|  Help  |  About  |  Contact Us

Search our database by keyword

Examples

  • Search this entire website. Enter identifiers, names or keywords for genes, diseases, strains, ontology terms, etc. (e.g. Pax6, Parkinson, ataxia)
  • Use OR to search for either of two terms (e.g. OR mus) or quotation marks to search for phrases (e.g. "dna binding").
  • Boolean search syntax is supported: e.g. Balb* for partial matches or mus AND NOT embryo to exclude a term

Search results 2901 to 3000 out of 4514 for Cdc42

<< First    < Previous  |  Next >    Last >>
0.018s

Categories

Hits by Pathway

Hits by Category

Hits by Strain

Type Details Score
Protein Coding Gene
MGI:102704 | Gng3
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGI:104581 | Gnb4
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGI:109164 | Gng5
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGI:1336169 | Gng10
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGI:95781 | Gnb1
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGI:95784 | Gnb2
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGI:109165 | Gngt1
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGI:1913316 | Gng11
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGI:1336171 | Gng12
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGI:95785 | Gnb3
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGI:109163 | Gng8
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGI:1098772 | Pik3r2
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGI:101848 | Gnb5
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein
P62881
Organism: Mus musculus/domesticus
Length: 395  
Fragment?: false
•
•
•
•
•
Protein
Q61017
Organism: Mus musculus/domesticus
Length: 69  
Fragment?: false
•
•
•
•
•
Protein
P62880
Organism: Mus musculus/domesticus
Length: 340  
Fragment?: false
•
•
•
•
•
Protein
Q61011
Organism: Mus musculus/domesticus
Length: 340  
Fragment?: false
•
•
•
•
•
Protein
P29387
Organism: Mus musculus/domesticus
Length: 340  
Fragment?: false
•
•
•
•
•
Protein
Q9DAS9
Organism: Mus musculus/domesticus
Length: 72  
Fragment?: false
•
•
•
•
•
Protein
Q9JMF3
Organism: Mus musculus/domesticus
Length: 67  
Fragment?: false
•
•
•
•
•
Protein
Q9CXP8
Organism: Mus musculus/domesticus
Length: 68  
Fragment?: false
•
•
•
•
•
Protein
Q61012
Organism: Mus musculus/domesticus
Length: 74  
Fragment?: false
•
•
•
•
•
Protein
P63213
Organism: Mus musculus/domesticus
Length: 71  
Fragment?: false
•
•
•
•
•
Protein
P63216
Organism: Mus musculus/domesticus
Length: 75  
Fragment?: false
•
•
•
•
•
Protein
P50153
Organism: Mus musculus/domesticus
Length: 75  
Fragment?: false
•
•
•
•
•
Protein
Q80SZ7
Organism: Mus musculus/domesticus
Length: 68  
Fragment?: false
•
•
•
•
•
Protein
Q61016
Organism: Mus musculus/domesticus
Length: 68  
Fragment?: false
•
•
•
•
•
Protein
P63078
Organism: Mus musculus/domesticus
Length: 70  
Fragment?: false
•
•
•
•
•
Protein
P62874
Organism: Mus musculus/domesticus
Length: 340  
Fragment?: false
•
•
•
•
•
Protein
O08908
Organism: Mus musculus/domesticus
Length: 722  
Fragment?: false
•
•
•
•
•
Protein
P61953
Organism: Mus musculus/domesticus
Length: 73  
Fragment?: false
•
•
•
•
•
Publication
15848799 | J:98309
First Author: Sahin M
Year: 2005
Journal: Neuron
Title: Eph-dependent tyrosine phosphorylation of ephexin1 modulates growth cone collapse.
Volume: 46
Issue: 2
Pages: 191-204
•
•
•
•
•
Publication
11274158 | -
First Author: Routhier EL
Year: 2001
Journal: J Biol Chem
Title: Human BIN3 complements the F-actin localization defects caused by loss of Hob3p, the fission yeast homolog of Rvs161p.
Volume: 276
Issue: 24
Pages: 21670-7
•
•
•
•
•
Publication
11163259 | J:66505
First Author: Sasaki S
Year: 2000
Journal: Neuron
Title: A LIS1/NUDEL/cytoplasmic dynein heavy chain complex in the developing and adult nervous system.
Volume: 28
Issue: 3
Pages: 681-96
•
•
•
•
•
Publication
15147912 | -
First Author: Sakakibara T
Year: 2004
