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Search results 701 to 800 out of 897 for Rgs4

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Type Details Score
Publication
21035448 | J:166146
First Author: Wang J
Year: 2010
Journal: FEBS Lett
Title: DHHC protein-dependent palmitoylation protects regulator of G-protein signaling 4 from proteasome degradation.
Volume: 584
Issue: 22
Pages: 4570-4
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Publication
10373502 | J:228419
First Author: Druey KM
Year: 1999
Journal: J Biol Chem
Title: Amino-terminal cysteine residues of RGS16 are required for palmitoylation and modulation of Gi- and Gq-mediated signaling.
Volume: 274
Issue: 26
Pages: 18836-42
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Publication
34127743 | J:312129
First Author: Liu Y
Year: 2021
Journal: Sci Rep
Title: Impaired regulation of heart rate and sinoatrial node function by the parasympathetic nervous system in type 2 diabetic mice.
Volume: 11
Issue: 1
Pages: 12465
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Publication
16930410 | J:112924
First Author: Stanwood GD
Year: 2006
Journal: Eur J Neurosci
Title: Genetic or pharmacological inactivation of the dopamine D1 receptor differentially alters the expression of regulator of G-protein signalling (Rgs) transcripts.
Volume: 24
Issue: 3
Pages: 806-18
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Publication
18337495 | J:133474
First Author: Takata Y
Year: 2008
Journal: Proc Natl Acad Sci U S A
Title: PPARdelta-mediated antiinflammatory mechanisms inhibit angiotensin II-accelerated atherosclerosis.
Volume: 105
Issue: 11
Pages: 4277-82
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Publication
27601729 | J:258164
First Author: Yilmaz A
Year: 2016
Journal: Sci Signal
Title: MuSK is a BMP co-receptor that shapes BMP responses and calcium signaling in muscle cells.
Volume: 9
Issue: 444
Pages: ra87
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Publication
12738888 | J:83620
First Author: Chen CK
Year: 2003
Journal: Proc Natl Acad Sci U S A
Title: Instability of GGL domain-containing RGS proteins in mice lacking the G protein beta-subunit Gbeta5.
Volume: 100
Issue: 11
Pages: 6604-9
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Publication
38971310 | J:353398
First Author: Pu Y
Year: 2024
Journal: J Biol Chem
Title: MGST3 regulates BACE1 protein translation and amyloidogenesis by controlling the RGS4-mediated AKT signaling pathway.
Volume: 300
Issue: 8
Pages: 107530
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Publication
12860966 | J:95213
First Author: Shin DM
Year: 2003
Journal: J Cell Biol
Title: Homer 2 tunes G protein-coupled receptors stimulus intensity by regulating RGS proteins and PLCbeta GAP activities.
Volume: 162
Issue: 2
Pages: 293-303
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Publication
22028430 | J:177710
First Author: Kõks S
Year: 2011
Journal: Physiol Genomics
Title: Hypothalamic gene expression profile indicates a reduction in G protein signaling in the Wfs1 mutant mice.
Volume: 43
Issue: 24
Pages: 1351-8
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Publication
12642593 | J:83579
First Author: Hiol A
Year: 2003
Journal: J Biol Chem
Title: Palmitoylation regulates regulators of G-protein signaling (RGS) 16 function. I. Mutation of amino-terminal cysteine residues on RGS16 prevents its targeting to lipid rafts and palmitoylation of an internal cysteine residue.
Volume: 278
Issue: 21
Pages: 19301-8
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Publication
18936096 | J:144554
First Author: Shankaranarayanan A
Year: 2008
Journal: J Biol Chem
Title: Assembly of high order G alpha q-effector complexes with RGS proteins.
Volume: 283
Issue: 50
Pages: 34923-34
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Publication
33359660 | J:305357
 
First Author: Yoon SY
Year: 2021
Journal: Neuroscience
Title: Analgesic Efficacy of α2 Adrenergic Receptor Agonists Depends on the Chronic State of Neuropathic Pain: Role of Regulator of G Protein Signaling 4.
Volume: 455
Pages: 177-194
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Publication
23262291 | J:318019
First Author: Bhushan R
Year: 2013
Journal: Int J Biochem Cell Biol
Title: miR-181a promotes osteoblastic differentiation through repression of TGF-β signaling molecules.
Volume: 45
Issue: 3
Pages: 696-705
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Publication
16219326 | J:102866
First Author: Xie GX
Year: 2005
Journal: J Mol Biol
Title: N-terminally truncated variant of the mouse GAIP/RGS19 lacks selectivity of full-length GAIP/RGS19 protein in regulating ORL1 receptor signaling.
