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Search results 101 to 200 out of 270 for Rgs1

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0.034s

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Hits by Pathway

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Hits by Category

Type Details Score
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
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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Publication
9108480 | -
First Author: Tesmer JJ
Year: 1997
Journal: Cell
Title: Structure of RGS4 bound to AlF4--activated G(i alpha1): stabilization of the transition state for GTP hydrolysis.
Volume: 89
Issue: 2
Pages: 251-61
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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
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
Q8K443
Organism: Mus musculus/domesticus
Length: 158  
Fragment?: false
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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
O08899
Organism: Mus musculus/domesticus
Length: 205  
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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Protein
Q3TAS0
Organism: Mus musculus/domesticus
Length: 168  
Fragment?: false
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Protein
A0A0A6YWD0
Organism: Mus musculus/domesticus
Length: 74  
Fragment?: false
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Protein
Q32MD7
Organism: Mus musculus/domesticus
Length: 181  
Fragment?: false
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Protein
F6XWC2
Organism: Mus musculus/domesticus
Length: 682  
Fragment?: true
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Protein
D3YXR2
Organism: Mus musculus/domesticus
Length: 93  
Fragment?: false
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Protein
A0A087WRB0
Organism: Mus musculus/domesticus
Length: 130  
Fragment?: false
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Protein
Q544K2
Organism: Mus musculus/domesticus
Length: 235  
Fragment?: false
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Protein
Q5D078
Organism: Mus musculus/domesticus
Length: 205  
Fragment?: false
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Protein
D3Z289
Organism: Mus musculus/domesticus
Length: 178  
Fragment?: false
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Protein
Q542M0
Organism: Mus musculus/domesticus
Length: 192  
Fragment?: false
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Protein
D3YVJ9
Organism: Mus musculus/domesticus
Length: 101  
Fragment?: true
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Protein
A0A0U1RPP2
Organism: Mus musculus/domesticus
Length: 192  
Fragment?: true
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Protein
A2ABQ9
Organism: Mus musculus/domesticus
Length: 103  
Fragment?: true
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Protein
A0A0U1RPH2
Organism: Mus musculus/domesticus
Length: 102  
Fragment?: true
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Publication
10987813 | -
First Author: Burchett SA
Year: 2000
Journal: J Neurochem
Title: Regulators of G protein signaling: a bestiary of modular protein binding domains.
Volume: 75
Issue: 4
Pages: 1335-51
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Publication
11470431 | -
First Author: Longenecker KL
Year: 2001
Journal: Structure
Title: Structure of the RGS-like domain from PDZ-RhoGEF: linking heterotrimeric g protein-coupled signaling to Rho GTPases.
Volume: 9
Issue: 7
Pages: 559-69
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Publication
11524686 | -
First Author: Chen Z
Year: 2001
Journal: Nat Struct Biol
Title: Structure of the rgRGS domain of p115RhoGEF.
Volume: 8
Issue: 9
Pages: 805-9
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Protein
O54828
Organism: Mus musculus/domesticus
Length: 675  
Fragment?: false
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Protein
Q9Z2H1
Organism: Mus musculus/domesticus
Length: 443  
Fragment?: false
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Protein
Q3ZT31
Organism: Mus musculus/domesticus
Length: 840  
Fragment?: false
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Protein
Q6PHS6
Organism: Mus musculus/domesticus
Length: 957  
Fragment?: false
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Protein
O54829
Organism: Mus musculus/domesticus
Length: 469  
Fragment?: false
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Protein
Q8BHY8
Organism: Mus musculus/domesticus
Length: 964  
Fragment?: false
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Protein
Q80TT7
Organism: Mus musculus/domesticus
Length: 577  
Fragment?: true
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Protein
Q80XD3
Organism: Mus musculus/domesticus
Length: 470  
Fragment?: false
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Protein
Q3U457
Organism: Mus musculus/domesticus
Length: 866  
Fragment?: true
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Protein
E9QNG6
Organism: Mus musculus/domesticus
Length: 958  
Fragment?: false
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Protein
D6RGQ8
Organism: Mus musculus/domesticus
Length: 608  
Fragment?: false
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Protein
G3UX33
Organism: Mus musculus/domesticus
Length: 946  
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