Journal: FEBS Lett
Title: Identification and characterization of a novel Rho GTPase activating protein implicated in receptor-mediated endocytosis.
Volume: 566
Issue: 1-3
Pages: 294-300
•
•
•
•
•
Protein
A0A2I3BRI9
Organism: Mus musculus/domesticus
Length: 142  
Fragment?: true
•
•
•
•
•
Protein
A0A1D5RLD3
Organism: Mus musculus/domesticus
Length: 331  
Fragment?: false
•
•
•
•
•
Protein
E9Q6V8
Organism: Mus musculus/domesticus
Length: 91  
Fragment?: true
•
•
•
•
•
Protein
H3BL84
Organism: Mus musculus/domesticus
Length: 91  
Fragment?: true
•
•
•
•
•
Publication
11331876 | -
First Author: Martinez-Quiles N
Year: 2001
Journal: Nat Cell Biol
Title: WIP regulates N-WASP-mediated actin polymerization and filopodium formation.
Volume: 3
Issue: 5
Pages: 484-91
•
•
•
•
•
Publication
11687573 | J:73645
First Author: Vetterkind S
Year: 2002
Journal: J Biol Chem
Title: The rat homologue of Wiskott-Aldrich syndrome protein (WASP)-interacting protein (WIP) associates with actin filaments, recruits N-WASP from the nucleus, and mediates mobilization of actin from stress fibers in favor of filopodia formation.
Volume: 277
Issue: 1
Pages: 87-95
•
•
•
•
•
Publication
17949983 | -
First Author: Antón IM
Year: 2007
Journal: Trends Cell Biol
Title: WASP-interacting protein (WIP): working in polymerisation and much more.
Volume: 17
Issue: 11
Pages: 555-62
•
•
•
•
•
Publication
16141245 | J:106360
First Author: Gallego MD
Year: 2006
Journal: Int Immunol
Title: WIP and WASP play complementary roles in T cell homing and chemotaxis to SDF-1alpha.
Volume: 18
Issue: 2
Pages: 221-32
•
•
•
•
•
Publication
16709815 | -
First Author: Tsuboi S
Year: 2006
Journal: J Immunol
Title: A complex of Wiskott-Aldrich syndrome protein with mammalian verprolins plays an important role in monocyte chemotaxis.
Volume: 176
Issue: 11
Pages: 6576-85
•
•
•
•
•
Publication
16546573 | -
First Author: Antón IM
Year: 2006
Journal: Eur J Cell Biol
Title: WIP: a multifunctional protein involved in actin cytoskeleton regulation.
Volume: 85
Issue: 3-4
Pages: 295-304
•
•
•
•
•
Publication
12504004 | -
First Author: Sasahara Y
Year: 2002
Journal: Mol Cell
Title: Mechanism of recruitment of WASP to the immunological synapse and of its activation following TCR ligation.
Volume: 10
Issue: 6
Pages: 1269-81
•
•
•
•
•
Publication
11869681 | J:74719
First Author: Antón IM
Year: 2002
Journal: Immunity
Title: WIP deficiency reveals a differential role for WIP and the actin cytoskeleton in T and B cell activation.
Volume: 16
Issue: 2
Pages: 193-204
•
•
•
•
•
Publication
22231303 | -
First Author: Lanzi G
Year: 2012
Journal: J Exp Med
Title: A novel primary human immunodeficiency due to deficiency in the WASP-interacting protein WIP.
Volume: 209
Issue: 1
Pages: 29-34
•
•
•
•
•
Publication
23896986 | J:238622
First Author: Huang LY
Year: 2013
Journal: Cell Res
Title: Deficiency of IRTKS as an adaptor of insulin receptor leads to insulin resistance.
Volume: 23
Issue: 11
Pages: 1310-21
•
•
•
•
•
Publication
21282465 | J:171006
First Author: Zyłkiewicz E
Year: 2011
Journal: J Cell Biol
Title: The N-terminal coiled-coil of Ndel1 is a regulated scaffold that recruits LIS1 to dynein.
Volume: 192
Issue: 3
Pages: 433-45
•
•
•
•
•
Publication
21036906 | -
First Author: Torisawa T
Year: 2011
Journal: J Biol Chem
Title: Functional dissection of LIS1 and NDEL1 towards understanding the molecular mechanisms of cytoplasmic dynein regulation.
Volume: 286
Issue: 3
Pages: 1959-65
•
•
•
•
•
Publication
17060449 | J:117672
First Author: Mori D
Year: 2007
Journal: Mol Cell Biol
Title: NDEL1 phosphorylation by Aurora-A kinase is essential for centrosomal maturation, separation, and TACC3 recruitment.
Volume: 27
Issue: 1
Pages: 352-67
•
•
•
•
•
Publication
11950587 | -
First Author: Jaffer ZM
Year: 2002
Journal: Int J Biochem Cell Biol
Title: p21-activated kinases: three more join the Pak.
Volume: 34
Issue: 7
Pages: 713-7
•
•
•
•
•
Publication
15581714 | -
 
