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Search results 3301 to 3400 out of 4514 for Cdc42

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Type Details Score
Publication
17371834 | -
First Author: Mattila PK
Year: 2007
Journal: J Cell Biol
Title: Missing-in-metastasis and IRSp53 deform PI(4,5)P2-rich membranes by an inverse BAR domain-like mechanism.
Volume: 176
Issue: 7
Pages: 953-64
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Publication
14704859 | -
First Author: Rothhammer T
Year: 2004
Journal: Cell Mol Life Sci
Title: The Ets-1 transcription factor is involved in the development and invasion of malignant melanoma.
Volume: 61
Issue: 1
Pages: 118-28
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Publication
9031109 | -
First Author: Wlodarska I
Year: 1996
Journal: Leuk Lymphoma
Title: ETV6 gene rearrangements in hematopoietic malignant disorders.
Volume: 23
Issue: 3-4
Pages: 287-95
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Publication
12577325 | J:135865
First Author: Coonan JR
Year: 2003
Journal: J Comp Neurol
Title: Role of EphA4 in defining the position of a motoneuron pool within the spinal cord.
Volume: 458
Issue: 1
Pages: 98-111
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Publication
14659698 | J:87527
First Author: Melino G
Year: 2003
Journal: Trends Biochem Sci
Title: Functional regulation of p73 and p63: development and cancer.
Volume: 28
Issue: 12
Pages: 663-70
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Publication
14499651 | -
First Author: Bloyer S
Year: 2003
Journal: Dev Biol
Title: Identification and characterization of polyhomeotic PREs and TREs.
Volume: 261
Issue: 2
Pages: 426-42
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Publication
11311560 | -
First Author: Ishikawa S
Year: 2001
Journal: Gene
Title: Interaction of MCC2, a novel homologue of MCC tumor suppressor, with PDZ-domain Protein AIE-75.
Volume: 267
Issue: 1
Pages: 101-10
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Publication
15219944 | -
First Author: Hirai A
Year: 2004
Journal: Cancer Lett
Title: Expression of AIE-75 PDZ-domain protein induces G2/M cell cycle arrest in human colorectal adenocarcinoma SW480 cells.
Volume: 211
Issue: 2
Pages: 209-18
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Publication
8643625 | -
First Author: Kolluri R
Year: 1996
Journal: Proc Natl Acad Sci U S A
Title: Direct interaction of the Wiskott-Aldrich syndrome protein with the GTPase Cdc42.
Volume: 93
Issue: 11
Pages: 5615-8
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Publication
11076964 | -
First Author: Lee WL
Year: 2000
Journal: J Cell Biol
Title: Fission yeast myosin-I, Myo1p, stimulates actin assembly by Arp2/3 complex and shares functions with WASp.
Volume: 151
Issue: 4
Pages: 789-800
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Publication
23290554 | -
First Author: Urbanek AN
Year: 2013
Journal: Curr Biol
Title: A novel actin-binding motif in Las17/WASP nucleates actin filaments independently of Arp2/3.
Volume: 23
Issue: 3
Pages: 196-203
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Publication
12879077 | -
First Author: Katoh H
Year: 2003
Journal: Nature
Title: RhoG activates Rac1 by direct interaction with the Dock180-binding protein Elmo.
Volume: 424
Issue: 6947
Pages: 461-4
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Publication
12805377 | -
First Author: Prieto-Sánchez RM
Year: 2003
Journal: J Biol Chem
Title: Structural basis for the signaling specificity of RhoG and Rac1 GTPases.
Volume: 278
Issue: 39
Pages: 37916-25
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Publication
16568096 | -
First Author: Prieto-Sánchez RM
Year: 2006
Journal: Oncogene
Title: Involvement of the Rho/Rac family member RhoG in caveolar endocytosis.
Volume: 25
Issue: 21
Pages: 2961-73
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Publication
16621998 | J:131659
First Author: Condliffe AM
Year: 2006
Journal: J Immunol
Title: RhoG regulates the neutrophil NADPH oxidase.
Volume: 176
Issue: 9
Pages: 5314-20
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Protein Domain
IPR016018 | SopE_N_dom
Type: Domain
Description: The type III secretion system of Gram-negative bacteria is used to transport virulence factors from the pathogen directly into the host cell []and is only triggered when the bacterium comes into close contact with the host. Effector proteins secreted by the type III system do not possess a secretion signal, and are considered unique because of this. Salmonella spp. secrete an effector protein called SopE that is responsible for stimulating the reorganisation of the host cell actin cytoskeleton, and ruffling of the cellular membrane []. It acts as a guanyl-nucleotide-exchange factor on Rho-GTPase proteins such as Cdc42 and Rac. As it is imperative for the bacterium to revert the cell back to its "normal"state as quickly as possible, another tyrosine phosphatase effector called SptP reverses the actions brought about by SopE [].Recently, it has been found that SopE and its protein homologue SopE2 can activate different sets of Rho-GTPases in the host cell []. Far from being a redundant set of two similar type III effectors, they both act in unison to specifically activate different Rho-GTPase signalling cascades in the host cell during infection.This entry represents the N-terminal domain of SopE and SopE2. The function of this domain is unknown.
