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Search results 201 to 300 out of 384 for Ralgds

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Type Details Score
Publication
18596699 | J:137819
First Author: Stieglitz B
Year: 2008
Journal: EMBO J
Title: Novel type of Ras effector interaction established between tumour suppressor NORE1A and Ras switch II.
Volume: 27
Issue: 14
Pages: 1995-2005
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Publication
9545376 | J:47809
First Author: Herberg JA
Year: 1998
Journal: J Mol Biol
Title: TAPASIN, DAXX, RGL2, HKE2 and four new genes (BING 1, 3 to 5) form a dense cluster at the centromeric end of the MHC.
Volume: 277
Issue: 4
Pages: 839-57
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Publication
10085114 | J:53936
First Author: Nancy V
Year: 1999
Journal: J Biol Chem
Title: Identification and characterization of potential effector molecules of the Ras-related GTPase Rap2.
Volume: 274
Issue: 13
Pages: 8737-45
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Publication
11839824 | J:74606
First Author: Wolfman JC
Year: 2002
Journal: Mol Cell Biol
Title: Cellular N-Ras promotes cell survival by downregulation of Jun N-terminal protein kinase and p38.
Volume: 22
Issue: 5
Pages: 1589-606
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Publication
12640676 | J:82870
First Author: Schlingemann J
Year: 2003
Journal: Int J Cancer
Title: Profile of gene expression induced by the tumour promotor TPA in murine epithelial cells.
Volume: 104
Issue: 6
Pages: 699-708
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Publication
15062572 | J:87885
First Author: Rivas M
Year: 2003
Journal: Mol Cell Endocrinol
Title: TSH-activated signaling pathways in thyroid tumorigenesis.
Volume: 213
Issue: 1
Pages: 31-45
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Publication
9253406 | -
First Author: Huang L
Year: 1997
Journal: Nat Struct Biol
Title: Three-dimensional structure of the Ras-interacting domain of RalGDS.
Volume: 4
Issue: 8
Pages: 609-15
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Publication
8987396 | -
First Author: Ponting CP
Year: 1996
Journal: Trends Biochem Sci
Title: A novel family of Ras-binding domains.
Volume: 21
Issue: 11
Pages: 422-5
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Publication
11723130 | -
First Author: Kido M
Year: 2002
Journal: J Biol Chem
Title: Critical function of the Ras-associating domain as a primary Ras-binding site for regulation of Saccharomyces cerevisiae adenylyl cyclase.
Volume: 277
Issue: 5
Pages: 3117-23
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Publication
10334925 | -
First Author: Wojcik J
Year: 1999
Journal: Biochem Biophys Res Commun
Title: Sequence analysis identifies a ras-associating (RA)-like domain in the N-termini of band 4.1/JEF domains and in the Grb7/10/14 adapter family.
Volume: 259
Issue: 1
Pages: 113-20
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Publication
9628477 | -
First Author: Huang L
Year: 1998
Journal: Nat Struct Biol
Title: Structural basis for the interaction of Ras with RalGDS.
Volume: 5
Issue: 6
Pages: 422-6
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Protein Domain
IPR000159 | RA_dom
Type: Domain
Description: Ras proteins are signal-transducing GTPases that cycle between inactive GDP-bound and active GTP-bound forms. Ras is a prolific signalling molecule interacting with a spectrum of effector molecules and acting through more than one signalling pathway. A domain of about 100 residues, termed RA for RalGDS/AF-6 or Ras-Associating, interacts with Ras and other small GTPases. It occurs in one or two copies in a variety of signalling molecules. It can be found associated with many other domains, such as PDZ, Dilute (DIL), GEF, myosin motor, IQ, C1, C2, protein kinase, VPS9 or sterile alpha motif (SAM) [, ].Structurally, the RA domain of RalGDS consists of a five-stranded mixed β-sheet interrupted by a 12 residue α-helix and two additional small α-helices. The structure of the RA domain belongs to the ubiquitin α/β roll superfold and is similar to that of the RBD domain and the N-terminal third of the FERM domain [, ]. The RA domain forms a homodimer where the interdimer surface is composed of two cysteines (Cys 2 in each monomer) forming an intermolecular disulfide bond and two interacting intermolecular antiparallel β-sheets []. The major interaction between Ras and RalGDS RA domain occurs between two antiparallel β-strands: β2 of Ras and β2 of RA. This interaction occurs both at the backbone as well as the side chain level [].
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Publication
24489653 | J:212700
First Author: Vandal G
Year: 2014
Journal: PLoS One
Title: Ras effector mutant expression suggest a negative regulator inhibits lung tumor formation.
Volume: 9
Issue: 1
Pages: e84745
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Publication
24069211 | J:206030
First Author: Scotland RL
Year: 2013
Journal: PLoS One
Title: The ral exchange factor rgl2 promotes cardiomyocyte survival and inhibits cardiac fibrosis.