First Author: van Galen EJ
Year: 2005
Journal: Prog Brain Res
Title: Rho proteins, mental retardation and the neurobiological basis of intelligence.
Volume: 147
Pages: 295-317
•
•
•
•
•
Publication
18523455 | -
First Author: Rejeb I
Year: 2008
Journal: Eur J Hum Genet
Title: A novel splice mutation in PAK3 gene underlying mental retardation with neuropsychiatric features.
Volume: 16
Issue: 11
Pages: 1358-63
•
•
•
•
•
Publication
18507705 | J:138645
First Author: Kreis P
Year: 2008
Journal: J Neurochem
Title: The four mammalian splice variants encoded by the p21-activated kinase 3 gene have different biological properties.
Volume: 106
Issue: 3
Pages: 1184-97
•
•
•
•
•
Publication
21949127 | -
First Author: Thévenot E
Year: 2011
Journal: J Biol Chem
Title: p21-Activated kinase 3 (PAK3) protein regulates synaptic transmission through its interaction with the Nck2/Grb4 protein adaptor.
Volume: 286
Issue: 46
Pages: 40044-59
•
•
•
•
•
Publication
18675265 | J:141962
First Author: Nekrasova T
Year: 2008
Journal: Dev Biol
Title: Targeted disruption of the Pak5 and Pak6 genes in mice leads to deficits in learning and locomotion.
Volume: 322
Issue: 1
Pages: 95-108
•
•
•
•
•
Publication
18642328 | -
First Author: Kaur R
Year: 2008
Journal: Prostate
Title: Increased PAK6 expression in prostate cancer and identification of PAK6 associated proteins.
Volume: 68
Issue: 14
Pages: 1510-6
•
•
•
•
•
Publication
15550393 | -
First Author: Kaur R
Year: 2005
Journal: J Biol Chem
Title: Activation of p21-activated kinase 6 by MAP kinase kinase 6 and p38 MAP kinase.
Volume: 280
Issue: 5
Pages: 3323-30
•
•
•
•
•
Publication
25855792 | -
First Author: Ha BH
Year: 2015
Journal: J Biol Chem
Title: Signaling, Regulation, and Specificity of the Type II p21-activated Kinases.
Volume: 290
Issue: 21
Pages: 12975-83
•
•
•
•
•
Publication
18954304 | -
First Author: Eberth A
Year: 2009
Journal: Biochem J
Title: A BAR domain-mediated autoinhibitory mechanism for RhoGAPs of the GRAF family.
Volume: 417
Issue: 1
Pages: 371-7
•
•
•
•
•
Publication
19249276 | -
First Author: Frank CA
Year: 2009
Journal: Neuron
Title: A presynaptic homeostatic signaling system composed of the Eph receptor, ephexin, Cdc42, and CaV2.1 calcium channels.
Volume: 61
Issue: 4
Pages: 556-69
•
•
•
•
•
Publication
20152127 | J:167656
First Author: Shi L
Year: 2010
Journal: Neuron
Title: Ephexin1 is required for structural maturation and neurotransmission at the neuromuscular junction.
Volume: 65
Issue: 2
Pages: 204-16
•
•
•
•
•
Publication
22467852 | -
First Author: Coutinho-Budd J
Year: 2012
Journal: J Cell Sci
Title: The F-BAR domains from srGAP1, srGAP2 and srGAP3 regulate membrane deformation differently.
Volume: 125
Issue: Pt 14
Pages: 3390-401
•
•
•
•
•
Publication
22159416 | -
First Author: Endris V
Year: 2011
Journal: J Cell Sci
Title: SrGAP3 interacts with lamellipodin at the cell membrane and regulates Rac-dependent cellular protrusions.
Volume: 124
Issue: Pt 23
Pages: 3941-55
•
•
•
•
•
Publication
18489790 | -
 
