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Hersteller INFOS

Antibodies to GTPase Regulators

Info

Regulatory GTPases have a common mechanism that enables them to switch a signal transduction chain on and off.
When a cell receives extracellular signals it may need to activate or turn on a number of downstream signaling pathways in order to initiate a particular cellular response. The downstream signals activated by growth factors, cytokines, hormones, cell-cell interactions, or physical stress can be complex and result in the modification of a number of cellular processes. These far reaching and complex effects can be achieved via a simple biochemical concept that involves proteins that function as pivotal molecular switches and interact with a multitude of effectors to turn on or turn off particular sets of responses.

The molecular switches are G-proteins, GTPases that hydrolyze GTP and cycle between two conformational states depending on whether GTP (guanine triphosphate) or GDP (guanine diphosphate) is bound. The GTP-bound GTPase is active, while the GDP-bound is inactive. In its active GTP-bound state, GTPases recognize and interact with target effectors that propagate downstream signals. Regulation of GTPase activity is achieved via activators called GEFs (guanine-nucleotide exchange factors) and inactivators called GAPs (GTPase-activating proteins). GEFs transduce signals from receptor tyrosine kinases, G-protein-coupled receptors, adhesion molecules, and second messengers and promote GTP binding to GTPases. GTP binding and signaling to target effectors is in turn terminated by the hydrolysis of GTP to GDP facilitated by GAPs. A third class of GTPase regulators, the GDIs (G-nucleotide dissociation inhibitors), also exists. GDIs are specific regulators of the Rho/Rac and Rab families of monomeric GTPases. GDIs influence G-protein signaling by binding the GDP or GTP form of the GTPase and preventing dissociation of the nucleotide.

It is apparent that the regulation of GTPase signaling is highly and carefully regulated. Hundreds of GTPase regulators have been identified and the G-protein signaling system is conserved well through evolution. The involvement of G-protein signaling in a wide variety of cellular activities has resulted in the study GTPases and their regulators as therapeutic targets in a number of human diseases.

Detection of Human and Mouse BIG1/ARFGEF1 by Western Blot (h&m) and Immunoprecipitation (h).

Samples: Whole cell lysate from HeLa (5, 15 and 50 mcg for WB; 1 mg for IP, 20% of IP loaded), 293T (T; 50 mcg) and mouse NIH3T3 (M; 50 mcg) cells. Antibody: Affinity purified rabbit anti-BIG1/ARFGEF1 antibody (Cat. No. A300-998A) used for Western Blot at 0.1 mcg/ml (A) and at 1 mcg/ml (B) and used for Immunoprecipitation at 3 mcg/mg lysate (B). For blotting immunoprecipitated BIG1/ARFGEF1, ReliaBLOT® Reagents and Procedures (Cat. No. WB120) were used. Detection: Chemiluminescence with exposure times of 3 minutes (A) and 30 seconds (B).

Detection of Human PDZ-RhoGEF by Western Blot and Immunoprecipitation.

Samples: Whole cell lysate (5, 15 and 50 mcg for WB; 1 mg for IP, 20% of IP loaded) from HeLa cells. Antibodies: Affinity purified rabbit anti-PDZ-RhoGEF antibody (Cat. No. A301-952A) used for WB at 0.04 mcg/ml (A) and 1 mcg/ml (B) and used for IP at 3 mcg/mg lysate. PDZ-RhoGEF was also immunoprecipitated by rabbit anti-PDZ-RhoGEF antibody (Cat. No. A301-951A), which recognizes an upstream epitope. For blotting immunoprecipitated PDZ-RhoGEF, ReliaBLOT® Reagents and Procedures (Cat. No. WB120) were used. Detection: Chemiluminescence with exposure times of 30 seconds (A) and 10 seconds (B).

 

Product Links


 
Applications
 Antibodies  Western Blot  IHC  Immunoprecipitation
 AKAP13/AKAP-Lbc  A301-404A
 
  
 A301-403A
 A301-404A
 ArfGAP1  A302-029A    A302-029A
 ArfGAP2  A302-031A    A302-030A
 ArfGAP3  A302-032A    A302-032A
 ARHGEF5  A302-203A
 A302-204A
   A302-203A
 A302-204A
 ARHGEF16  A301-961A    A301-961A
 ASAP1  A302-117A
 A302-118A
  
