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Search results 3401 to 3500 out of 4514 for Cdc42

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Hits by Strain

Type Details Score
Protein
Q3UFT3
Organism: Mus musculus/domesticus
Length: 876  
Fragment?: false
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Protein
B2XXT9
Organism: Mus musculus/domesticus
Length: 29  
Fragment?: true
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Protein
E9QAJ7
Organism: Mus musculus/domesticus
Length: 158  
Fragment?: true
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Protein
A0A0G2JEU6
Organism: Mus musculus/domesticus
Length: 236  
Fragment?: true
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Protein
A0A1W2P7L9
Organism: Mus musculus/domesticus
Length: 143  
Fragment?: true
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Protein
A0A494B9M9
Organism: Mus musculus/domesticus
Length: 132  
Fragment?: true
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Protein
Q6TDG7
Organism: Mus musculus/domesticus
Length: 80  
Fragment?: true
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Protein
E9PVB8
Organism: Mus musculus/domesticus
Length: 391  
Fragment?: false
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Protein
E0CZ69
Organism: Mus musculus/domesticus
Length: 392  
Fragment?: true
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Protein
E0CXB4
Organism: Mus musculus/domesticus
Length: 175  
Fragment?: false
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Protein
Q8CC79
Organism: Mus musculus/domesticus
Length: 217  
Fragment?: true
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Protein
A0A1W2P6I7
Organism: Mus musculus/domesticus
Length: 182  
Fragment?: true
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Protein
Q3V381
Organism: Mus musculus/domesticus
Length: 316  
Fragment?: false
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Protein
S4R1A7
Organism: Mus musculus/domesticus
Length: 54  
Fragment?: true
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Protein
Q9CSJ1
Organism: Mus musculus/domesticus
Length: 129  
Fragment?: true
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Protein
Q8C9L7
Organism: Mus musculus/domesticus
Length: 138  
Fragment?: true
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Protein
Q8BXT3
Organism: Mus musculus/domesticus
Length: 511  
Fragment?: false
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Protein
Q9CTN7
Organism: Mus musculus/domesticus
Length: 127  
Fragment?: true
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Protein
A0A571BF98
Organism: Mus musculus/domesticus
Length: 690  
Fragment?: false
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Protein
F6RQI2
Organism: Mus musculus/domesticus
Length: 58  
Fragment?: true
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Protein
A0A3B2WCY8
Organism: Mus musculus/domesticus
Length: 282  
Fragment?: true
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Protein
Q8BII0
Organism: Mus musculus/domesticus
Length: 223  
Fragment?: false
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Protein
D3Z292
Organism: Mus musculus/domesticus
Length: 66  
Fragment?: true
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Protein
A0A571BEM4
Organism: Mus musculus/domesticus
Length: 311  
Fragment?: false
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Protein
F6QWW7
Organism: Mus musculus/domesticus
Length: 196  
Fragment?: true
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Protein
D3YY99
Organism: Mus musculus/domesticus
Length: 205  
Fragment?: true
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Protein
A0A494BAB2
Organism: Mus musculus/domesticus
Length: 135  
Fragment?: true
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Protein
B2XXT3
Organism: Mus musculus/domesticus
Length: 29  
Fragment?: true
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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
10512884 | -
First Author: Madania A
Year: 1999
Journal: Mol Biol Cell
Title: The Saccharomyces cerevisiae homologue of human Wiskott-Aldrich syndrome protein Las17p interacts with the Arp2/3 complex.
Volume: 10
Issue: 10
Pages: 3521-38
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Publication
17460121 | -
First Author: Gao XD
Year: 2007
Journal: Mol Biol Cell
Title: Sequential and distinct roles of the cadherin domain-containing protein Axl2p in cell polarization in yeast cell cycle.
Volume: 18
Issue: 7
Pages: 2542-60
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Publication
12858164 | -
First Author: Aviv T
Year: 2003
Journal: Nat Struct Biol
Title: The RNA-binding SAM domain of Smaug defines a new family of post-transcriptional regulators.
Volume: 10
Issue: 8
Pages: 614-21
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Publication
18650809 | -
First Author: Cheng HC
Year: 2008
Journal: Nature
Title: Structural mechanism of WASP activation by the enterohaemorrhagic E. coli effector EspF(U).
