs bind RhoGTPases including Rac1, RhoA, and RhoG, while other members of the GEF family are specific for a single RhoGTPase. This promiscuity is thought to be a result of its CRD [].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 [].
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Protein
P27870
Organism: Mus musculus/domesticus
Length: 845  
Fragment?: false
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Protein
Q3UAH3
Organism: Mus musculus/domesticus
Length: 845  
Fragment?: false
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Protein
Q3UAV5
Organism: Mus musculus/domesticus
Length: 821  
Fragment?: false
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Protein
Q3U8U1
Organism: Mus musculus/domesticus
Length: 845  
Fragment?: false
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Protein
Q3U4K7
Organism: Mus musculus/domesticus
Length: 845  
Fragment?: false
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Protein
Q3TXC4
Organism: Mus musculus/domesticus
Length: 845  
Fragment?: false
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Protein
Q3UAG9
Organism: Mus musculus/domesticus
Length: 845  
Fragment?: false
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Protein
E9PXI0
Organism: Mus musculus/domesticus
Length: 821  
Fragment?: false
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Protein
Q3U9E2
Organism: Mus musculus/domesticus
Length: 845  
Fragment?: false
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Protein
Q3U670
Organism: Mus musculus/domesticus
Length: 845  
Fragment?: false
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Protein
Q8VDU4
Organism: Mus musculus/domesticus
Length: 806  
Fragment?: false
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Protein
O08526
Organism: Mus musculus/domesticus
Length: 166  
Fragment?: false
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Protein
Q3V0U7
Organism: Mus musculus/domesticus
Length: 146  
Fragment?: true
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Protein
Q9R0C8
Organism: Mus musculus/domesticus
Length: 847  
Fragment?: false
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Publication
15493994 | -
First Author: Lemmon MA
Year: 2004
Journal: Biochem Soc Trans
Title: Pleckstrin homology domains: not just for phosphoinositides.
Volume: 32
Issue: Pt 5
Pages: 707-11
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Publication
14594214 | -
 
First Author: Cozier GE
Year: 2004
Journal: Curr Top Microbiol Immunol
Title: Membrane targeting by pleckstrin homology domains.
Volume: 282
Pages: 49-88
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Publication
22728242 | -
First Author: Scheffzek K
Year: 2012
Journal: FEBS Lett
Title: Pleckstrin homology (PH) like domains - versatile modules in protein-protein interaction platforms.
Volume: 586
Issue: 17
Pages: 2662-73
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Publication
15489334 | -
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
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Publication
21183079 | J:292518
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
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Publication
19468303 | -
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
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