 A302-117A
 A302-118A
 BCR  A302-057A
 
  
 A302-056A
 A302-057A
 BIG1/ARFGEF1  A300-998A   
 A300-998A
 BIG2/ARFGEF2  A301-004A    A301-004A
 BORG2      A301-722A
 A301-723A
 BRAF  A301-695A    A301-695A
 C3G  A301-964A
 A301-965A
   A301-964A
 A301-965A
 Cdc42GAP  A301-853A
 A301-854A
   A301-853A
 A301-854A
 CENTD2/ARAP1  A301-413A    A301-413A
 CENTG3  A302-172A   
 A302-171A
 A302-172A
 CSN1  A300-026A  IHC-00113
 DAB2IP  A302-439A
 A302-440A
   A302-439A
 A302-440A
 Diaphanous 1  A300-077A
 A300-078A
   
 Diaphanous 2   A300-079A    
 DOCK4  A302-263A
 
   A302-263A
 A302-264A
 DOCK9  A300-530A
 A300-532A
   A300-530A
 A300-531A
 DOCK10  A301-305A
 A301-306A
   A301-305A
 A301-306A
 DOCK11  
   A301-638A
 A301-639A
 DOCK180  A301-288A
   A301-287A
 A301-288A
 ECT2  A302-348A
   
 eEF2  A301-688A
 IHC-00330  
 EFTUD2/SNRP116  A300-957A
 IHC-00161  A300-957A
 eIF5  A301-771A
   
 eIF5B/IF2  A301-744A
 A301-745A
   A301-744A
 
 EVI5  A300-875A
   A300-874A
 A300-875A
 Filamin A  A301-133A
 A301-134A
 
A301-135A
 IHC-00225  A301-134A
 A301-135A
 G3BP1  A302-033A
 A302-034A
   A302-033A
 A302-034A
 G3BP2  A302-040A
   A302-040A
 A302-041A
 GAPex5  A302-115A
 A302-116A
   A302-115A
 A302-116A
 GBF1  A301-963A
   A301-962A
 A301-963A
 GEF-H1  A301-928A
   A301-929A
 A301-930A
 GRLF1/p190RhoGAP  A301-736A
   A301-736A
 HERC1      A301-903A
 A301-904A
 HERC2  A301-905A
   A301-905A
 LARG  A301-959A
 A301-960A
   A301-959A
 A301-960A
 NF1  A300-140A
   A300-140A 
 PARG1  A301-924A
   A301-923A
 A301-924A
 PDZ-GEF1  A301-966A    A301-966A
 PDZ-GEF2  A301-967A
 A301-968A
   A301-967A
 A301-968A
 PDZ-RhoGEF
 A301-952A
   A301-951A
 A301-952A
 PLEKHG2  A302-414A
 A302-415A
   A302-414A
 A302-415A
 Rab3-GAP1  A302-113A
 A302-114A
   A302-113A
 A302-114A
 RanBP1  A300-512A
   A300-512A
 A300-513A
 RanBP2  A301-796A
 A301-797A
   A301-796A
 A301-797A
 RanBP3  A301-520A
 IHC-00295  A301-520A
 RanBP8  A301-804A
   
 RanGAP1  A302-026A
   A302-026A
 A302-027A
 RASAL2  A302-109A
 
   A302-109A
 A302-108A
 RCC1  A300-866A
   A300-866A
 Sin1  A300-910A
 IHC-00183  A300-910A
 SIPA1  A302-028A
   A302-028A
 SOS1  A301-890A
   A301-889A
 A301-890A
 SOS2  A301-893A
   A301-893A
 SRGAP1/ARHGAP13  A301-286A
   A301-285A
 A301-286A
 TBC1D9/MDR1  A301-028A
   A301-027A
 A301-028A
 TIAM1  A300-099A
   