First Author: Fujimoto M
Year: 2008
Journal: BMC Med Genet
Title: Immunological profile in a family with nephrogenic diabetes insipidus with a novel 11 kb deletion in AVPR2 and ARHGAP4 genes.
Volume: 9
Pages: 42
•
•
•
•
•
Publication
12414125 | -
First Author: Foletta VC
Year: 2002
Journal: Brain Res Mol Brain Res
Title: Cloning of rat ARHGAP4/C1, a RhoGAP family member expressed in the nervous system that colocalizes with the Golgi complex and microtubules.
Volume: 107
Issue: 1
Pages: 65-79
•
•
•
•
•
Publication
16101281 | -
First Author: Mott HR
Year: 2005
Journal: Biochemistry
Title: Structural analysis of the SH3 domain of beta-PIX and its interaction with alpha-p21 activated kinase (PAK).
Volume: 44
Issue: 33
Pages: 10977-83
•
•
•
•
•
Publication
16527308 | -
First Author: Hoelz A
Year: 2006
Journal: J Mol Biol
Title: Crystal structure of the SH3 domain of betaPIX in complex with a high affinity peptide from PAK2.
Volume: 358
Issue: 2
Pages: 509-22
•
•
•
•
•
Publication
11481676 | -
First Author: Breton AM
Year: 2001
Journal: Yeast
Title: The yeast Rvs161 and Rvs167 proteins are involved in secretory vesicles targeting the plasma membrane and in cell integrity.
Volume: 18
Issue: 11
Pages: 1053-68
•
•
•
•
•
Publication
16394103 | -
First Author: Friesen H
Year: 2006
Journal: Mol Biol Cell
Title: Characterization of the yeast amphiphysins Rvs161p and Rvs167p reveals roles for the Rvs heterodimer in vivo.
Volume: 17
Issue: 3
Pages: 1306-21
•
•
•
•
•
Publication
19840940 | -
First Author: Yi SJ
Year: 2009
Journal: J Biol Chem
Title: Transglutaminase 2 regulates the GTPase-activating activity of Bcr.
Volume: 284
Issue: 51
Pages: 35645-51
•
•
•
•
•
Publication
21310073 | -
 