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Protein Domain
IPR016019 | SopE_GEF_dom
Type: Domain
Description: The type III secretion system of Gram-negative bacteria is used to transport virulence factors from the pathogen directly into the host cell []and is only triggered when the bacterium comes into close contact with the host. Effector proteins secreted by the type III system do not possess a secretion signal, and are considered unique because of this. Salmonella spp. secrete an effector protein called SopE that is responsible for stimulating the reorganisation of the host cell actin cytoskeleton, and ruffling of the cellular membrane []. It acts as a guanyl-nucleotide-exchange factor on Rho-GTPase proteins such as Cdc42 and Rac. As it is imperative for the bacterium to revert the cell back to its "normal"state as quickly as possible, another tyrosine phosphatase effector called SptP reverses the actions brought about by SopE []. Recently, it has been found that SopE and its protein homologue SopE2 can activate different sets of Rho-GTPases in the host cell []. Far from being a redundant set of two similar type III effectors, they both act in unison to specifically activate different Rho-GTPase signalling cascades in the host cell during infection.This entry represents the guanine nucleotide exchange factor domain of SopE. This domain has an α-helical structure consisting of two three-helix bundles arranged in a lamdba shape [, ].
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Protein Domain
IPR037793 | OCRL1/INPP5B_INPP5c
Type: Domain
Description: OCRL1 hydrolyzes phosphatidylinositol 4,5-bisphosphate (PtIns(4,5)P2) and the signaling molecule phosphatidylinositol 1,4,5-trisphosphate (PtIns(1,4,5)P3), and thereby modulates cellular signaling events []. OCRL1 resides on vesicular structures throughout the endosomal system and the Golgi complex, and is also present at the plasma membrane in membrane ruffles and at late-stage endocytic clathrin-coated pits. It binds clathrin, clathrin adaptors, several GTPases, and the endocytic proteins APPL1 and Ses1/2 []. Mutations in the OCRL1 gene cause Lowe Syndrome, leading to cataracts, mental retardation and renal failure []. Mutations in OCRL can also give rise to a milder pathology, Dent disease 2, which is characterised by renal Fanconi syndrome in the absence of extrarenal pathologies [].OCRL1 shares ~45% sequence identity with INPP5B and has the same domain organization. However, a loop in the Rho GAP domain contains a second clathrin box which is absent in INPP5B. INPP5B shares most interacting partners with OCRL, except for clathrin and the endocytic clathrin adaptor AP-2 []. OCRL1 contains a PH domain, a 5-phosphatase domain, an ASH domain and a Rho-GAP domain. The RhoGAP domain lacks the catalytic arginine and is catalytically inactive. However, the RhoGAP domain of OCRL interacts with Rac and Cdc42, but only the Cdc42 interaction is GTP-dependent. The RhoGAP domain also interacts with three endocytic proteins containing the F&H motif: APPL1, Ses1 and Ses2. OCRL1 interacts with Rab GTPase (Rab8) through its ASH domain []. This entry represents the inositol polyphosphate 5-phosphatase (INPP5c) domain of OCRL1/INPP5B.
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Protein Domain
IPR046770 | DOCKER_Lobe_B
Type: Domain
Description: This entry represents a conserved region within a number of eukaryotic dedicator of cytokinesis proteins (DOCK), which are guanine nucleotide exchange factors (GEFs) [, , ], that activate some small GTPases by exchanging bound GDP for free GTP such as Rac. DOCK proteins are required during several cellular processes, such as cell motility and phagocytosis []. These proteins have a DOCK-homology region 1 (DHR-1, also known as DOCK-type C2 domain) at the N-terminal and a DHR-2 (also known as DOCKER domain) at the C-terminal. The DOCKER domain () is a GEF catalytic domain organised into three lobes, A, B and C, with the Rho-family binding site and catalytic centre generated entirely from lobes B and C. This entry represents Lobe B, which adopts an unusual architecture of two antiparallel beta sheets disposed in a loosely packed orthogonal arrangement. This lobe changes its position relative to lobe C and the bound GTPase, which suggests that lobe B distinguishes between the switch 1 conformations of the small GTPases Rac1 and Cdc42 [, ].
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Protein Domain
IPR005414 | SopE
Type: Family
Description: The type III secretion system of Gram-negative bacteria is used to transport virulence factors from the pathogen directly into the host cell []and is only triggered when the bacterium comes into close contact with the host. Effector proteins secreted by the type III system do not possess a secretion signal, and are considered unique because of this. Salmonella spp. secrete an effector protein called SopE that is responsible for stimulating the reorganisation of the host cell actin cytoskeleton, and ruffling of the cellular membrane []. It acts as a guanyl-nucleotide-exchange factor on Rho-GTPase proteins such as Cdc42 and Rac. As it is imperative for the bacterium to revert the cell back to its "normal"state as quickly as possible, another tyrosine phosphatase effector called SptP reverses the actions brought about by SopE []. SopE and its protein homologue SopE2 canactivate different sets of Rho-GTPases in the host cell []. Far from being a redundant set of two similar type III effectors, they both act in unison to specifically activate different Rho-GTPase signalling cascades in thehost cell during infection.