 TSC1  A300-316A
   A300-316A
 TSC2  A300-463A
   A300-463A
 A300-526A

Protein Information

 AKAP13/AKAP-Lbc AKAP13/AKAP-Lbc was originally identified as an oncogenic protein that associates with the GTP-binding protein Rho. AKAP13-Lbc is also a member of the A-kinase anchoring protein family that functions as a molecular scaffold for the subcellular compartmentalization of A- kinase signaling molecules. AKAP13-Lbc has been found to possess Rho-specific guanine nucleotide exchange factor (GEF) activity and is critical to mediating RhoA activation and signal transduction. Alternate names for AKAP13/AKAP-Lbc include A-kinase anchor protein 13, protein kinase A-anchoring protein, guanine nucleotide exchange factor Lbc, LBC oncogene, lymphoid blast crisis oncogene, BRX, HT31, LBC, c-lbc, HA-3, FLJ11952, and FLJ43341.
 ArfGAP1 ADP-ribosylation factor GTPase activating protein 1 (ArfGAP1) is a GTPase activating protein that interacts with the GTPase ADP-ribosylation factor (Arf) in Golgi membranes and vesicles. ArfGAP1 promotes the hydrolysis of ARF1-bound GTP to promote fusion of golgi-derived vesicles with the target compartment. Although they are differentially regulated, ArfGAP1, ArfGAP2, and ArfGAP3 have been shown to play overlapping roles in COPI-mediated transport and in the maintenance of Golgi organization.
 ArfGAP2 ADP-ribosylation factor GTPase activating protein 2 (ArfGAP2) is a GTPase activating protein that interacts with the GTPase ADP-ribosylation factor (Arf) in Golgi membranes and vesicles. Although they are differentially regulated, ArfGAP2 along with ArfGAP1 and ArfGAP3 has been shown to play an overlapping role in COPI-mediated transport and in the maintenance of Golgi organization. ArfGAP2 is also known as zinc finger protein 289 or ZNF289.
 ArfGAP3 ADP-ribosylation factor GTPase activating protein 3 (ArfGAP3) is a GTPase activating protein that interacts with the GTPase ADP-ribosylation factor (Arf) in Golgi membranes and vesicles. Although they are differentially regulated, ArfGAP3 along with ArfGAP1 and ArfGAP2 has been shown to play an overlapping role in COPI-mediated transport and in the maintenance of Golgi organization.
 ARHGEF5 ARHGEF5, also known as TIM (transforming immortalized mammary), is an oncogene that belongs to the Dbl family of guanine nucleotide exchange factors (GEFs) for Rho GTPases. It is implicated to play a role in proliferative breast disease Alternative names for ARHGEF5 include Rho guanine nucleotide exchange factor (GEF) 5, GEF5, P60, TIM1, and ARHGEF5.
 ARHGEF16 The gene for ARHGEF16 [Rho guanine exchange factor (GEF)16] was isolated as a candidate gene for human neuroblastoma. It is a member of the Rho/Rac GEF family of proteins which catalyze the exchange of GDP for GTP on the GTPases, Rho and Rac, to activate downstream signaling pathways. ARHGEF16 is also known as NBR.
 ASAP1 ASAP1 ( Arf-Gap with SH3 domain, ANK repeat and PH domain-containing protein 1) is an Arf (ADP-ribosylation factor) GAP (GTPase-activating protein) that catalyzes the hydrolysis of GTP bound to Arf, a small GTP-binding protein. As a regulator of Arf activity ASAP1 has been shown to regulate cell adhesion and migration, and to be involved in carcinogenesis. Structurally, ASAP1 bears two ankyrin repeats, one Arf-GAP domain, one PH domain, one SH3 domain, and an N-terminal Bin, Amphiphysin and Rvs167 (BAR) domain. Alternative names for ASAP1 include PIP2-dependent ARF1 GAP, ARF GTPase-activating protein 1, development and differentiation-enhancing factor 1, differentiation-enhancing factor 1, PAP, PAG2, AMAP1, ZG14P, CENTB4, DEF-1, DDEF1, and KIAA1249.
 BCR BCR (breakpoint cluster region) was identified as part of a fusion protein that results from a reciprocal translocation with the ABL gene between chromosomes 22 and 9. The BCR-ABL fusion is the cause of chronic myeloid leukemia (CML). The BCR protein contains a C2 domain, a DBL-homology domain, a PH domain, and a Rho-GAP domain and functions as a GTPase-activating protein for RAC1 and CDC42.
 BIG1/ARFGEF1 BIG1/ARFGEF1 is a brefeldin A-inhibited guanine nucleotide exchange protein (GEP) that activates ADP-ribosylation factor (ARF) GTPases and functions in vesicle formation from Golgi membranes. BIG1/ARFGEF1 is also known as brefeldin A-inhibited guanine nucleotide-exchange protein 1, Brefeldin A-inhibited GEP1, p200 ARF-GEP1, p200 ARF guanine nucleotide exchange factor, ARFGEP1, P200, DKFZP434L057, and D730028O18Rik.