Volume: 454
Issue: 7207
Pages: 1009-13
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Publication
22847007 | -
First Author: Gaucher JF
Year: 2012
Journal: J Biol Chem
Title: Interactions of isolated C-terminal fragments of neural Wiskott-Aldrich syndrome protein (N-WASP) with actin and Arp2/3 complex.
Volume: 287
Issue: 41
Pages: 34646-59
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Publication
17512409 | -
First Author: Shimada A
Year: 2007
Journal: Cell
Title: Curved EFC/F-BAR-domain dimers are joined end to end into a filament for membrane invagination in endocytosis.
Volume: 129
Issue: 4
Pages: 761-72
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Publication
15043839 | -
First Author: Zimmerberg J
Year: 2004
Journal: Curr Biol
Title: Membrane curvature: how BAR domains bend bilayers.
Volume: 14
Issue: 6
Pages: R250-2
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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
IPR000219 | DH-domain
Type: Domain
Description: The Rho family GTPases Rho, Rac and CDC42 regulate a diverse array of cellular processes. Like all members of the Ras superfamily, the Rho proteins cycle between active GTP-bound and inactive GDP-bound conformational states.Activation of Rho proteins through release of bound GDP and subsequentbinding of GTP, is catalysed by guanine nucleotide exchange factors (GEFs) inthe Dbl family. The proteins encoded by members of the Dbl family share acommon domain, presented in this entry, of about 200 residues (designated the Dbl homology or DH domain) that has been shown to encode a GEF activity specific for a number of Rho family members. In addition, all family members possess a second, shared domain designated the pleckstrin homology (PH) domain (). Trio and its homologue UNC-73 are unique within the Dbl family insomuch as they encode two distinct DH/PH domain modules. The PH domain is invariably located immediately C-terminal to the DH domain and this invariant topography suggests a functional interdependence between these two structural modules. Biochemical data have established the role of the conserved DH domain in Rho GTPase interaction and activation, and the role of the tandem PH domain in intracellular targeting and/or regulation of DH domain function. The DH domain of Dbl has been shown to mediate oligomerisation that is mostly homophilic in nature. In addition to the tandem DH/PH domains Dbl family GEFs contain diverse structural motifs like serine/threonine kinase, RBD, PDZ, RGS, IQ, REM, Cdc25, RasGEF, CH, SH2, SH3, EF, spectrin or Ig.The DH domain is composed of three structurally conserved regions separated bymore variable regions. It does not share significant sequence homology withother subtypes of small G-protein GEF motifs such as the Cdc25 domain and theSec7 domain, which specifically interact with Ras and ARF family small GTPases, respectively, nor with other Rho protein interactive motifs, indicating that the Dbl family proteins are evolutionarily unique. The DH domain is composed of 11 alpha helices that are folded into a flattened, elongated α-helix bundle in which two of the three conserved regions, conserved region 1 (CR1) and conserved region 3 (CR3), are exposed near the centre of one surface. CR1 and CR3, together with a part of alpha-6 and the DH/PH junction site, constitute the Rho GTPase interacting pocket.
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Protein Domain
IPR035939 | FGD1_PH1
Type: Domain
Description: This entry represents the N-terminal PH domain of FGD1.In general, FGDs (including FGD1, FGD2, FGD3 and FGD4/Frabin) have a RhoGEF (DH) domain, followed by an N-terminal PH domain, a FYVE domain and a C-terminal PH domain. All FGDs are guanine nucleotide exchange factors that activates the Rho GTPase Cdc42, an important regulator of membrane trafficking. The RhoGEF domain is responsible for GEF catalytic activity, while the N-terminal PH domain is involved in intracellular targeting of the DH domain []. Mutations in the FGD1 gene are responsible for the X-linked disorder known as faciogenital dysplasia (FGDY) []. Both FGD1 and FGD3 are targeted by the ubiquitin ligase SCF(FWD1/beta-TrCP) upon phosphorylation of two serine residues in its DSGIDS motif and subsequently degraded by the proteasome. However, FGD1 and FGD3 induced significantly different morphological changes in HeLa Tet-Off cells and while FGD1 induced long finger-like protrusions, FGD3 induced broad sheet-like protrusions when the level of GTP-bound Cdc42 was significantly increased by the inducible expression of FGD3. They also reciprocally regulated cell motility in inducibly expressed in HeLa Tet-Off cells, FGD1 stimulated cell migration while FGD3 inhibited it. FGD1 and FGD3 therefore play different roles to regulate cellular functions, even though their intracellular levels are tightly controlled by the same destruction pathway through SCF(FWD1/beta-TrCP) [, ].PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner []. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity []. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane []. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes [].