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Protein Domain
IPR042734 | RhoG
Type: Family
Description: RhoG is a GTPase with high sequence similarity to members of the Rac subfamily, including the regions involved in effector recognition and binding. However, RhoG does not bind to known Rac1 and Cdc42 effectors, including proteins containing a Cdc42/Rac interacting binding (CRIB) motif. Instead, RhoG interacts directly with Elmo, an upstream regulator of Rac1, in a GTP-dependent manner and forms a ternary complex with Dock180 to induce activation of Rac1 []. The RhoG-Elmo-Dock180 pathway is required for activation of Rac1 and cell spreading mediated by integrin, as well as for neurite outgrowth induced by nerve growth factor. Thus RhoG activates Rac1 through Elmo and Dock180 to control cell morphology []. RhoG has also been shown to play a role in caveolar trafficking []and has a novel role in signaling the neutrophil respiratory burst stimulated by G protein-coupled receptor (GPCR) agonists []. Most Rho proteins contain a lipid modification site at the C terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins.
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Protein Domain
IPR027641 | WASP
Type: Family
Description: This entry represents the Actin nucleation-promoting factor WAS (WASP). The WASP proteins signal to the cytoskeleton through the Arp2/3 complex, an actin-nucleating assembly that regulates the structure and dynamics of actin filament networks at the leading edge of the cell []. The activity of WASP can be regulated by the Rho-family GTPase, Cdc42 []. Mutations in WASP lead to the Wiskott-Aldrich syndrome, a paediatric disorder characterised by actin cytoskeletal defects in haematopoietic cells, leading clinically to thrombocytopenia, eczema and immunodeficiency [].Similar to mammalian WASP proteins, Wsp1 and Las17 also has a role in regulating actin assembly [, ]. In Saccharomyces cerevisiae, Las17 is the primary activator of Arp2/3-driven actin nucleation and is required for membrane invagination during endocytosis []. Las17 can also nucleate actin filaments independently of Arp2/3 through its polyproline domain [].WASP family members have unique N-terminal regions, followed by a central segment rich in proline, and a common C-terminal region. Their conserved C-terminal VCA domain consists of two WH2 (WASP homology 2) domains ("V"referring to either a single or multiple WH2 domains), followed by a connector domain ("C") and an acidic short extension ("A"). In the VCA region, the WH2 domain(s) bind G-actin, whereas the CA domain binds Arp2/3 complex []. Their distinct N-terminal region enables family members to activate Arp2/3 in response to differentupstream signals.
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Protein Domain
IPR001060 | FCH_dom
Type: Domain
Description: FCH domain is a short conserved region of around 60 amino acids first described as a region of homology between FER and CIP4 proteins []. In the CIP4 protein the FCH domain binds to microtubules []. The FCH domain is always found N-terminally and is followed by a coiled-coil region. The FCH and coiled-coil domains are structurally similar to Bin/amphiphysin/RVS (BAR) domains []. They are α-helical membrane-binding modules that function in endocytosis, regulation of the actin cytoskeleton and signalling []. Proteins containing an FCH domain can be divided in 3 classes []:A subfamily of protein kinases usually associated with an SH2 domain:Fps/fes (Fujimani poultry sarcoma/feline sarcoma) proto-oncogenes. They are non-receptor protein-tyrosine kinases preferentially expressed in myeloid lineage. The viral oncogene has an unregulated kinase activity which abrogates the need for cytokines and influences differentiation of haematopoietic progenitor cells.Fes related protein (fer). It is an ubiquitously expressed homologue of Fes.Adaptor proteins usually associated with a C-terminal SH3 domain:Schizosaccharomyces pombe CDC15 protein. It mediates cytoskeletal rearrangements required for cytokinesis. It is essential for viability.CD2 cytoplasmic domain binding protein.Mammalian Cdc42-interacting protein 4 (CIP4). It may act as a link between Cdc42 signaling and regulation of the actin cytoskeleton.Mammalian PACSIN proteins. A family of cytoplasmic phosphoproteins playing a role in vesicle formation and transport.A subfamily of Rho-GAP proteins:Mammalian RhoGAP4 proteins. They may down-regulate Rho-like GTPases in hematopoietic cells.Yeast RHO GTPase-activating protein RGD1 (also known as YBR260C).Caenorhabditis elegans hypothetical protein ZK669.1.