Volume: 353
Issue: 5
Pages: 1081-92
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Publication
14742685 | J:156234
First Author: Waldo GL
Year: 2004
Journal: Mol Pharmacol
Title: Agonist binding and Gq-stimulating activities of the purified human P2Y1 receptor.
Volume: 65
Issue: 2
Pages: 426-36
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Protein
G3UX14
Organism: Mus musculus/domesticus
Length: 262  
Fragment?: true
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Protein
A0A0G2JEW1
Organism: Mus musculus/domesticus
Length: 92  
Fragment?: false
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Protein
F6Y9P3
Organism: Mus musculus/domesticus
Length: 110  
Fragment?: true
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Publication
10811618 | -
First Author: Spink KE
Year: 2000
Journal: EMBO J
Title: Structural basis of the Axin-adenomatous polyposis coli interaction.
Volume: 19
Issue: 10
Pages: 2270-9
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Publication
10452897 | -
First Author: de Alba E
Year: 1999
Journal: J Mol Biol
Title: Solution structure of human GAIP (Galpha interacting protein): a regulator of G protein signaling.
Volume: 291
Issue: 4
Pages: 927-39
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Publication
11234020 | -
First Author: Slep KC
Year: 2001
Journal: Nature
Title: Structural determinants for regulation of phosphodiesterase by a G protein at 2.0 A.
Volume: 409
Issue: 6823
Pages: 1071-7
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Publication
12764189 | -
First Author: Lodowski DT
Year: 2003
Journal: Science
Title: Keeping G proteins at bay: a complex between G protein-coupled receptor kinase 2 and Gbetagamma.
Volume: 300
Issue: 5623
Pages: 1256-62
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Publication
10836135 | -
 
First Author: De Vries L
Year: 2000
Journal: Annu Rev Pharmacol Toxicol
Title: The regulator of G protein signaling family.
Volume: 40
Pages: 235-71
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Publication
15090201 | -
First Author: Chasse SA
Year: 2003
Journal: Assay Drug Dev Technol
Title: RGS proteins: G protein-coupled receptors meet their match.
Volume: 1
Issue: 2
Pages: 357-64
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Publication
18434541 | -
First Author: Soundararajan M
Year: 2008
Journal: Proc Natl Acad Sci U S A
Title: Structural diversity in the RGS domain and its interaction with heterotrimeric G protein alpha-subunits.
Volume: 105
Issue: 17
Pages: 6457-62
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Publication
23900842 | -
First Author: Croft W
Year: 2013
Journal: J Biol Chem
Title: A physiologically required G protein-coupled receptor (GPCR)-regulator of G protein signaling (RGS) interaction that compartmentalizes RGS activity.
Volume: 288
Issue: 38
Pages: 27327-42
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Protein
P97428
Organism: Mus musculus/domesticus
Length: 201  
Fragment?: false
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Protein
Q9CX84
Organism: Mus musculus/domesticus
Length: 216  
Fragment?: false
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Protein
Q8BFU4
Organism: Mus musculus/domesticus
Length: 194  
Fragment?: false
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Protein
A0A5S9EHU9
Organism: Mus musculus/domesticus
Length: 131  
Fragment?: false
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Protein
D3YXA5
Organism: Mus musculus/domesticus
Length: 116  
Fragment?: true
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Protein
D3Z5I4
Organism: Mus musculus/domesticus
Length: 98  
Fragment?: true
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Protein
A0A087WS51
Organism: Mus musculus/domesticus
Length: 129  
Fragment?: true
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Protein
Q9CTC4
Organism: Mus musculus/domesticus
Length: 79  
Fragment?: true
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Protein
D3Z1B6
Organism: Mus musculus/domesticus
Length: 85  
Fragment?: true
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Protein
A0A0J9YTS6
Organism: Mus musculus/domesticus
Length: 221  
Fragment?: true
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Protein
B7ZCT1
Organism: Mus musculus/domesticus
Length: 243  
Fragment?: false
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Protein
Q7TNU9
Organism: Mus musculus/domesticus
Length: 201  
Fragment?: false
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Protein
D3Z1V2
Organism: Mus musculus/domesticus
Length: 137  
Fragment?: true
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Protein
Q8CGT5
Organism: Mus musculus/domesticus
Length: 194  
Fragment?: false
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Protein
V9GXL8
Organism: Mus musculus/domesticus
Length: 393  
Fragment?: false
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Protein
A0A0U1RPU5
Organism: Mus musculus/domesticus
Length: 93  
Fragment?: false
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Protein
D3Z4Z8
Organism: Mus musculus/domesticus
Length: 200  
Fragment?: true
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Protein
D3YYE5
Organism: Mus musculus/domesticus
Length: 115  