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Protein Domain
IPR035941 | FGD1-4_PH2
Type: Domain
Description: This entry represents the C-terminal PH domain of FGD1-4.In general, FGDs (including FGD1, FGD2, FGD3 and FGD4/Frabin) have a RhoGEF (DH) domain, followed by an N-terminal PH domain, a FYVE domain and a C-terminal PH domain. All FGDs are guanine nucleotide exchange factors that activates the Rho GTPase Cdc42, an important regulatorof membrane trafficking. The RhoGEF domain is responsible for GEF catalytic activity, while the N-terminal PH domain is involved in intracellular targeting of the DH domain []. Mutations in the FGD1 gene are responsible for the X-linked disorder known as faciogenital dysplasia (FGDY) []. Both FGD1 and FGD3 are targeted by the ubiquitin ligase SCF(FWD1/beta-TrCP) upon phosphorylation of two serine residues in its DSGIDS motif and subsequently degraded by the proteasome. However, FGD1 and FGD3 induced significantly different morphological changes in HeLa Tet-Off cells and while FGD1 induced long finger-like protrusions, FGD3 induced broad sheet-like protrusions when the level of GTP-bound Cdc42 was significantly increased by the inducible expression of FGD3. They also reciprocally regulated cell motility in inducibly expressed in HeLa Tet-Off cells, FGD1 stimulated cell migration while FGD3 inhibited it. FGD1 and FGD3 therefore play different roles to regulate cellular functions, even though their intracellular levels are tightly controlled by the same destruction pathway through SCF(FWD1/beta-TrCP) [, ].PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner []. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity []. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane []. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes [].
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Publication
30995482 | J:281311
First Author: Nakano Y
Year: 2019
Journal: Cell Rep
Title: Overlapping Activities of Two Neuronal Splicing Factors Switch the GABA Effect from Excitatory to Inhibitory by Regulating REST.
Volume: 27
Issue: 3
Pages: 860-871.e8
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Protein
Q3UU96
Organism: Mus musculus/domesticus
Length: 1719  
Fragment?: false
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Protein
Q7TT50
Organism: Mus musculus/domesticus
Length: 1713  
Fragment?: false
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Protein
Q3UQN2
Organism: Mus musculus/domesticus
Length: 809  
Fragment?: false
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Protein
Q80UW5
Organism: Mus musculus/domesticus
Length: 1551  
Fragment?: false
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Protein
A0A0U1RPB9
Organism: Mus musculus/domesticus
Length: 173  
Fragment?: false
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Protein
Q8CGG9
Organism: Mus musculus/domesticus
Length: 213  
Fragment?: true
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Protein
Q32MS3
Organism: Mus musculus/domesticus
Length: 450  
Fragment?: false
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Protein
Q3U806
Organism: Mus musculus/domesticus
Length: 581  
Fragment?: true
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Protein
Q7TPP0
Organism: Mus musculus/domesticus
Length: 314  
Fragment?: true
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Protein
Q6A091
Organism: Mus musculus/domesticus
Length: 512  
Fragment?: true
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Protein
Q9CRE2
Organism: Mus musculus/domesticus
Length: 150  
Fragment?: true
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Protein
D3YYN8
Organism: Mus musculus/domesticus
Length: 1691  
Fragment?: false
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Protein
A0A087WS26
Organism: Mus musculus/domesticus
Length: 564  
Fragment?: true
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Protein
B1AW94
Organism: Mus musculus/domesticus
Length: 114  
Fragment?: true
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Protein
A2AQ47
Organism: Mus musculus/domesticus
Length: 160  
Fragment?: true
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Protein
H7BX44
Organism: Mus musculus/domesticus
Length: 1638  
Fragment?: false
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Protein
Q6A075
Organism: Mus musculus/domesticus
Length: 351  
Fragment?: true
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Protein
D6RCG0
Organism: Mus musculus/domesticus
Length: 304  
Fragment?: false
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Protein
J3QQ55
Organism: Mus musculus/domesticus
Length: 168  
Fragment?: true
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Protein
A0A0U1RQ80
Organism: Mus musculus/domesticus
Length: 177  
Fragment?: false
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Protein
Q3UPB8
Organism: Mus musculus/domesticus