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Protein Domain
IPR001180 | CNH_dom
Type: Domain
Description: Based on sequence similarities a domain of homology has been identified in the following proteins [, ]:Citron and Citron kinase. These two proteins interact with the GTP-bound forms of the small GTPases Rho and Rac but not with Cdc42.Myotonic dystrophy kinase-related Cdc42-binding kinase (MRCKalpha). This serine/threonine kinase interacts with the GTP-bound form of the small GTPase Cdc42 and to a lesser extent with that of Rac.NCK Interacting Kinase (NIK), a serine/threonine protein kinase.ROM-1 and ROM-2, from yeast. These proteins are GDP/GTP exchange proteins (GEPs) for the small GTP binding protein Rho1.This domain, called the citron homology domain (CNH), is often found after cysteine rich and pleckstrin homology (PH) domains at the C-terminal end of a group of eukaryotic proteins. It is thought to act as a regulatory domain and could be involved in macromolecular interactions [, , , ]. Its structure has been solved in Rho guanyl nucleotide exchange factor (Rom2) from Neosartorya fumigata (Aspergillus fumigatus, ), where it shows a canonical β-propeller fold containing seven blades connected by small loops and arranged in a circular fashion [].
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Protein Domain
IPR013606 | I-BAR_dom
Type: Domain
Description: The I-BAR domain (also known as IMD domain, IRSp53 and MIM homology domain) is a BAR-like domain of approximately 250 amino acids found at the N-terminal in the IRSp53 (insulin receptor tyrosine kinase substrate p53) and in the evolutionarily related IRSp53/MIM family. The BAR domain forms an anti-parallel all-helical dimer, with a curved (banana-like) shape, that promotes membrane tubulation. The BAR domain containing proteins can be classified into three types: BAR, F-BAR and I-BAR. BAR and F-BAR proteins generate positive membrane curvature, while I-BAR proteins induce negative curvature [, ]. The I-BAR domain containing proteins include: Vertebrate MIM (missing in metastasis), an actin-binding scaffold protein that may be involved in cancer metastasis.Vertebrate ABBA, a MIM-related protein.Vertebrate insulin receptor tyrosine kinase substrate p53 (IRSp53), a multifunctional adaptor protein that links Rac1 with a Wiskott-Aldrich syndrome family verprolin-homologous protein 2 (WAVE2) to induce lamellipodia or Cdc42 with Mena to induce filopodia [].Vertebrate IRTKS.Vertebrate Pinkbar.Drosophila melanogaster (Fruit fly) CG32082-PA.Caenorhabditis elegans M04F3.5 protein.The vertebrate I-BAR family is divided into two major groups: the IRSp53/IRTKS/Pinkbar subfamily and the MIM/ABBA subfamily. The putative invertebrate homologues are positioned between them. The IRSp53/IRTKS/Pinkbar subfamily members contain a SH3 domain, and the MIM/ABBA subfamily proteins contain a WH2 (WASP-homology 2) domain. The vertebrate SH3-containing subfamily is further divided into three groups according to the presence or absence of the WWB and the half-CRIB motif [, ]. The BAR domain binds phosphoinositide-rich vesicles with high affinity and does not display strong actin filament binding/bundling activity [, ].
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Protein Domain
IPR013761 | SAM/pointed_sf
Type: Homologous_superfamily
Description: Sterile alpha motif (SAM) domains are known to be involved in diverse protein-protein interactions, associating with both SAM-containing and non-SAM-containing proteins pathway []. SAM domains exhibit a conserved structure, consisting of a 4-5-helical bundle of two orthogonally packed alpha-hairpins. However SAM domains display a diversity of function, being involved in interactions with proteins, DNA and RNA []. The name sterile alpha motif arose from its presence in proteins that are essential for yeast sexual differentiation. The SAM domain has had various names, including SPM, PTN (pointed), SEP (yeast sterility, Ets-related, PcG proteins), NCR (N-terminal conserved region) and HLH (helix-loop-helix) domain, all of which are related and can be classified as SAM domains.SAM domains occur in eukaryotic and in some bacterial proteins. Structures have been determined for several proteins that contain SAM domains, including Ets-1 transcription factor, which plays a role in the development and invasion of tumour cells by regulating the expression of matrix-degrading proteases []; Etv6 transcription factor, gene rearrangements of which have been demonstrated in several malignancies []; EphA4 receptor tyrosine kinase, which is believed to be important for the correct localization of a motoneuron pool to a specific position in the spinal cord []; EphB2 receptor, which is involved in spine morphogenesis via intersectin, Cdc42 and N-Wasp []; p73, a p53 homologue involved in neuronal development []; and polyhomeotic, which is a member of the Polycomb group of genes (Pc-G) required for the maintenance of the spatial expression pattern of homeotic genes [].
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Protein Domain
IPR035949 | SopE-like_GEF_dom_sf
Type: Homologous_superfamily
Description: The type III secretion system of Gram-negative bacteria is used to transport virulence factors from the pathogen directly into the host cell []and is only triggered when the bacterium comes into close contact with the host. Effector proteins secreted by the type III system do not possess a secretion signal, and are considered unique because of this. Salmonella spp. secrete an effector protein called SopE that is responsible for stimulating the reorganisation of the host cell actin cytoskeleton, and ruffling of the cellular membrane []. It acts as a guanyl-nucleotide-exchange factor on Rho-GTPase proteins such as Cdc42 and Rac. As it is imperative for the bacterium to revert the cell back to its "normal"state as quickly as possible, another tyrosine phosphatase effector called SptP reverses the actions brought about by SopE []. Recently, it has been found that SopE and its protein homologue SopE2 can activate different sets of Rho-GTPases in the host cell []. Far from being a redundant set of two similar type III effectors, they both act in unison to specifically activate different Rho-GTPase signalling cascades in the host cell during infection.This entry represents the guanine nucleotide exchange factor domain of SopE and homologues. This domain has an α-helical structure consisting of two three-helix bundles arranged in a lamdba shape [, ].