Fragment?: true
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Protein
D3YX00
Organism: Mus musculus/domesticus
Length: 115  
Fragment?: true
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Protein
F8WH97
Organism: Mus musculus/domesticus
Length: 163  
Fragment?: true
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Protein
B7ZCT0
Organism: Mus musculus/domesticus
Length: 160  
Fragment?: false
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Protein
A0A5S9EHU3
Organism: Mus musculus/domesticus
Length: 147  
Fragment?: false
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Protein
Q78NN4
Organism: Mus musculus/domesticus
Length: 216  
Fragment?: false
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Protein
Q542U0
Organism: Mus musculus/domesticus
Length: 201  
Fragment?: false
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Protein
V9GXQ3
Organism: Mus musculus/domesticus
Length: 152  
Fragment?: false
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Protein Domain
IPR016137 | RGS
Type: Domain
Description: This entry represents a structural domain with a multi-helical fold consisting of a 4-helical bundle with a left-handed twist and an up-and-down topology. This domain can be divided into two all-alpha subdomains. This domain is found in regulation of G-protein signalling (RGS) proteins, as well as other related proteins, including:RGS4 [].RGS9 [].G-alpha interacting protein GaIP [].Axin [].p115RhoGEF [].Pdz-RhoGEF [].G-protein coupled receptor kinase 2 N-terminal domain [].RGS (Regulator of G Protein Signalling) proteins are multi-functional, GTPase-accelerating proteins that promote GTP hydrolysis by the alpha subunit of heterotrimeric G proteins, thereby inactivating the G protein and rapidly switching off G protein-coupled receptor signalling pathways. Upon activation by GPCRs, heterotrimeric G proteins exchange GDP for GTP, are released from the receptor, and dissociate into free, active GTP-bound alpha subunit and beta-gamma dimer, both of which activate downstream effectors. The response is terminated upon GTP hydrolysis by the alpha subunit (), which can then bind the beta-gamma dimer (, ) and the receptor. RGS proteins markedly reduce the lifespan of GTP-bound alpha subunits by stabilising the G protein transition state.All RGS proteins contain an 'RGS-box' (or RGS domain), which is required for activity. Some small RGS proteins such as RGS1 and RGS4 are comprised of little more than an RGS domain, while others also contain additional domains that confer further functionality. RGS domains can be found in conjunction with a variety of domains, including: DEP for membrane targeting (), PDZ for binding to GPCRs (), PTB for phosphotyrosine-binding (), RBD for Ras-binding (), GoLoco for guanine nucleotide inhibitor activity (), PX for phosphatidylinositol-binding (), PXA that is associated with PX (), PH for stimulating guanine nucleotide exchange (), and GGL (G protein gamma subunit-like) for binding G protein beta subunits (). Those RGS proteins that contain GGL domains can interact with G protein beta subunits to form novel dimers that prevent G protein gamma subunit binding and G protein alpha subunit association, thereby preventing heterotrimer formation.
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Protein Domain
IPR024066 | RGS_subdom1/3
Type: Homologous_superfamily
Description: RGS (Regulator of G Protein Signalling) proteins are multi-functional, GTPase-accelerating proteins that promote GTP hydrolysis by the alpha subunit of heterotrimeric G proteins []. Upon activation by GPCRs, heterotrimeric G proteins exchange GDP for GTP, are released from the receptor, and dissociate into free, active GTP-bound alpha subunit and beta-gamma dimer, both of which activate downstream effectors. Usually, the response is terminated upon GTP hydrolysis by the alpha subunit (), which can then bind the beta-gamma dimer (, ) and the receptor. However, in some cases, RGS proteins can have a positive effect on signal potentiation []. All RGS proteins contain an 'RGS-box' (or RGS domain), which is required for activity. Some small RGS proteins such as RGS1 and RGS4 are comprised of little more than an RGS domain, while others also contain additional domains that confer further functionality [, ]. RGS domains can be found in conjunction with a variety of domains, including: DEP for membrane targeting (), PDZ for binding to GPCRs (), PTB for phosphotyrosine-binding (), RBD for Ras-binding (), GoLoco for guanine nucleotide inhibitor activity (), PX for phosphatidylinositol-binding (), PXA that is associatedwith PX (), PH for stimulating guanine nucleotide exchange (), and GGL (G protein gamma subunit-like) for binding G protein beta subunits () []. Those RGS proteins that contain GGL domains can interact with G protein beta subunits to form novel dimers that prevent G protein gamma subunit binding and G protein alpha subunit association, thereby preventing heterotrimer formation.The RSG box in RSG4 corresponds to an array of α-helices that fold into two domains. Both are required for GAP (GTPase activating protein) activity []. This superfamily represents the subdomains 1 and 3 of the RSG box.