Length: 173  
Fragment?: false
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Protein
Q05CX7
Organism: Mus musculus/domesticus
Length: 288  
Fragment?: true
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Protein
B1AW92
Organism: Mus musculus/domesticus
Length: 95  
Fragment?: true
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Protein
E9PVQ1
Organism: Mus musculus/domesticus
Length: 137  
Fragment?: true
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Protein
A0A1D5RLQ9
Organism: Mus musculus/domesticus
Length: 1748  
Fragment?: false
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Protein
B1AW93
Organism: Mus musculus/domesticus
Length: 125  
Fragment?: true
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Protein
Q8BYX6
Organism: Mus musculus/domesticus
Length: 159  
Fragment?: true
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Protein
H3BKQ0
Organism: Mus musculus/domesticus
Length: 250  
Fragment?: true
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Protein
A0A087WRV4
Organism: Mus musculus/domesticus
Length: 110  
Fragment?: true
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Protein
Q3TME9
Organism: Mus musculus/domesticus
Length: 389  
Fragment?: true
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Protein
A0A286YCL2
Organism: Mus musculus/domesticus
Length: 281  
Fragment?: true
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Protein
A0A140LIU6
Organism: Mus musculus/domesticus
Length: 179  
Fragment?: true
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Protein
E9PVY0
Organism: Mus musculus/domesticus
Length: 1732  
Fragment?: false
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Protein
F6RG68
Organism: Mus musculus/domesticus
Length: 356  
Fragment?: false
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Protein
A0A087WNR5
Organism: Mus musculus/domesticus
Length: 55  
Fragment?: true
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Protein
D3YYE9
Organism: Mus musculus/domesticus
Length: 87  
Fragment?: true
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Protein
A6PWR1
Organism: Mus musculus/domesticus
Length: 178  
Fragment?: true
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Protein
D3Z6N2
Organism: Mus musculus/domesticus
Length: 203  
Fragment?: true
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Protein
A0A286YDL7
Organism: Mus musculus/domesticus
Length: 395  
Fragment?: false
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Protein
Q3U0A9
Organism: Mus musculus/domesticus
Length: 266  
Fragment?: true
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Protein
A2AF65
Organism: Mus musculus/domesticus
Length: 527  
Fragment?: false
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Protein
A0A338P6K4
Organism: Mus musculus/domesticus
Length: 109  
Fragment?: true
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Protein
E9Q363
Organism: Mus musculus/domesticus
Length: 108  
Fragment?: true
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Protein
J3QPQ1
Organism: Mus musculus/domesticus
Length: 414  
Fragment?: false
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Protein
Q3U860
Organism: Mus musculus/domesticus
Length: 171  
Fragment?: true
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Protein
E9Q4R3
Organism: Mus musculus/domesticus
Length: 605  
Fragment?: false
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Protein
A0A0U1RNL3
Organism: Mus musculus/domesticus
Length: 360  
Fragment?: false
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Protein
B1AW91
Organism: Mus musculus/domesticus
Length: 168  
Fragment?: true
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Protein
B1AW95
Organism: Mus musculus/domesticus
Length: 64  
Fragment?: true
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Protein
Q3U8N2
Organism: Mus musculus/domesticus
Length: 354  
Fragment?: true
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Protein
H3BJY3
Organism: Mus musculus/domesticus
Length: 146  
Fragment?: true
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Protein
A0A0U1RPD6
Organism: Mus musculus/domesticus
Length: 95  
Fragment?: true
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Protein
A0A2R8W750
Organism: Mus musculus/domesticus
Length: 124  
Fragment?: true
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Protein
A2AQ39
Organism: Mus musculus/domesticus
Length: 208  
Fragment?: true
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Protein
B2RXX8
Organism: Mus musculus/domesticus
Length: 1732  
Fragment?: false
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Protein
Q3UP40
Organism: Mus musculus/domesticus
Length: 191  
Fragment?: true
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Protein
B2RQQ7
Organism: Mus musculus/domesticus
Length: 1713  
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