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Protein
A0A498WGD8
Organism: Mus musculus/domesticus
Length: 292  
Fragment?: false
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Protein Coding Gene
MGI:1915589 | Ccdc88c
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:108474 | Fzd6
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:108100 | Dvl3
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1931553 | Rhoq
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:101766 | Ryk
Type: protein_coding_gene
Organism: mouse, laboratory
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Publication
19929439 | J:183371
First Author: Leung R
Year: 2010
Journal: J Bone Miner Res
Title: Filamin A regulates monocyte migration through Rho small GTPases during osteoclastogenesis.
Volume: 25
Issue: 5
Pages: 1077-91
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Publication
37635877 | J:340049
 
First Author: Valdivia A
Year: 2023
Journal: Front Cell Dev Biol
Title: Nox1-based NADPH oxidase regulates the Par protein complex activity to control cell polarization.
Volume: 11
Pages: 1231489
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Publication
31302143 | J:290900
First Author: López-Posadas R
Year: 2019
Journal: Gastroenterology
Title: Inhibiting PGGT1B Disrupts Function of RHOA, Resulting in T-cell Expression of Integrin α4β7 and Development of Colitis in Mice.
Volume: 157
Issue: 5
Pages: 1293-1309
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Protein
H3BKT3
Organism: Mus musculus/domesticus
Length: 128  
Fragment?: true
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Protein
A0A2I3BRJ9
Organism: Mus musculus/domesticus
Length: 177  
Fragment?: true
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Protein
H3BKV6
Organism: Mus musculus/domesticus
Length: 161  
Fragment?: true
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Publication
19745154 | -
First Author: Yang J
Year: 2009
Journal: Science
Title: Activation of Rho GTPases by DOCK exchange factors is mediated by a nucleotide sensor.
Volume: 325
Issue: 5946
Pages: 1398-402
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Publication
23505444 | -
First Author: Ma Y
Year: 2013
Journal: PLoS One
Title: The inverse F-BAR domain protein srGAP2 acts through srGAP3 to modulate neuronal differentiation and neurite outgrowth of mouse neuroblastoma cells.
Volume: 8
Issue: 3
Pages: e57865
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Publication
20810653 | -
First Author: Guo S
Year: 2010
Journal: J Biol Chem
Title: srGAP2 arginine methylation regulates cell migration and cell spreading through promoting dimerization.
Volume: 285
Issue: 45
Pages: 35133-41
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Publication
22381590 | -
First Author: Pirruccello M
Year: 2012
Journal: Trends Biochem Sci
Title: Inositol 5-phosphatases: insights from the Lowe syndrome protein OCRL.
Volume: 37
Issue: 4
Pages: 134-43
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Publication
9115846 | -
First Author: Romero F
Year: 1996
Journal: Cell Signal
Title: Structure and function of vav.
Volume: 8
Issue: 8
Pages: 545-53
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Publication
21901156 | -
First Author: Grieve AG
Year: 2011
Journal: PLoS One
Title: Lowe Syndrome protein OCRL1 supports maturation of polarized epithelial cells.
Volume: 6
Issue: 8
Pages: e24044
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Publication
21971085 | -
First Author: Vicinanza M
Year: 2011
Journal: EMBO J
Title: OCRL controls trafficking through early endosomes via PtdIns4,5Pâ‚‚-dependent regulation of endosomal actin.
Volume: 30
Issue: 24
Pages: 4970-85
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Publication
28669993 | -
First Author: De Matteis MA
Year: 2017
Journal: Nat Rev Nephrol
Title: The 5-phosphatase OCRL in Lowe syndrome and Dent disease 2.
Volume: 13
Issue: 8
Pages: 455-470
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Protein
Q8R3Y5
Organism: Mus musculus/domesticus
Length: 413  
Fragment?: false
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Publication
16418535 | -
First Author: Tsujita K
Year: 2006
Journal: J Cell Biol
Title: Coordination between the actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis.