Volume: 8
Issue: 9
Pages: e73599
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Publication
10733581 | J:230394
First Author: Missero C
Year: 2000
Journal: Mol Cell Biol
Title: Multiple ras downstream pathways mediate functional repression of the homeobox gene product TTF-1.
Volume: 20
Issue: 8
Pages: 2783-93
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Protein
D3YUD2
Organism: Mus musculus/domesticus
Length: 229  
Fragment?: true
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Protein
D3YYI1
Organism: Mus musculus/domesticus
Length: 107  
Fragment?: true
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Protein
Q3TLN8
Organism: Mus musculus/domesticus
Length: 162  
Fragment?: true
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Protein
D3Z7L2
Organism: Mus musculus/domesticus
Length: 221  
Fragment?: true
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Protein
B0R019
Organism: Mus musculus/domesticus
Length: 152  
Fragment?: true
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Protein
A0A1L1ST67
Organism: Mus musculus/domesticus
Length: 87  
Fragment?: false
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Protein
A0A087WSF9
Organism: Mus musculus/domesticus
Length: 53  
Fragment?: false
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Publication
17344481 | J:127490
First Author: Takaya A
Year: 2007
Journal: Mol Biol Cell
Title: R-Ras regulates exocytosis by Rgl2/Rlf-mediated activation of RalA on endosomes.
Volume: 18
Issue: 5
Pages: 1850-60
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Protein Domain
IPR038083 | NSP3A-like
Type: Homologous_superfamily
Description: The multi-domain non-structural protein NSP3 is the largest protein encoded by the coronavirus (CoV) genome, with an average molecular mass of about 200 kD. While some of the domains differ between CoV genera, eight domains of NSP3 exist in all known CoVs: the ubiquitin-like domain 1 (Ubl1), the Glu-rich acidic domain (also called "hypervariable region"), a macrodomain (also named "X domain"), the ubiquitin-like domain 2 (Ubl2), the papain-like protease 2 (PL2pro), the NSP3 ectodomain (3Ecto, also called "zinc-finger domain"), as well as the domains Y1 and CoV-Y of unknown functions. There are also two transmembrane regions, TM1 and TM2, which exist in all CoVs [].The ubiquitin-like domain 1 (Ubl1) and the Glu-rich acidic region are located at the N-terminal of NSP3. These two regions together are also named "NSP3A". In addition to the four β-strands and two α-helices that are common to ubiquitin-like folds, the globular domain of NSP3A contains two short helices []. NSP3A is well conserved within different SARS-CoV sequencesbut exhibits low sequence identity (less than 35%) to other CoV NSP3 proteins []. It is an essential component of the replication/transcription complex and is involved in multiple biological processes, such as proteolysis and RNA processing [].This entry represents NSP3A that has been shown to bind ssRNA. The overall structure of the SARS-CoV Ubl1 domain is similar to human ubiquitin (Ub) and that of each of the two ubiquitin-like domains of human or mouse interferon-stimulated gene 15 (hISG15 or mISG15). It is also similar to the Ras-interacting domain (RID) of RalGDS [, ].
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Protein Domain
IPR030749 | RGL2
Type: Family
Description: RGL2 (RalGDS-like 2) belongs to the Ral GDP dissociation stimulator (RalGDS) family []. The C-terminal fragment (Ras/Rap-binding domain) of RGL2 interacts specifically with Ras family proteins that share identical effector domain sequences with Rap1 (H-Ras, R-Ras, Tc21). The binding ability of RGL2 to H-Ras can be regulated through a PKA phosphorylation site identified in this C-terminal domain []. This phoshorylation site is only conserved in the RGL2 murine orthologue, Rlf, but not in RalGDS, RGL and RGL3 []. RGL2 is a guanine nucleotide exchange factor (GEF) for RalA, which plays an important role in the assembly of the exocyst complex. R-Ras regulates exocytosis by RGL2/Rlf-mediated activation of RalA on endosomes [].RalGDS family members can act both as Ras effectors and as guanine nucleotide exchange factors (GEFs) for Ral. They act downstream of Ras and bind to the GTP-bound active form of Ras or Ras family members. They also promote the GDP to GTP exchange for Ral small GTPase, member of the Ras family []. Due to their double action, the RalGDS proteins bridge Ras and Ral [].