 BIG2/ARFGEF2 BIG2/ARFGEF2 is a brefeldin A-inhibited guanine nucleotide exchange protein (GEP) that activates ADP-ribosylation factor (ARF) GTPases and functions in vesicle formation from Golgi membranes. BIG2/ARFGEF2 is also known as brefeldin A-inhibited guanine nucleotide-exchange protein 2, brefeldin A-inhibited GEP2, ARFGEP2, FLJ23723, and dJ1164I10.1.
 BORG2 BORG2 (binder of Rho GTPases 2) is a member of a family of proteins that bind the TC10 and Cdc42 GTPases in a GTP-dependent manner. BORG family members have been shown to play a role in the regulation of septin assembly and organization. Alternate names for BORG2 include Cdc42 effector protein 3, MSE55-related Cdc42-binding protein, CRIB-containing BORG2 protein, CDC42EP3, and CEP3.
 BRAF B-Raf proto-oncogene serine/threonine-protein kinase (BRAF) is a member of the raf/mil family of serine/threonine kinases. BRAF is involved in transducing mitogenic signals via the MAP kinase/ERKs signaling pathway. Mutations in BRAF are involved in a wide range of cancers such as lung, non-Hodgkin lymphoma, and colorectal cancer. Defects in BRAF are also the cause of cardiofaciocutaneous syndrome (CFC), an autosomal dominant syndrome characterized by facial anomalies, heart defects, and ectodermal abnormalities. Alternate names for BRAF include murine sarcoma viral (v-raf) oncogene homolog B1, 94 kDa B-raf protein, RAFB1, and B-RAF1.
 C3G CRK SH3-binding GNRP (C3G) is a guanine nucleotide exchange factor (GEF) that binds to the SH3 domain of CRK and GRB2/ASH and catalyzes the exchange of GDP for GTP on GTPases of the Ras family. C3G has been reported to be involved in signaling that mediates cell adhesion and migration. Alternative names for C3G include Rap guanine nucleotide exchange factor 1, guanine nucleotide-releasing factor 2, RAPGEF1, and GRF2.
 Cdc42GAP Cdc42 GTPase-activating protein (Cdc42GAP) is also known as p50RhoGAP and ARHGAP1. Cdc42GAP functions as a negative regulator of the Rho GTPase, Cdc42, by catalyzing the hydrolysis of GTP to GDP by Cdc42. Cdc42 activity is proposed to be involved in multiple cellular activities such as motility, survival, and genomic stability. Alternative names for Cdc42GAP include Rho GTPase-activating protein 1, Rho-type GTPase-activating protein 1, Rho-related small GTPase protein activator, RHOGAP, and RHOGAP1.
 CENTD2/ARAP1 CENTD2/ARAP1 is an adapter protein that functions as an Arf 1 and Rho GTPase-activation protein. CENTD2/ARAP1 associates with the Golgi and appears to play a role in cytoskeleton remodeling as well as membrane receptor recycling and trafficking. Alternate names for CENTD2/ARAP1 include centaurin-delta-2, cnt-d2, Arf-GAP Rho-Gap ankyrin repeat and pleckstrin homology domain-containing protein 1, and KIAA0782.
 CENTG3 CENTG3 (centaurin gamma-3) is a member of the centaurin Arf-GAP family of proteins. CENTG3 is also known as AGAP3, MR1 interacting protein, MRIP-1, CRAM-associated GTPase, and CRAG.
 CSN1 CSN1 is one of eight subunits (CSN1 to 8) of the highly conserved COP9 signalsome (CSN) complex originally identified as a regulator of light-mediated development in Arabidopsis. Characterization of CSN from yeast to mammals reveals a function as a modulator of signal transduction pathways involved in a variety of cellular and developmental processes. One of the major functions of the CSN is the regulation of protein degradation via intersection with the ubiquitin-proteasome pathway and regulation of E3-ubiquitin ligases. Alternate designations for CSN1 include COP9 signalsome complex subunit 1, signalsome subunit 1, SGN1, JAB1-containing signalsome subunit 1, G protein pathway suppressor 1, protein GPS1, protein MFH, GPS1, COPS1, and MGC71287.
 DAB2IP DAB2-interacting protein (DAB2IP) functions as a Ras GTPase-activating protein. Through its interaction with MAP3K5, it disrupts the association of MAP3K5 with the inhibitory 14-3-3 complex. DAB2IP also Mediates TNF/TRAF2-induced MAP3K5-JNK activation, while it inhibits CHUK-NF-kappa-B signaling. DAB2IP may act as a tumor suppressor gene. DAB2IP is also known as ASK-interacting protein 1, AIP1, and KIAA1743. [taken from the Universal Protein Resource (UniProt) www.uniprot.org/uniprot/Q5VWQ8]