Volume: 172
Issue: 2
Pages: 269-79
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Protein
Q9ERR1
Organism: Mus musculus/domesticus
Length: 345  
Fragment?: false
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Protein
Q5SXE1
Organism: Mus musculus/domesticus
Length: 80  
Fragment?: true
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Protein
Q8C8B2
Organism: Mus musculus/domesticus
Length: 294  
Fragment?: false
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Protein
Z4YMR3
Organism: Mus musculus/domesticus
Length: 262  
Fragment?: true
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Protein
A0A087WPA4
Organism: Mus musculus/domesticus
Length: 190  
Fragment?: true
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Protein
D2JZZ5
Organism: Mus musculus/domesticus
Length: 80  
Fragment?: true
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Protein
G5E8E3
Organism: Mus musculus/domesticus
Length: 413  
Fragment?: false
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Protein
Q9D0J3
Organism: Mus musculus/domesticus
Length: 109  
Fragment?: false
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Protein
A0A0R4J2B5
Organism: Mus musculus/domesticus
Length: 391  
Fragment?: false
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Protein
D3Z1X5
Organism: Mus musculus/domesticus
Length: 170  
Fragment?: true
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Protein
A0A087WRI8
Organism: Mus musculus/domesticus
Length: 397  
Fragment?: false
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Protein
Q5SXE2
Organism: Mus musculus/domesticus
Length: 205  
Fragment?: true
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Protein
A2ALX7
Organism: Mus musculus/domesticus
Length: 385  
Fragment?: false
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Protein
Q3THY1
Organism: Mus musculus/domesticus
Length: 225  
Fragment?: false
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Protein
A2ALX6
Organism: Mus musculus/domesticus
Length: 294  
Fragment?: false
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Publication
11416147 | -
First Author: Xu Z
Year: 2001
Journal: Mol Cell Biol
Title: The MLK family mediates c-Jun N-terminal kinase activation in neuronal apoptosis.
Volume: 21
Issue: 14
Pages: 4713-24
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Publication
19366662 | -
First Author: Vingadassalom D
Year: 2009
Journal: Proc Natl Acad Sci U S A
Title: Insulin receptor tyrosine kinase substrate links the E. coli O157:H7 actin assembly effectors Tir and EspF(U) during pedestal formation.
Volume: 106
Issue: 16
Pages: 6754-9
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Publication
16326391 | -
First Author: Itoh T
Year: 2005
Journal: Dev Cell
Title: Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins.
Volume: 9
Issue: 6
Pages: 791-804
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Publication
20585502 | -
First Author: Ahmed S
Year: 2010
Journal: Commun Integr Biol
Title: F-BAR domain proteins: Families and function.
Volume: 3
Issue: 2
Pages: 116-21
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Publication
24093049 | -
First Author: Bradshaw NJ
Year: 2013
Journal: Biomol Concepts
Title: NDE1 and NDEL1: twin neurodevelopmental proteins with similar 'nature' but different 'nurture'.
Volume: 4
Issue: 5
Pages: 447-64
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Publication
20067472 | -
First Author: Ola A
Year: 2010
Journal: Br J Pharmacol
Title: The mixed-lineage kinase 1-3 signalling pathway regulates stress response in cardiac myocytes via GATA-4 and AP-1 transcription factors.
Volume: 159
Issue: 3
Pages: 717-25
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Publication
27259981 | -
First Author: Craige SM
Year: 2016
Journal: Biochim Biophys Acta
Title: Mixed - Lineage Protein kinases (MLKs) in inflammation, metabolism, and other disease states.
Volume: 1862
Issue: 9
Pages: 1581-6
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Publication
17408454 | -
First Author: Handley ME
Year: 2007
Journal: Int J Exp Pathol
Title: Mixed lineage kinases (MLKs): a role in dendritic cells, inflammation and immunity?
Volume: 88
Issue: 2
Pages: 111-26
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Publication
15610029 | -
First Author: Durkin JT
Year: 2004
Journal: Biochemistry
Title: Phosphoregulation of mixed-lineage kinase 1 activity by multiple phosphorylation in the activation loop.
Volume: 43
Issue: 51
Pages: 16348-55
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Publication
18414056 | J:137358
First Author: Bisson N
Year: 2008
Journal: Cell Cycle
Title: Mice lacking both mixed-lineage kinase genes Mlk1 and Mlk2 retain a wild type phenotype.
Volume: 7
Issue: 7
Pages: 909-16
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Publication
19332348 | -
First Author: Nagao M
Year: 2009
Journal: J Neurol Sci
Title: Mixed lineage kinase 2 and hippocalcin are localized in Lewy bodies of Parkinson's disease.
Volume: 281
Issue: 1-2
Pages: 51-4
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Publication
20514022 | -
First Author: Chen J
Year: 2010
Journal: Oncogene
Title: MLK3 is critical for breast cancer cell migration and promotes a malignant phenotype in mammary epithelial cells.
Volume: 29
Issue: 31
Pages: 4399-411
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Publication
19782705 | J:164833
First Author: Cole ET
Year: 2009
Journal: Biochim Biophys Acta
Title: Mixed lineage kinase 3 negatively regulates IKK activity and enhances etoposide-induced cell death.