First Author: Yi SJ
Year: 2011
Journal: BMC Biochem
Title: Bcr is a substrate for Transglutaminase 2 cross-linking activity.
Volume: 12
Pages: 8
•
•
•
•
•
Publication
21295482 | -
First Author: Vaughan EM
Year: 2011
Journal: Curr Biol
Title: Control of local Rho GTPase crosstalk by Abr.
Volume: 21
Issue: 4
Pages: 270-7
•
•
•
•
•
Publication
9376659 | -
First Author: Groffen J
Year: 1997
Journal: Baillieres Clin Haematol
Title: The chimeric BCR-ABL gene.
Volume: 10
Issue: 2
Pages: 187-201
•
•
•
•
•
Publication
8246975 | -
First Author: McWhirter JR
Year: 1993
Journal: Mol Cell Biol
Title: A coiled-coil oligomerization domain of Bcr is essential for the transforming function of Bcr-Abl oncoproteins.
Volume: 13
Issue: 12
Pages: 7587-95
•
•
•
•
•
Publication
19555689 | -
First Author: Arnaud C
Year: 2009
Journal: FEBS Lett
Title: MCC, a new interacting protein for Scrib, is required for cell migration in epithelial cells.
Volume: 583
Issue: 14
Pages: 2326-32
•
•
•
•
•
Publication
18591935 | -
First Author: Fukuyama R
Year: 2008
Journal: Oncogene
Title: Mutated in colorectal cancer, a putative tumor suppressor for serrated colorectal cancer, selectively represses beta-catenin-dependent transcription.
Volume: 27
Issue: 46
Pages: 6044-55
•
•
•
•
•
Publication
22480440 | -
First Author: Pangon L
Year: 2012
Journal: Biochim Biophys Acta
Title: The PDZ-binding motif of MCC is phosphorylated at position -1 and controls lamellipodia formation in colon epithelial cells.
Volume: 1823
Issue: 6
Pages: 1058-67
•
•
•
•
•
Publication
24824780 | -
First Author: Pangon L
Year: 2015
Journal: Int J Cancer
Title: MCC inhibits beta-catenin transcriptional activity by sequestering DBC1 in the cytoplasm.
Volume: 136
Issue: 1
Pages: 55-64
•
•
•
•
•
Publication
30817801 | J:273736
First Author: Charron Y
Year: 2019
Journal: PLoS Genet
Title: Two isoforms of the RAC-specific guanine nucleotide exchange factor TIAM2 act oppositely on transmission ratio distortion by the mouse t-haplotype.
Volume: 15
Issue: 2
Pages: e1007964
•
•
•
•
•
Publication
8999801 | -
First Author: Sone M
Year: 1997
Journal: Science
Title: Still life, a protein in synaptic terminals of Drosophila homologous to GDP-GTP exchangers.
Volume: 275
Issue: 5299
Pages: 543-7
•
•
•
•
•
Publication
21192692 | -
First Author: Shepherd TR
Year: 2011
Journal: Biochemistry
Title: Distinct ligand specificity of the Tiam1 and Tiam2 PDZ domains.
Volume: 50
Issue: 8
Pages: 1296-308
•
•
•
•
•
Publication
29844364 | J:262990
First Author: Woroniuk A
Year: 2018
Journal: Nat Commun
Title: STEF/TIAM2-mediated Rac1 activity at the nuclear envelope regulates the perinuclear actin cap.
Volume: 9
Issue: 1
Pages: 2124
•
•
•
•
•
Publication
24377522 | -
First Author: Zhao ZY
Year: 2013
Journal: Asian Pac J Cancer Prev
Title: TIAM2 enhances non-small cell lung cancer cell invasion and motility.
Volume: 14
Issue: 11
Pages: 6305-9
•
•
•
•
•
Publication
21469146 | -
First Author: Chen JS
Year: 2012
Journal: Int J Cancer
Title: Expression of T-cell lymphoma invasion and metastasis 2 (TIAM2) promotes proliferation and invasion of liver cancer.
Volume: 130
Issue: 6
Pages: 1302-13
•
•
•
•
•
Publication
18829452 | -
First Author: Lammers M
Year: 2008
Journal: J Biol Chem
Title: Specificity of interactions between mDia isoforms and Rho proteins.
Volume: 283
Issue: 50
Pages: 35236-46
•
•
•
•
•
Protein Domain
IPR037429 | Rvs161/Hob3_BAR
Type: Domain
Description: BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions []. This entry represents the BAR domain found in fungal proteins with similarity to Saccharomyces cerevisiae Reduced viability upon starvation protein 161 (Rvs161p) and Schizosaccharomyces pombe Hob3 (homologue of Bin3). S. cerevisiae Rvs161p plays a role in regulating cell polarity, actin cytoskeleton polarization, vesicle trafficking, endocytosis, bud formation, and the mating response. It forms a heterodimer with another BAR domain protein Rvs167p. Rvs161p and Rvs167p share common functions but are not interchangeable [, ]. Their BAR domains cannot be replaced with each other and the overexpression of one cannot suppress the mutant phenotypes of the other. S. pombe Hob3 is important in regulating filamentous actin localization and may be required in activating Cdc42 and recruiting it to cell division sites []. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions [].
•
•
•
•
•
Protein Domain
IPR043537 | Tiam1/Tiam2/Sif
Type: Family
