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Search results 1801 to 1900 out of 2041 for Rhoa

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Hits by Pathway

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Hits by Strain

Type Details Score
Protein
Q8C9L7
Organism: Mus musculus/domesticus
Length: 138  
Fragment?: true
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Protein
Q9CTN7
Organism: Mus musculus/domesticus
Length: 127  
Fragment?: true
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Protein
G3UZI7
Organism: Mus musculus/domesticus
Length: 478  
Fragment?: false
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Publication
9846874 | -
First Author: Nassar N
Year: 1998
Journal: Nat Struct Biol
Title: Structures of Cdc42 bound to the active and catalytically compromised forms of Cdc42GAP.
Volume: 5
Issue: 12
Pages: 1047-52
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Publication
12163169 | -
First Author: Fiegen D
Year: 2002
Journal: FEBS Lett
Title: Crystal structure of Rnd3/RhoE: functional implications.
Volume: 525
Issue: 1-3
Pages: 100-4
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Publication
11927263 | -
First Author: Graham DL
Year: 2002
Journal: Chem Biol
Title: MgF(3)(-) as a transition state analog of phosphoryl transfer.
Volume: 9
Issue: 3
Pages: 375-81
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Publication
17683937 | -
First Author: Kevei E
Year: 2007
Journal: Curr Biol
Title: Arabidopsis thaliana circadian clock is regulated by the small GTPase LIP1.
Volume: 17
Issue: 17
Pages: 1456-64
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Publication
11371358 | J:69473
First Author: Le LQ
Year: 2001
Journal: Immunity
Title: Mice lacking the orphan G protein-coupled receptor G2A develop a late-onset autoimmune syndrome.
Volume: 14
Issue: 5
Pages: 561-71
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Publication
16732272 | -
First Author: Gao M
Year: 2006
Journal: Nat Cell Biol
Title: A conserved GTPase-containing complex is required for intracellular sorting of the general amino-acid permease in yeast.
Volume: 8
Issue: 7
Pages: 657-67
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Publication
15989961 | -
First Author: Dubouloz F
Year: 2005
Journal: Mol Cell
Title: The TOR and EGO protein complexes orchestrate microautophagy in yeast.
Volume: 19
Issue: 1
Pages: 15-26
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Publication
16054646 | -
First Author: Reinert DJ
Year: 2005
Journal: J Mol Biol
Title: Structural basis for the function of Clostridium difficile toxin B.
Volume: 351
Issue: 5
Pages: 973-81
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Protein Domain
IPR003578 | Small_GTPase_Rho
Type: Family
Description: Small GTPases form an independent superfamily within the larger class of regulatory GTP hydrolases. This superfamily contains proteins that control a vast number of important processes and possess a common, structurally preserved GTP-binding domain [, ]. Sequence comparisons of small G proteins from various species have revealed that they are conserved in primary structures at the level of 30-55% similarity [].Crystallographic analysis of various small G proteins revealed the presence of a 20kDa catalytic domain that is unique for the whole superfamily [, ]. The domain is built of five alpha helices (A1-A5),six β-strands (B1-B6) and five polypeptide loops (G1-G5). A structural comparison of the GTP- and GDP-bound form, allows one to distinguish two functional loop regions: switch I and switch II that surround the gamma-phosphate group of the nucleotide. The G1 loop (also called the P-loop) that connects the B1 strand and the A1 helix is responsible for the binding of the phosphate groups. The G3 loop provides residues for Mg2 and phosphate binding and is located at the N terminus of the A2 helix. The G1 and G3 loops are sequentially similar to Walker A and Walker B boxes that are found in other nucleotide binding motifs. The G2 loop connects the A1 helix and the B2 strand and contains a conserved Thr residue responsible for Mg2 binding. The guanine base is recognised by the G4 and G5 loops. The consensus sequence NKXD of the G4 loop contains Lys and Asp residues directly interacting with the nucleotide. Part of the G5 loop located between B6 and A5 acts as a recognition site for the guanine base [].The small GTPase superfamily can be divided into at least 8 different families, including:Arf small GTPases. GTP-binding proteins involved in protein trafficking by modulating vesicle budding and uncoating within the Golgi apparatus.Ran small GTPases. GTP-binding proteins involved in nucleocytoplasmic transport. Required for the import of proteins into the nucleus and also for RNA export.Rab small GTPases. GTP-binding proteins involved in vesicular traffic.Rho small GTPases. GTP-binding proteins that control cytoskeleton reorganisation.Ras small GTPases. GTP-binding proteins involved in signalling pathways.Sar1 small GTPases. Small GTPase component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER).Mitochondrial Rho (Miro). Small GTPase domain found in mitochondrial proteins involved in mitochondrial trafficking.Roc small GTPases domain. Small GTPase domain always found associated with the COR domain.This entry represents the Rho subfamily of Ras-like small GTPases. The small GTPase-like protein LIP2 (light insensitive period 2) from Arabidopsis thalianais implicated in control of the plant circadian rhythm []. The crystal structures of a number of the members of this entry have been determined: Rnd3/RhoE [], RhoA []and Cdc42 [].
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Protein Domain
IPR005388 | G2A_lysphc_rcpt
Type: Family
Description: G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups []. The term clan can be used to describe the GPCRs, as they embrace a group of families for which there are indications of evolutionary relationship, but between which there is no statistically significant similarity in sequence []. The currently known clan members include rhodopsin-like GPCRs (Class A, GPCRA), secretin-like GPCRs (Class B, GPCRB), metabotropic glutamate receptor family (Class C, GPCRC), fungal mating pheromone receptors (Class D, GPCRD), cAMP receptors (Class E, GPCRE) and frizzled/smoothened (Class F, GPCRF) [, , , , ]. GPCRs are major drug targets, and are consequently the subject of considerable research interest. It has been reported that the repertoire of GPCRs for endogenous ligands consists of approximately 400 receptors in humans and mice []. Most GPCRs are identified on the basis of their DNA sequences, rather than the ligand they bind, those that are unmatched to known natural ligands are designated by as orphan GPCRs, or unclassified GPCRs [].The rhodopsin-like GPCRs (GPCRA) represent a widespread protein family that includes hormone, neurotransmitter and light receptors, all of which transduce extracellular signals through interaction with guanine nucleotide-binding (G) proteins. Although their activating ligands vary widely in structure and character, the amino acid sequences of the receptors are very similar and are believed to adopt a common structural framework comprising 7 transmembrane (TM) helices [, , ].G2A is expressed mainly in lymphocytes and its expression is up-regulated by stress and prolonged mitogenic signals. Micelacking the receptor have been found to develop a late-onset autoimmunedisease []. It has therefore been suggested that G2A may function as a sensor of LPC levels at sites of inflammation and act as a negativeregulator of lymphocyte growth to limit expansion of tissue-infiltratingcells and overt autoimmune disease. Activation of G2A by LPC results inan increase in intracellular calcium levels (through coupling to Giproteins) and activation of MAP kinases. The receptor has also been shown to couple to G13 proteins, causing RhoA activation and formation of actinstress fibres.
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Protein
Q14B46
Organism: Mus musculus/domesticus
Length: 604  
Fragment?: false
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Protein
B2RY47
Organism: Mus musculus/domesticus
Length: 604  
Fragment?: false
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Protein
Q497Z4
Organism: Mus musculus/domesticus
Length: 686  
Fragment?: false
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Protein
E9QP76
Organism: Mus musculus/domesticus
Length: 602  
Fragment?: false
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Protein
Q3U860
Organism: Mus musculus/domesticus
Length: 171  
Fragment?: true
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Publication
20199662 | J:189950
 