Volume: 1793
Issue: 12
Pages: 1811-8
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Protein Domain
IPR037787 | OCRL1_PH
Type: Domain
Description: OCRL1 hydrolyzes phosphatidylinositol 4,5-bisphosphate (PtIns(4,5)P2) and the signaling molecule phosphatidylinositol 1,4,5-trisphosphate (PtIns(1,4,5)P3), and thereby modulates cellular signaling events []. OCRL1 resides on vesicular structures throughout the endosomal system and the Golgi complex, and is also present at the plasma membrane in membrane ruffles and at late-stage endocytic clathrin-coated pits. It binds clathrin, clathrin adaptors, several GTPases, and the endocytic proteins APPL1 and Ses1/2 []. Mutations in the OCRL1 gene cause Lowe Syndrome, leading to cataracts, mental retardation and renal failure []. Mutations in OCRL can also give rise to a milder pathology, Dent disease 2, which is characterised by renal Fanconi syndrome in the absence of extrarenal pathologies [].OCRL1 shares ~45% sequence identity with INPP5B (not included in this entry) and has the same domain organization. However, a loop in the Rho GAP domain contains a second clathrin box which is absent in INPP5B. INPP5B shares most interacting partners with OCRL, except for clathrin and the endocytic clathrin adaptor AP-2 []. OCRL1 contains a PH domain, a 5-phosphatase domain, an ASH domain and a Rho-GAP domain. The RhoGAP domain lacks the catalytic arginine and is catalytically inactive. However, the RhoGAP domain of OCRL interacts with Rac and Cdc42, but only the Cdc42 interaction is GTP-dependent. The RhoGAP domain also interacts with three endocytic proteins containing the F&H motif: APPL1, Ses1 and Ses2. OCRL1 interacts with Rab GTPase (Rab8) through its ASH domain []. This entry represents the PH domain of OCRL1 []. The PH domain connects to the 5-phosphatase domain, which has a Dnase I-like fold [].
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Protein Domain
IPR027357 | DOCKER_dom
Type: Domain
Description: Rho guanosine triphosphatases (GTPases) are critical regulators of cell motility, polarity, adhesion, cytoskeletal organisation, proliferation, geneexpression, and apoptosis. Conversion of these biomolecular switches to the activated GTP-bound state is controlled by two families of guanine nucleotide exchanges factors (GEFs). DH-PH proteins are a large group of Rho GEFs comprising a catalytic Dbl homology (DH) domain with anadjacent pleckstrin homology (PH) domain within the context of functionally diverse signalling modules. The evolutionarily distinct and smaller family of DOCK (dedicator of cytokinesis) or CDM (CED-5, DOCK1180, Myoblast city) proteins activate either Rac or Cdc42 to control cell migration, morphogenesis, and phagocytosis. DOCK proteins share the DOCK-type C2 domain (also termed the DOCK-homology region (DHR)-1 or CDM-zizimin homology 1 (CZH1) domain and the DOCKER domain (also termed the DHR-2 or CZH2 domain) [, , , , , , ].The DOCK-type C2 domain is located toward the N terminus []. The DOCKER domain is a GEF catalytic domain of ~400 residues situated within the C terminus. The structure of the DOCKER domain differs from that of other GEF catalytic domains. It is organised into three lobes of roughly equal size (lobes A, B, and C), with the Rho-family binding site and catalytic centre generated entirely from lobes B and C. Lobe A is formed from an antiparallel array of alpha helices. Through extensive contacts with lobe B, lobe A stabilises the DHR2 domain. Lobe B adopts an unusual architecture of two antiparallel beta sheets disposed in a loosely packed orthogonal arrangement, whereas lobe C comprises a four-helix bundle [, ].This entry represents the DOCKER domain.
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Protein Domain
IPR027007 | C2_DOCK-type_domain
Type: Domain
Description: Rho guanosine triphosphatases (GTPases) are critical regulators of cell motility, polarity, adhesion, cytoskeletal organisation, proliferation, geneexpression, and apoptosis. Conversion of these biomolecular switches to the activated GTP-bound state is controlled by two families of guanine nucleotide exchanges factors (GEFs). DH-PH proteins are a large group of Rho GEFs comprising a catalytic Dbl homology (DH) domain with an adjacent pleckstrin homology (PH) domain within the context of functionally diverse signalling modules. The evolutionarily distinct andsmaller family of DOCK (dedicator of cytokinesis) or CDM (CED-5, DOCK1180, Myoblast city) proteins activate either Rac or Cdc42 to control cell migration, morphogenesis, and phagocytosis. DOCK proteins share the DOCK-type C2 domain (also termed the DOCK-homology region (DHR)-1 or CDM-zizimin homology 1 (CZH1) domain and the DHR-2 domain (also termed the CZH2 or DOCKER domain), [, , , , , ].The ~200 residue DOCK-type C2 domain is located toward the N terminus. It adopts a C2-like architecture and interacts with phosphatidylinositol3,4,5-trisphosphate []to mediate signalling and membrane localization. The central core of the DOCK-type C2 domain domain adopts an antiparallel β-sandwich with the "type II"C2 domain fold (a circular permutation of the more common "type I"topology), in which two 4-stranded sheets with strand order 6-5-2-3 and 7-8-1-4 create convex- and concave-exposed faces, respectively [].Some DOCK proteins are listed below:Mammalian Mammalian dedicator of cytokinesis 180 (DOCK180 or DOCK1),important for cell migration.Mammalian DOCK2, important for lymphocyte development, homong, activation,adhesion, polarization and migration processes.Mammalian DOCK3 (also known as MOCA), is expressed predominantly in neuronsand resides in growth cones and membrane ruffles.Mammalian DOCK4, possesses tumor suppressor properties.Mammalian DOCK9 (zizimin1), plays an important role in dendrite growth inhippocampal neurons through activation of Cdc42.Drosophila melanogaster Myoblast city.Caenorhabditis elegans CED-5.