Description: T-lymphoma invasion and metastasis-inducing protein 1 (Tiam1) is a guanine exchange factor (GEF) for CDC42 and the Rho-family GTPase Rac1, which plays an important role in cell-matrix adhesion and in cell migration [, ]. Tiam1 is involved in multiple steps of tumorigenesis [].Tiam2 has been shown to localise to the nuclear envelope and to regulate Rac1 activity at the nuclear envelope which regulates the perinuclear actin cap []. It has been shown to promote invasion and motility of non-small cell lung cancer cells []. It has also been shown to promote epithelial-to-mesenchymal transition and results in proliferation and invasion in liver cancer cells []. This entry includes a group of guanine nucleotide exchange factors, including Tiam1/2 from humans and Sif from Drosophila [, , ]. Tiam1/2 are activators of the Rho GTPase Rac1 and critical for cell morphology, adhesion, migration, and polarity [].
•
•
•
•
•
Protein Domain
IPR028295 | WIP
Type: Family
Description: WAS/WASL-interacting protein family member 1 (WIPF1, also known as WIP) is involved in a wide variety of cellular functions,including cellular signalling, endocytosis and actin cytoskeletonremodelling []. It binds to and stabilises N-WASP and WASP []. WIP and WASP can form a complex, which plays an important role in Arp2/3-mediated actin polymerisation and is regulated by Cdc42 (a small GTPase of the Rho family) [, ]. WIP can also participates in the reorganisation of the actin-based cytoskeleton and stabilises actin filaments in a WASP-independent manner []. In blood cells, WIP participates in conveying WASP to areas of active actin assembly following antigen-receptor and chemokinereceptor signalling [, , , ]. WIP deficiency is linked to Wiskott-Aldrich syndrome 2, which is an immunodeficiency disorder characterised by eczema, thrombocytopenia, recurrent infections, defective T-cell proliferation, and impaired natural killer cell function [].
•
•
•
•
•
Protein Domain
IPR026796 | DOCK9
Type: Family
Description: DOCK family members are evolutionarily conserved guanine nucleotide exchange factors (GEFs) for Rho-family GTPases []. DOCK proteins are required during several cellular processes, such as cell motility and phagocytosis. The N-terminal SH3 domain of the DOCK proteins functions as an inhibitor of GEF, which can be relieved upon its binding to the ELMO1-3 adaptor proteins, after their binding to active RhoG at the plasma membrane [, ]. DOCK family proteins are categorised into four subfamilies based on their sequence homology: DOCK-A subfamily (DOCK1/180, 2, 5), DOCK-B subfamily (DOCK3, 4), DOCK-C subfamily (DOCK6, 7, 8), DOCK-D subfamily (DOCK9, 10, 11) []. This entry represents DOCK9 (also known as Zizimin). DOCK9 and DOCK11 activate Cdc42 [, ].
•
•
•
•
•
Protein Domain
IPR035063 | STK_PAK3
Type: Domain
Description: This entry represents the catalytic domain of serine/threonine kinase p21-activated kinase (PAK) 3.PAK3 is highly expressed in the brain. It is implicated in neuronal plasticity, synapse formation, dendritic spine morphogenesis, cell cycle progression, neuronal migration, and apoptosis [, ]. Inactivating mutations in the PAK3 gene cause X-linked non-syndromic mental retardation, the severity of which depends on the site of the mutation [, ]. PAK3 belongs to the group I PAKs.Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac [].
•
•
•
•
•
Protein Domain
IPR035064 | STK_PAK2
Type: Domain
Description: PAK2 plays a role in pro-apoptotic signaling. It is cleaved and activated by caspases leading to morphological changes during apoptosis []. PAK2 is also activated in response to a variety of stresses including DNA damage, hyperosmolarity, serum starvation, and contact inhibition, and may play a role in coordinating the stress response []. PAK2 also contributes to cancer cell invasion through a mechanism distinct fromthat of PAK1 []. PAK2 belongs to the group I PAKs.Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac [].This entry corresponds to the PAK2 C-terminal catalytic domain.
•
•
•
•
•
Protein Domain
IPR010473 | GTPase-bd
Type: Domain
Description: Diaphanous-related formins (Drfs) are a family of formin homology (FH) proteins that act as effectors of Rho small GTPases during growth factor-induced cytoskeletal remodelling, stress fibre formation, and cell division []. Drf proteins are characterised by a variety of shared domains: an N-terminal GTPase-binding domain (GBD), formin-homology domains FH1, FH2 () and FH3 (), and a C-terminal conserved Dia-autoregulatory domain (DAD) that binds the GBD.This entry represents the GBD, which is a bifunctional autoinhibitory domain that interacts with and is regulated by activated Rho family members. Mammalian Drf3 contains a CRIB-like motif within its GBD for binding to Cdc42, which is required for Cdc42 to activate and guide Drf3 towards the cell cortex where it remodels the actin skeleton [].