First Author: Sabbir MG
Year: 2010
Journal: BMC Biol
Title: Identification and characterization of Dlc1 isoforms in the mouse and study of the biological function of a single gene trapped isoform.
Volume: 8
Pages: 17
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Publication
29980568 | J:292253
First Author: Issa Bhaloo S
Year: 2018
Journal: Circ Res
Title: Binding of Dickkopf-3 to CXCR7 Enhances Vascular Progenitor Cell Migration and Degradable Graft Regeneration.
Volume: 123
Issue: 4
Pages: 451-466
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Publication
34579569 | J:312951
First Author: Loeven NA
Year: 2021
Journal: mBio
Title: The Burkholderia cenocepacia Type VI Secretion System Effector TecA Is a Virulence Factor in Mouse Models of Lung Infection.
Volume: 12
Issue: 5
Pages: e0209821
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Publication
19929439 | J:183371
First Author: Leung R
Year: 2010
Journal: J Bone Miner Res
Title: Filamin A regulates monocyte migration through Rho small GTPases during osteoclastogenesis.
Volume: 25
Issue: 5
Pages: 1077-91
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Publication
31564129 | J:298044
First Author: Sakaguchi T
Year: 2019
Journal: Circulation
Title: Protein Kinase N Promotes Stress-Induced Cardiac Dysfunction Through Phosphorylation of Myocardin-Related Transcription Factor A and Disruption of Its Interaction With Actin.
Volume: 140
Issue: 21
Pages: 1737-1752
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Publication
29454793 | J:320437
First Author: Dou C
Year: 2018
Journal: Gastroenterology
Title: P300 Acetyltransferase Mediates Stiffness-Induced Activation of Hepatic Stellate Cells Into Tumor-Promoting Myofibroblasts.
Volume: 154
Issue: 8
Pages: 2209-2221.e14
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Publication
37635877 | J:340049
 