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Protein Domain
IPR036305 | RGS_sf
Type: Homologous_superfamily
Description: This entry represents a structural domain superfamily with a multi-helical fold consisting of a 4-helical bundle with a left-handed twist and an up-and-down topology. This domain can be divided into two all-alpha subdomains. This domain is found in regulation of G-protein signalling (RGS) proteins, as well as other related proteins, including:RGS4 [].RGS9 [].G-alpha interacting protein GaIP [].Axin [].p115RhoGEF [].Pdz-RhoGEF [].G-protein coupled receptor kinase 2 N-terminal domain [].RGS (Regulator of G Protein Signalling) proteins are multi-functional, GTPase-accelerating proteins that promote GTP hydrolysis by the alpha subunit of heterotrimeric G proteins, thereby inactivating the G protein and rapidly switching off G protein-coupled receptor signalling pathways. Upon activation by GPCRs, heterotrimeric G proteins exchange GDP for GTP, are released from the receptor, and dissociate into free, active GTP-bound alpha subunit and beta-gamma dimer, both of which activate downstream effectors. The response is terminated upon GTP hydrolysis by the alpha subunit (), which can then bind the beta-gamma dimer (, ) and the receptor. RGS proteins markedly reduce the lifespan of GTP-bound alpha subunits by stabilising the G protein transition state.All RGS proteins contain an 'RGS-box' (or RGS domain), which is required for activity. Some small RGS proteins such as RGS1 and RGS4 are comprised of little more than an RGS domain, while others also contain additional domains that confer further functionality. RGS domains can be found in conjunction with a variety of domains, including: DEP for membrane targeting (), PDZ for binding to GPCRs (), PTB for phosphotyrosine-binding (), RBD for Ras-binding (), GoLoco for guanine nucleotide inhibitor activity (), PX for phosphatidylinositol-binding (), PXA that is associated with PX (), PH for stimulating guanine nucleotide exchange (), and GGL (G protein gamma subunit-like) for binding G protein beta subunits (). Those RGS proteins that contain GGL domains can interact with G protein beta subunits to form novel dimers that prevent G protein gamma subunit binding and G protein alpha subunit association, thereby preventing heterotrimer formation.
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Protein Domain
IPR044926 | RGS_subdomain_2
Type: Homologous_superfamily
Description: RGS (Regulator of G Protein Signalling) proteins are multi-functional, GTPase-accelerating proteins that promote GTP hydrolysis by the alpha subunit of heterotrimeric G proteins []. Upon activation by GPCRs, heterotrimeric G proteins exchange GDP for GTP, are released from the receptor, and dissociate into free, active GTP-bound alpha subunit and beta-gamma dimer, both of which activate downstream effectors. Usually, the response is terminated upon GTP hydrolysis by the alpha subunit (), which can then bind the beta-gamma dimer (, ) and the receptor. However, in some cases, RGS proteins can have a positive effect on signal potentiation []. All RGS proteins contain an 'RGS-box' (or RGS domain), which is required for activity. Some small RGS proteins such as RGS1 and RGS4 are comprised of little more than an RGS domain, while others also contain additional domains that confer further functionality [, ]. RGS domains can be found in conjunction with a variety of domains, including: DEP for membrane targeting (), PDZ for binding to GPCRs (), PTB for phosphotyrosine-binding (), RBD for Ras-binding (), GoLoco for guanine nucleotide inhibitor activity (), PX for phosphatidylinositol-binding (), PXA that is associated with PX (), PH for stimulating guanine nucleotide exchange (), and GGL (G protein gamma subunit-like) for binding G protein beta subunits () []. Those RGS proteins that contain GGL domains can interact with G protein beta subunits to form novel dimers that prevent G protein gamma subunit binding and G protein alpha subunit association, thereby preventing heterotrimer formation.The RSG box in RSG4 corresponds to an array of α-helices that fold into two domains. Both are required for GAP (GTPase activating protein) activity []. This superfamily represents the subdomain 2 of the RSG box.