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Protein
Q8CJ96
Organism: Mus musculus/domesticus
Length: 419  
Fragment?: false
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Protein
A2A555
Organism: Mus musculus/domesticus
Length: 138  
Fragment?: true
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Protein
E9QA00
Organism: Mus musculus/domesticus
Length: 79  
Fragment?: true
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Protein Domain
IPR019804 | Ras_G-nucl-exch_fac_CS
Type: Conserved_site
Description: Ras proteins are membrane-associated molecular switches that bind GTP and GDP and slowly hydrolyse GTP to GDP []. The balance between the GTP bound (active) and GDP bound (inactive) states is regulated by the opposite action of proteins activating the GTPase activity and that of proteins which promote the loss of bound GDP and the uptake of fresh GTP [, ]. The latter proteins are known as guanine-nucleotide dissociation stimulators (GDSs) (or also as guanine-nucleotide releasing (or exchange) factors (GRFs)). Proteins that act as GDS can be classified into at least two families, on the basis of sequence similarities, the CDC24 family (see ) and the CDC25 family.The size of the proteins of the CDC25 family range from 309 residues (LTE1) to 1596 residues (sos). The sequence similarity shared by all these proteins is limited to a region of about 250 amino acids generally located in their C-terminal section (currently the only exceptions are sos and ralGDS where this domain makes up the central part of the protein). This domain has been shown, in CDC25 an SCD25, to be essential for the activity of these proteins.The crystal structure of the GEF region of human Sos1 complexes with Ras has been solved []. The structure consists of two distinct alpha helical structural domains: the N-terminal domain which seems to have a purely structural role and the C-terminal domain which is sufficient for catalytic activity and contains all residues that interact with Ras. A main feature of the catalytic domain is the protrusion of a helical hairpin important for the nucleotide-exchange mechanism. The N-terminal domain is likely to be important for the stability and correct placement of the hairpin structure. The signature pattern for this entry spans the helical hairpin.
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Protein
Q69ZU7
Organism: Mus musculus/domesticus
Length: 333  
Fragment?: true
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Protein
G3UZ21
Organism: Mus musculus/domesticus
Length: 314  
Fragment?: true
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Protein
Q60695
Organism: Mus musculus/domesticus
Length: 768  
Fragment?: false
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Protein
Q3UYI5
Organism: Mus musculus/domesticus
Length: 709  
Fragment?: false
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Protein
E9Q8N0
Organism: Mus musculus/domesticus
Length: 766  
Fragment?: false
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Protein
E9Q8M9
Organism: Mus musculus/domesticus
Length: 803  
Fragment?: false
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Protein
Q80UQ2
Organism: Mus musculus/domesticus
Length: 353  
Fragment?: false
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Protein
Q9DD19
Organism: Mus musculus/domesticus
Length: 359  
Fragment?: false
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Protein
Q8K342
Organism: Mus musculus/domesticus
Length: 435  
Fragment?: false
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Protein
Q8BL43
Organism: Mus musculus/domesticus
Length: 508  
Fragment?: false
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Protein
Q3U0S6
Organism: Mus musculus/domesticus
Length: 961  
Fragment?: false
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Protein
Q8BMS9
Organism: Mus musculus/domesticus
Length: 326  
Fragment?: false
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Protein
Q99P51
Organism: Mus musculus/domesticus
Length: 232  
Fragment?: false
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Protein
Q8CB96
Organism: Mus musculus/domesticus
Length: 322  
Fragment?: false
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Protein
Q3V0P3
Organism: Mus musculus/domesticus
Length: 650  
Fragment?: false
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Protein
G3X8Z9
Organism: Mus musculus/domesticus
Length: 341  
Fragment?: false
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Protein
Q3TBT4
Organism: Mus musculus/domesticus
Length: 447  
Fragment?: false
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Protein
A0A1B0GS39
Organism: Mus musculus/domesticus
Length: 116  
Fragment?: true
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Protein
D3YXM9
Organism: Mus musculus/domesticus
Length: 243  
Fragment?: true
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Protein
Q3TR60
Organism: Mus musculus/domesticus
Length: 649  
Fragment?: true
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Protein
A0A1D5RM65
Organism: Mus musculus/domesticus
Length: 313  
Fragment?: false
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Protein
D3Z133
Organism: Mus musculus/domesticus
Length: 199  
Fragment?: true
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Protein
Q3UIV8
Organism: Mus musculus/domesticus
Length: 222  
Fragment?: false
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Protein
D3YXD9
Organism: Mus musculus/domesticus
Length: 201  
Fragment?: true
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Protein
Q6PDX1
Organism: Mus musculus/domesticus
Length: 235  
Fragment?: false
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Protein
D3Z7S9
Organism: Mus musculus/domesticus
Length: 169  
Fragment?: true
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Protein
Q3U8Y2
Organism: Mus musculus/domesticus
Length: 463  
Fragment?: false
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Protein
A0A1X7SB70
Organism: Mus musculus/domesticus
Length: 433  
Fragment?: false
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Protein
B9EK92
Organism: Mus musculus/domesticus
Length: 961  
Fragment?: false
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Protein
A0A1B0GRE0
Organism: Mus musculus/domesticus
Length: 383  
Fragment?: false
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Protein
Q3U461
Organism: Mus musculus/domesticus
Length: 447  
Fragment?: false
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Protein
Q3U332
Organism: Mus musculus/domesticus
Length: 900  
Fragment?: false
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Protein
Q8BXG0
Organism: Mus musculus/domesticus
Length: 128  
Fragment?: false
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Protein
Q61193
Organism: Mus musculus/domesticus
Length: 778  
Fragment?: false
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Protein
A0A068BD34
Organism: Mus musculus/domesticus
Length: 778  
Fragment?: false
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Publication
9690470 | -
First Author: Boriack-Sjodin PA
Year: 1998
Journal: Nature
Title: The structural basis of the activation of Ras by Sos.
