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Search results 101 to 139 out of 139 for Arhgef18

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Type Details Score
Publication
29876405 | -
 
First Author: Chen Z
Year: 2018
Journal: Data Brief
Title: Crystal structures of the PH domains from Lbc family of RhoGEFs bound to activated RhoA GTPase.
Volume: 17
Pages: 356-362
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Publication
21064165 | -
First Author: Chen Z
Year: 2011
Journal: Protein Sci
Title: Modulation of a GEF switch: autoinhibition of the intrinsic guanine nucleotide exchange activity of p115-RhoGEF.
Volume: 20
Issue: 1
Pages: 107-17
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Protein Domain
IPR041020 | PH_16
Type: Domain
Description: This pleckstrin homology (PH) domain is found in some Rho guanine nucleotide exchange factors, such as ARHGEF18 (p114RhoGEF) []and ARHGEF1 (p115-RhoGEF) [].
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Publication
28132693 | -
First Author: Arno G
Year: 2017
Journal: Am J Hum Genet
Title: Biallelic Mutation of ARHGEF18, Involved in the Determination of Epithelial Apicobasal Polarity, Causes Adult-Onset Retinal Degeneration.
Volume: 100
Issue: 2
Pages: 334-342
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Protein Domain
IPR037744 | ARHGEF18_PH
Type: Domain
Description: ARHGEF18 is a guanine nucleotide exchange factor that activates RhoA, a small GTPase protein that is a key component of tight junctions and adherens junctions []. It is crucial for maintenance of polarity in the vertebrate retinal epithelium, and consequently is essential for cellular differentiation, morphology and eventually organ function []. ARHGEF18 contains Dbl-homology (DH) and pleckstrin-homology (PH) domains which bind and catalyze the exchange of GDP for GTP on RhoA. This entry represents the PH domain of ARHGEF18.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
Q6P9R4
Organism: Mus musculus/domesticus
Length: 1405  
Fragment?: false
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Protein
A0A5F8MPF6
Organism: Mus musculus/domesticus
Length: 1126  
Fragment?: false
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Protein
A0A5F8MPH6
Organism: Mus musculus/domesticus
Length: 1405  
Fragment?: false
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Protein
Q3TDN6
Organism: Mus musculus/domesticus
Length: 489  
Fragment?: true
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Protein
F6ZN61
Organism: Mus musculus/domesticus
Length: 616  
Fragment?: true
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Protein
P97433
Organism: Mus musculus/domesticus
Length: 1693  
Fragment?: false
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Protein
E9Q394
Organism: Mus musculus/domesticus
Length: 2776  
Fragment?: false
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Protein
Q60875
Organism: Mus musculus/domesticus
Length: 985  
Fragment?: false
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Protein
A0A2X0SFE2
Organism: Mus musculus/domesticus
Length: 987  
Fragment?: true
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Protein
H3BJ40
Organism: Mus musculus/domesticus
Length: 970  
Fragment?: false
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Protein
H3BJX8
Organism: Mus musculus/domesticus
Length: 1183  
Fragment?: false
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Protein
A0A140LJJ5
Organism: Mus musculus/domesticus
Length: 2794  
Fragment?: false
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Protein
A0A286YDI4
Organism: Mus musculus/domesticus
Length: 1324  
Fragment?: false
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Protein
H3BKH9
Organism: Mus musculus/domesticus
Length: 983  
Fragment?: false
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Protein
G5E8P2
Organism: Mus musculus/domesticus
Length: 1700  
Fragment?: false
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Protein
Q3TYZ4
Organism: Mus musculus/domesticus
Length: 637  
Fragment?: true
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Protein
Q5DU33
Organism: Mus musculus/domesticus
Length: 653  
Fragment?: true
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Protein
Q3UZK5
Organism: Mus musculus/domesticus
Length: 607  
Fragment?: true
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Protein
A0A571BEH9
Organism: Mus musculus/domesticus
Length: 1387  
Fragment?: false
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Protein
B2RQQ2
Organism: Mus musculus/domesticus
Length: 1700  
Fragment?: false
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Protein
H3BJU7
Organism: Mus musculus/domesticus
Length: 956  
Fragment?: false
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Protein
A0A140LHG3
Organism: Mus musculus/domesticus
Length: 607  
Fragment?: true
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Protein
H3BJ45
Organism: Mus musculus/domesticus
Length: 968  
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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Protein
Q8R4H2
Organism: Mus musculus/domesticus
Length: 1543  
Fragment?: false
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Protein
Q61210
Organism: Mus musculus/domesticus
Length: 920  
Fragment?: false
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Protein
Q6KAM6
Organism: Mus musculus/domesticus
Length: 939  
Fragment?: true
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Protein
F8VQN6
Organism: Mus musculus/domesticus
Length: 1544  
Fragment?: false
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Protein
E9PUF7
Organism: Mus musculus/domesticus
Length: 976  
Fragment?: false
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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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Protein
Q3U048
Organism: Mus musculus/domesticus
Length: 1476  
Fragment?: true
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Protein
E9Q0A3
Organism: Mus musculus/domesticus
Length: 1475  
Fragment?: true
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Protein
Q68FM7
Organism: Mus musculus/domesticus
Length: 1552  
Fragment?: false
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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.

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