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Protein Domain
IPR031160 | F_BAR
Type: Domain
Description: All eukaryotic cells are surrounded by a plasma membrane, and they alsocontain multiple membrane-based organelles and structures inside cells. Thusmembrane remodeling is likely to be important for most cellular activities anddevelopment. The Bin-Amphiphysin-Rvs (BAR) domain superfamily of proteins hasbeen found to play a major role in remodeling cellular membranes linked withorganelle biogenesis, membrane trafficking, cell division, cell morphology andcell migration. The BAR domain superfamily of proteins is evolutionarilyconserved with representative members present from yeast to man. Currentlythere are three distinct families of BAR domain proteins: classical BAR, F-BAR (FCH-BAR e.g., Fes/CIP4 homology BAR e.g., Toca-1) and I-BAR (inverse-BAR e.g., IRSp53). The classical BAR, F-BAR, and I-BAR domainsare structurally similar homodimeric modules with antiparallel arrangement ofmonomers [, ].The F-BAR domain is emerging as an important player in membrane remodelingpathways. F-BAR domain proteins couple membrane remodeling with actin dynamicsassociated with endocytic pathways and filopodium formation. F-BAR domaincontaining proteins can be categorized into five sub-families based on theirphylogeny which is consistent with the additional protein domains theypossess, for example, RhoGAP domains, Cdc42 binding sites,SH2 domains, SH3 domains and tyrosinekinase domains [].The N-terminal part (about one third) of the F-BAR domain was previouslycharacterised as an FCH (FER-CIP4 homology) domain. However, the region ofsequence similarity extends to an adjacent region with a coiled-coil (CC)structure. Hence, the F-BAR domain (FCH+CC, ~300 amino acids) has also beencalled extended FC (EFC) domain. The F-BAR domain plays a role in dimerizationand membrane phospholipid binding. It binds specifically to certain kinds oflipids and acts as a a dimeric membrane-binding curvature effector [, , ].The F-BAR domain is composed of five helices. Its structure is composed of ashort N-terminal helix, three long α-helices, and a short C-terminal helixfollowed by an extended peptide of 17 amino acids [, ].
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Protein Domain
IPR035779 | MLK1-3_SH3
Type: Domain
Description: MLKs 1, 2, and 3 are Serine/Threonine Kinases (STKs), catalyzing the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals [, ]. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation [, ]. Little is known about the specific function of MLK1, also called MAP3K9. It is capable of activating the c-Jun N-terminal kinase pathway []. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans []. MLK2, also called MAP3K10, is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease []. MLK3, also called MAP3K11, is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells []. It also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and thus impacts inflammation and immunity []. MLKs contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac.This entry represents the SH3 domains of MLKs.
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Protein
Q3UYH1
Organism: Mus musculus/domesticus
Length: 279  
Fragment?: true
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Protein
Q8C9Y7
Organism: Mus musculus/domesticus
Length: 692  
Fragment?: false
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Protein
Q6P1D6
Organism: Mus musculus/domesticus
Length: 900  
Fragment?: false
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Publication
23384583 | -
First Author: Chen Y
Year: 2013
Journal: Semin Cell Dev Biol
Title: Biochemical and functional significance of F-BAR domain proteins interaction with WASP/N-WASP.
Volume: 24
Issue: 4
Pages: 280-6
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Protein
A0A1W2P775
Organism: Mus musculus/domesticus
Length: 712  
Fragment?: true
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Protein Coding Gene
MGI:106613 | Dvl2
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:108476 | Fzd3
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:99260 | Prkci
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:2135608 | Pard3
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1926212 | Med12
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
A0A1D5RMB5
Organism: Mus musculus/domesticus
Length: 1576  
Fragment?: false
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Protein
A0A0R4J055
Organism: Mus musculus/domesticus
Length: 1580  
Fragment?: false
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Protein
A0A2X0SFE3
Organism: Mus musculus/domesticus
Length: 915  
Fragment?: true
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Protein
Q3UVX2
Organism: Mus musculus/domesticus
Length: 622  
Fragment?: false
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Protein
E9Q1R7
Organism: Mus musculus/domesticus
Length: 622  
Fragment?: false
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Protein
Q6PF84
Organism: Mus musculus/domesticus
Length: 738  
Fragment?: false
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Publication
19536138 | -
First Author: Mao Y
Year: 2009
Journal: EMBO J
Title: A PH domain within OCRL bridges clathrin-mediated membrane trafficking to phosphoinositide metabolism.
Volume: 28
Issue: 13
Pages: 1831-42
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Protein
Q6PAJ3
Organism: Mus musculus/domesticus
Length: 880  
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.

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