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Protein
Q9QZB0
Organism: Mus musculus/domesticus
Length: 210  
Fragment?: false
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Protein
Q9JL25
Organism: Mus musculus/domesticus
Length: 209  
Fragment?: false
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Protein
Q9QZB1
Organism: Mus musculus/domesticus
Length: 239  
Fragment?: false
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Protein
G3UYX5
Organism: Mus musculus/domesticus
Length: 1258  
Fragment?: false
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Protein
Q45FE2
Organism: Mus musculus/domesticus
Length: 191  
Fragment?: true
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Protein
F6WK59
Organism: Mus musculus/domesticus
Length: 51  
Fragment?: true
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Protein
Q45FE4
Organism: Mus musculus/domesticus
Length: 153  
Fragment?: true
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Protein
A0A494B9K8
Organism: Mus musculus/domesticus
Length: 125  
Fragment?: false
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Protein
Q3TCG6
Organism: Mus musculus/domesticus
Length: 473  
Fragment?: true
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Protein
Q8BRK0
Organism: Mus musculus/domesticus
Length: 57  
Fragment?: true
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Protein
V9GXV7
Organism: Mus musculus/domesticus
Length: 970  
Fragment?: false
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Protein
Q45FE3
Organism: Mus musculus/domesticus
Length: 71  
Fragment?: true
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Protein
E9Q720
Organism: Mus musculus/domesticus
Length: 372  
Fragment?: false
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Protein
Q8BR34
Organism: Mus musculus/domesticus
Length: 230  
Fragment?: false
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Protein
F7BEP0
Organism: Mus musculus/domesticus
Length: 96  
Fragment?: true
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Protein
H3BL40
Organism: Mus musculus/domesticus
Length: 1073  
Fragment?: false
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Protein
A0A0A6YVV6
Organism: Mus musculus/domesticus
Length: 71  
Fragment?: true
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Protein
Q3TR91
Organism: Mus musculus/domesticus
Length: 343  
Fragment?: false
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Protein
Q45FE5
Organism: Mus musculus/domesticus
Length: 160  
Fragment?: true
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Protein
G5E8E0
Organism: Mus musculus/domesticus
Length: 230  
Fragment?: false
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Protein
Q8CDT4
Organism: Mus musculus/domesticus
Length: 451  
Fragment?: true
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Protein
A0A5F8MPV0
Organism: Mus musculus/domesticus
Length: 1108  
Fragment?: false
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Protein
G3UXI4
Organism: Mus musculus/domesticus
Length: 219  
Fragment?: true
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Protein
Q9D203
Organism: Mus musculus/domesticus
Length: 218  
Fragment?: false
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Protein
Q8BHZ1
Organism: Mus musculus/domesticus
Length: 495  
Fragment?: true
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Protein
Q8C5F3
Organism: Mus musculus/domesticus
Length: 210  
Fragment?: false
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Protein
G3UX13
Organism: Mus musculus/domesticus
Length: 665  
Fragment?: false
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Protein
Q6P208
Organism: Mus musculus/domesticus
Length: 210  
Fragment?: false
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Protein
Q8BP13
Organism: Mus musculus/domesticus
Length: 177  
Fragment?: false
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Protein
Q8C5J7
Organism: Mus musculus/domesticus
Length: 208  
Fragment?: false
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Protein
Q8BX71
Organism: Mus musculus/domesticus
Length: 217  
Fragment?: false
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Protein
Q45FE1
Organism: Mus musculus/domesticus
Length: 178  
Fragment?: true
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Protein
O88845
Organism: Mus musculus/domesticus
Length: 662  
Fragment?: false
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Protein
A1L351
Organism: Mus musculus/domesticus
Length: 466  
Fragment?: false
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Protein
A2A6V6
Organism: Mus musculus/domesticus
Length: 449  
Fragment?: false
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Protein
Q9CQE5
Organism: Mus musculus/domesticus
Length: 181  
Fragment?: false
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Protein
O08849
Organism: Mus musculus/domesticus
Length: 211  
Fragment?: false
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Protein
Q8BXT1
Organism: Mus musculus/domesticus
Length: 180  
Fragment?: false
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Protein
O08850
Organism: Mus musculus/domesticus
Length: 181  
Fragment?: false
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Protein
Q99PG4
Organism: Mus musculus/domesticus
Length: 235  
Fragment?: false
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Protein
Q8K443
Organism: Mus musculus/domesticus
Length: 158  
Fragment?: false
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Protein
Q3TTW9
Organism: Mus musculus/domesticus
Length: 499  
Fragment?: false
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Protein
A0A1B0GT31
Organism: Mus musculus/domesticus
Length: 149  
Fragment?: true
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Protein
F6X4A2
Organism: Mus musculus/domesticus
Length: 126  
Fragment?: true
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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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Cambridge CB2 3EH, United Kingdom