•
•
•
•
•
Protein Domain
IPR042139 | PX_ARHGAP32
Type: Domain
Description: This entry represents the PX domain found in Rho GTPase-activating protein 32 (ARHGAP32, also known as RICS). RICS is a Rho GTPase-activating protein for cdc42 and Rac1. It is implicated in the regulation of postsynaptic signaling and neurite outgrowth. An N-terminal splicing variant of RICS containing additional PX and Src Homology 3 (SH3) domains, also called PX-RICS, is the main isoform expressed during neural development. PX-RICS is involved in neural functions including axon and dendrite extension, postnatal remodeling, and fine-tuning of neural circuits during early brain development []. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction []. The PX domain of PX-RICS specifically binds phosphatidylinositol 3-phosphate (PI3P), PI4P, and PI5P [].
•
•
•
•
•
Protein Domain
IPR030060 | IRTKS
Type: Family
Description: IRTKS (insulin receptor tyrosine kinase substrate; brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 1 or BAIAP2L1) is an I-BAR (Bin/amphipysin/Rvs) domain containing protein. I-BAR domain is a type of the BAR domain, which 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 [].IRTKS binds small GTPase Rac rather than Cdc42 []. It serves as an adaptor of the insulin receptor (IR), modulates IR-IRS1-PI3K-AKT signalling via regulating the phosphorylation of IR []. It has been linked to the formation of actin-rich membrane protrusions, called pedestals, during the infection process of enterohemorrhagic Escherichia coli [].
•
•
•
•
•
Protein Domain
IPR044933 | DIA_GBD_sf
Type: Homologous_superfamily
Description: This superfamily contains the N-terminal domain of diaphanous, a subclass of formins whose members are regulated by the binding of a small GTP-binding protein of the Rho subfamily. These proteins are characterised by a variety of shared domains: an N-terminal GTPase-binding domain (GBD), formin-homology domains FH1, FH2 and FH3, and a C-terminal conserved Dia-autoregulatory domain (DAD) that binds the GBD. This N-terminal domain corresponds to the GBD, a bifunctional autoinhibitory domain that interacts with and is regulated by activated Rho family members. Mammalian Drf3 contains a CRIB-like motif within its GBD for binding to Cdc42, which is required for Cdc42 to activate and guide Drf3 towards the cell cortex where it remodels the actin skeleton [, ].
•
•
•
•
•
Protein Domain
IPR040171 | USBP1-like
Type: Family
Description: This entry includes Harmonin-binding protein USHBP1 also known as MCC2) and colorectal mutant cancer protein known as MCC. MCC has been found to suppresses cell proliferation and the Wnt/b-catenin pathway in colorectal cancer cells [, ]. It may works as a scaffold protein regulating cell movement and able to bind Scrib, beta-catenin and NHERF1/2 []. MCC1 inhibits DNA binding of b-catenin/TCF/LEF transcription factors, and it is involved in cell migration independently of RAC1, CDC42 and p21-activated kinase (PAK) activation [, , ].MCC2 protein binds the first PDZ domain of AIE-75 with its C-terminal amino acids -DTFL. A possible role of MCC2 as a tumour suppressor has been put forward. The carboxyl terminus of the predicted protein was DTFL which matched the consensus motif X-S/T-X-phi (phi: hydrophobic amino acid residue) for binding to the PDZ domain of AIE-75 [, ].
•
•
•
•
•
Protein Domain
IPR015767 | ARHGAP27
Type: Family
Description: Members of Rho family are small G proteins that transduce signals from plasma-membrane receptors and control cell adhesion, motility and shape by actin cytoskeleton formation. Like all other GTPases, Rho proteins act as molecular switches, with an active GTP-bound form and an inactive GDP-bound form. The active conformation is promoted by guanine-nucleotide exchange factors, and the inactive state by GTPase-activating proteins (GAPs), which stimulate the intrinsic GTPase activity of small G proteins.This entry represents Rho GTPase activating protein 27 (ARHGAP27, also known as CIN85-associated multi-domain-containing Rho GTPase-activating protein 1, CAMGAP1), a binding protein for Cbl-interacting protein of 85kDa (CIN85), an adaptor protein involved in the endocytic process of several receptor tyrosine kinases. It also has activity towards Rac1 and Cdc42 [].
•
•
•
•
•




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