First Author: Valdivia A
Year: 2023
Journal: Front Cell Dev Biol
Title: Nox1-based NADPH oxidase regulates the Par protein complex activity to control cell polarization.
Volume: 11
Pages: 1231489
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Publication
29440387 | J:263262
     
First Author: Kawakami Y
Year: 2018
Journal: J Neurosci
Title: The soluble form of LOTUS inhibits Nogo receptor-mediated signaling by interfering with the interaction between Nogo receptor type 1 and p75 neurotrophin receptor.
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Publication
9361006 | J:44051
First Author: Park SK
Year: 1997
Journal: J Biol Chem
Title: Cloning and characterization of phospholipase D from rat brain.
Volume: 272
Issue: 46
Pages: 29263-71
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Publication
9841865 | J:52459
 
First Author: Auer KL
Year: 1998
Journal: Biochem J
Title: Prolonged activation of the mitogen-activated protein kinase pathway promotes DNA synthesis in primary hepatocytes from p21Cip-1/WAF1-null mice, but not in hepatocytes from p16INK4a-null mice.
Volume: 336 ( Pt 3)
Pages: 551-60
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Publication
18255094 | J:133927
First Author: Samarakoon R
Year: 2008
Journal: J Mol Cell Cardiol
Title: TGF-beta1-induced plasminogen activator inhibitor-1 expression in vascular smooth muscle cells requires pp60(c-src)/EGFR(Y845) and Rho/ROCK signaling.
Volume: 44
Issue: 3
Pages: 527-38
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Publication
33307764 | J:325022
First Author: Bibli SI
Year: 2021
Journal: Circulation
Title: Mapping the Endothelial Cell S-Sulfhydrome Highlights the Crucial Role of Integrin Sulfhydration in Vascular Function.
Volume: 143
Issue: 9
Pages: 935-948
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Protein
Q9QYM5
Organism: Mus musculus/domesticus
Length: 227  
Fragment?: false
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Protein
A2A4Q3
Organism: Mus musculus/domesticus
Length: 227  
Fragment?: false
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Protein
E9Q912
Organism: Mus musculus/domesticus
Length: 607  
Fragment?: false
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Protein
Q80U16
Organism: Mus musculus/domesticus
Length: 1078  
Fragment?: false
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Protein
E9PYH9
Organism: Mus musculus/domesticus
Length: 100  
Fragment?: true
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Protein
E9Q922
Organism: Mus musculus/domesticus
Length: 98  
Fragment?: true
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Protein
A6PW28
Organism: Mus musculus/domesticus
Length: 1053  
Fragment?: false
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Protein
Q8BUX6
Organism: Mus musculus/domesticus
Length: 180  
Fragment?: true
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Protein
A2AWP4
Organism: Mus musculus/domesticus
Length: 261  
Fragment?: true
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Protein
Q8BKH0
Organism: Mus musculus/domesticus
Length: 544  
Fragment?: false
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Protein
E9QAZ7
Organism: Mus musculus/domesticus
Length: 97  
Fragment?: true
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Protein
A0A1Y7VJQ5
Organism: Mus musculus/domesticus
Length: 88  
Fragment?: true
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Protein
E9PZ17
Organism: Mus musculus/domesticus
Length: 93  
Fragment?: true
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Protein
Q3TYN8
Organism: Mus musculus/domesticus
Length: 136  
Fragment?: false
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Protein
F7BCP8
Organism: Mus musculus/domesticus
Length: 579  
Fragment?: true
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Protein
E9Q1X7
Organism: Mus musculus/domesticus
Length: 101  
Fragment?: false
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Protein
A0A0G2JGC8
Organism: Mus musculus/domesticus
Length: 544  
Fragment?: false
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Publication
21231971 | -
First Author: Genisyuerek S
Year: 2011
Journal: Mol Microbiol
Title: Structural determinants for membrane insertion, pore formation and translocation of Clostridium difficile toxin B.
Volume: 79
Issue: 6
Pages: 1643-54
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Publication
20498856 | -
First Author: Papatheodorou P
Year: 2010
Journal: PLoS One
Title: Clostridial glucosylating toxins enter cells via clathrin-mediated endocytosis.
Volume: 5
Issue: 5
Pages: e10673
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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
Q5DTT9
Organism: Mus musculus/domesticus
Length: 668  
Fragment?: true
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Protein
H3BKH9
Organism: Mus musculus/domesticus
Length: 983  
Fragment?: false
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Protein
Q3TYZ4
Organism: Mus musculus/domesticus
Length: 637  
Fragment?: true
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Protein
F6XTB7
Organism: Mus musculus/domesticus
Length: 388  
Fragment?: true
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Protein
H3BJU7
Organism: Mus musculus/domesticus
Length: 956  
Fragment?: false
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Protein
Q8BIY6
Organism: Mus musculus/domesticus
Length: 447  
Fragment?: false
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Protein
E9Q7Q7
Organism: Mus musculus/domesticus
Length: 661  
Fragment?: false