Volume: 394
Issue: 6691
Pages: 337-43
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Protein
Q6P5E8
Organism: Mus musculus/domesticus
Length: 934  
Fragment?: false
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Protein
Q99MK9
Organism: Mus musculus/domesticus
Length: 340  
Fragment?: false
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Protein
Q5EBH1
Organism: Mus musculus/domesticus
Length: 413  
Fragment?: false
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Protein
Q69Z89
Organism: Mus musculus/domesticus
Length: 1099  
Fragment?: false
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Protein
Q8R5A3
Organism: Mus musculus/domesticus
Length: 670  
Fragment?: false
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Protein
Q6IFT4
Organism: Mus musculus/domesticus
Length: 1182  
Fragment?: false
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Protein
Q8BVL3
Organism: Mus musculus/domesticus
Length: 470  
Fragment?: false
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Protein
P59729
Organism: Mus musculus/domesticus
Length: 980  
Fragment?: false
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Protein
D3YUH8
Organism: Mus musculus/domesticus
Length: 1146  
Fragment?: false
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Protein
Q562E3
Organism: Mus musculus/domesticus
Length: 504  
Fragment?: true
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Protein
F2Z3U3
Organism: Mus musculus/domesticus
Length: 1266  
Fragment?: false
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Protein
D3YWJ9
Organism: Mus musculus/domesticus
Length: 1093  
Fragment?: false
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Protein
F2Z4B7
Organism: Mus musculus/domesticus
Length: 645  
Fragment?: false
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Protein
Q3TM19
Organism: Mus musculus/domesticus
Length: 980  
Fragment?: false
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Protein
B0QZV7
Organism: Mus musculus/domesticus
Length: 344  
Fragment?: false
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Protein
G5E867
Organism: Mus musculus/domesticus
Length: 679  
Fragment?: false
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Protein
Q3U3Y6
Organism: Mus musculus/domesticus
Length: 980  
Fragment?: false
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Protein
Q8R3E5
Organism: Mus musculus/domesticus
Length: 834  
Fragment?: true
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Protein
E9PUB0
Organism: Mus musculus/domesticus
Length: 727  
Fragment?: false
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Protein
B1AYC9
Organism: Mus musculus/domesticus
Length: 670  
Fragment?: false
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Protein
A9YZW8
Organism: Mus musculus/domesticus
Length: 340  
Fragment?: false
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Protein
Q80WA0
Organism: Mus musculus/domesticus
Length: 980  
Fragment?: false
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Protein
Q9QZQ1
Organism: Mus musculus/domesticus
Length: 1820  
Fragment?: false
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Protein
Q9D684
Organism: Mus musculus/domesticus
Length: 903  
Fragment?: false
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Protein
Q921Q7
Organism: Mus musculus/domesticus
Length: 763  
Fragment?: false
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Protein
Q5SUW3
Organism: Mus musculus/domesticus
Length: 550  
Fragment?: false
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Protein
Q5DTR1
Organism: Mus musculus/domesticus
Length: 1046  
Fragment?: true
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Protein
E9Q9C3
Organism: Mus musculus/domesticus
Length: 1827  
Fragment?: false
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Protein
F8WGD2
Organism: Mus musculus/domesticus
Length: 858  
Fragment?: false
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Protein
E9PYX7
Organism: Mus musculus/domesticus
Length: 1663  
Fragment?: false
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Protein
E9Q852
Organism: Mus musculus/domesticus
Length: 1805  
Fragment?: false
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Protein
A0A5F8MPT3
Organism: Mus musculus/domesticus
Length: 1267  
Fragment?: false
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Protein
A0A0G2JF85
Organism: Mus musculus/domesticus
Length: 435  
Fragment?: false
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Protein
A2ASX1
Organism: Mus musculus/domesticus
Length: 221  
Fragment?: true
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Protein
Q3UPQ2
Organism: Mus musculus/domesticus
Length: 1131  
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.

Copyright © 2017 by The Jackson Laboratory. All Rights Reserved

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