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Protein
H3BJ45
Organism: Mus musculus/domesticus
Length: 968  
Fragment?: false
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Protein Coding Gene
MGI:107168 | Aurkb
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
Q003U3
Organism: Mus musculus/domesticus
Length: 1097  
Fragment?: false
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Protein
E9PY12
Organism: Mus musculus/domesticus
Length: 1101  
Fragment?: false
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Protein
E9PXE2
Organism: Mus musculus/domesticus
Length: 1175  
Fragment?: false
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Protein
E9PY13
Organism: Mus musculus/domesticus
Length: 1097  
Fragment?: false
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Protein
F6VR53
Organism: Mus musculus/domesticus
Length: 807  
Fragment?: true
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Protein
Q6PDM6
Organism: Mus musculus/domesticus
Length: 1166  
Fragment?: false
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Protein
B9EJ96
Organism: Mus musculus/domesticus
Length: 722  
Fragment?: false
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Protein
E9PXE1
Organism: Mus musculus/domesticus
Length: 1125  
Fragment?: false
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Protein
E9QAQ3
Organism: Mus musculus/domesticus
Length: 759  
Fragment?: false
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Protein
F6T836
Organism: Mus musculus/domesticus
Length: 722  
Fragment?: false
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Protein
G3UX72
Organism: Mus musculus/domesticus
Length: 1118  
Fragment?: false
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Protein
Q80U26
Organism: Mus musculus/domesticus
Length: 806  
Fragment?: true
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Protein
Q3UHQ9
Organism: Mus musculus/domesticus
Length: 1118  
Fragment?: false
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Protein
E9QPM7
Organism: Mus musculus/domesticus
Length: 1149  
Fragment?: false
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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
G3UXP9
Organism: Mus musculus/domesticus
Length: 1059  
Fragment?: false
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Protein
D3YUF4
Organism: Mus musculus/domesticus
Length: 1046  
Fragment?: false
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Protein
E9Q863
Organism: Mus musculus/domesticus
Length: 1067  
Fragment?: false
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Protein
D3YUF3
Organism: Mus musculus/domesticus
Length: 866  
Fragment?: true
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Publication
10934474 | J:69174
First Author: Joberty G
Year: 2000
Journal: Nat Cell Biol
Title: The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42.
Volume: 2
Issue: 8
Pages: 531-9
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Protein
Q9Z282
Organism: Mus musculus/domesticus
Length: 382  
Fragment?: false
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Protein
Q9DBG9
Organism: Mus musculus/domesticus
Length: 124  
Fragment?: false
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Protein
F6UKC6
Organism: Mus musculus/domesticus
Length: 188  
Fragment?: true
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Protein
Q61053
Organism: Mus musculus/domesticus
Length: 237  
Fragment?: true
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Protein
F7BQE4
Organism: Mus musculus/domesticus
Length: 988  
Fragment?: true
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Protein
A0A1L1SS34
Organism: Mus musculus/domesticus
Length: 239  
Fragment?: true
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Protein
Q6A003
Organism: Mus musculus/domesticus
Length: 499  
Fragment?: true
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Protein
F6UIH6
Organism: Mus musculus/domesticus
Length: 96  
Fragment?: true
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Protein
Q3UGZ6
Organism: Mus musculus/domesticus
Length: 1345  
Fragment?: false
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Protein
Q8C9Y7
Organism: Mus musculus/domesticus
Length: 692  
Fragment?: false
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Protein
F6S3V7
Organism: Mus musculus/domesticus
Length: 611  
Fragment?: true
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Protein
A2AWP6
Organism: Mus musculus/domesticus
Length: 1040  
Fragment?: false
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Publication
20381137 | J:320089
First Author: Sancak Y
Year: 2010
Journal: Cell
Title: Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids.
Volume: 141
Issue: 2
Pages: 290-303
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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
D6RH37
Organism: Mus musculus/domesticus
Length: 796  
Fragment?: false
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Protein
G3UXH4
Organism: Mus musculus/domesticus
Length: 935  
Fragment?: false
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Protein
F8VQN6
Organism: Mus musculus/domesticus
Length: 1544  
Fragment?: false
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Protein
Q3UQS3
Organism: Mus musculus/domesticus
Length: 756  
Fragment?: false
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Protein
P60766
Organism: Mus musculus/domesticus
Length: 191  
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.

Copyright © 2017 by The Jackson Laboratory. All Rights Reserved

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