 Diaphanous 1 Diaphanous 1 is a member of the formin family of proteins that is responsible for actin polymerization and nucleation activity and the formation of linear, unbranched actin cables and stress fibers. Diaphanous 1 is a target of the small GTPase, Rho, and couples Rho and Src tyrosine kinase during signaling and the regulation of actin dynamics. Diaphanous 1 has been linked to heritable nonsyndromic progressive hearing loss. Alternate names for diaphanous 1 include protein diaphanous homolog 1, diaphanous-related formin-1, DRF1, DIAPH1, DIAP1, DFNA1, LFHL1, hDIA1, and FLJ25265.
 Diaphanous 2  Diaphanous 2 is a member of the formin family of proteins that is responsible for actin polymerization and nucleation activity and the formation of linear, unbranched actin cables and stress fibers. Diaphanous 1 is a target of the small GTPase, Rho. RhoB and diaphanous 2 have been shown to interact on endosomes and control actin dynamics involved in vesicle trafficking. Alternate names for diaphanous 2 include protein diaphanous homolog 2, diaphanous-related formin-2, DRF2, DIAPH2, DIA, POF, POF2, DIA2, and FLJ11167.
 DOCK4 DOCK4 (dedicator of cytokinesis 4) is a member of the CDM gene family and functions as a guanine nucleotide exchange factor (GEF) for the Rac small GTPase. It has been found to play a role in regulating the development of dendrites and rac-dependent cell migration. As a regulator of Rac, DOCK4 participates in wnt signaling by acting as a scaffold and influencing beta-catenin stability. Alternative gene names for DOCK4 include FLJ34238 and KIAA0716.
 DOCK9 Dedicator of cytokinesis 9 (DOCK9) is a Rho-GTPase guanine-nucleotide exchange factor (GEF) that activates Rho by catalyzing the exchange of GDP for GTP. DOCK9 is responsible for activating Cdc42, a Rho family GTPase that is involved in cell polarity, gene expression, cell-cycle progression and cell-cell interactions. Alternate names for DOCK9 include Cdc42 guanine nucleotide exchange factor zizimin-1, ZIZ1, and KIAA1058.
 DOCK10 DOCK10 is a potential Rho-guanine nucleotide exchange factor (Rho-GEF) that may function to activate small GTPases such as Rac and Cdc42. It is a member of the CZH (CDM-zizimin homology) family of proteins that contain two highly conserved domains, CZH1 and CZH2. Alternate names for DOCK10 include dedicator of cytokinesis protein 10, zizimin-3, ZIZ3, DRIP2, and KIAA0694.
 DOCK11 DOCK11 (dedicator of cytokinesis 11) is also known as zizimin-2. It is a DOCK180-related guanine nucleotide exchange factor (GEF) for the small GTPase, Cdc42. As a GEF, DOCK11 functions to catalyze the dissociation of GDP from the GTPase. Dissociation of GDP allows an exchange for GTP and subsequent downstream signaling by the GTPase. Alternate names for DOCK11 include activated Cdc42-associated guanine nucleotide exchange factor, ACG, and ZIZ2.
 DOCK180 DOCK80 is a non-conventional Rho-guanine nucleotide exchange factor (Rho-GEF) that functions to activate the small GTPases Rac and Cdc42. It is a member of the CZH (CDM-zizimin homology) family of proteins that contain two highly conserved domains, CZH1 and CZH2. Dock180 functions to activate Rac and regulate cell adhesion, cell spreading, migration and phagocytosis. Alternate names for Dock180 include dedicator of cytokinesis protein 1, 180 kDa protein downstream of CRK, DOCK1, and ced5.
 ECT2 Epithelial cell-transforming sequence 2 (ECT2) is a transforming protein that is related to Rho-specific exchange factors and yeast cell cycle regulators. The expression of this gene is elevated with the onset of DNA synthesis and remains elevated during G2 and M phases. In situ hybridization analysis showed that expression is at a high level in cells undergoing mitosis in regenerating liver. Thus, this protein is expressed in a cell cycle-dependent manner during liver regeneration, and is thought to have an important role in the regulation of cytokinesis. Alternate names for ECT2 include FLJ10461 and MGC138291 [taken from NCBI GeneID:1894]
 eEF2 Eukaryotic translation elongation factor 2 (eEF2) is a non-ribosomal protein that mediates ribosomal translocation and catalyzes peptide elongation in the presence of GTP. eEF2 is a substrate of the eEF2 kinase. Phosphorylation of eEF2 in response to increased energy demand or reduction in supply inhibits eEF2 activity for the conservation of energy. Alternate names for eEF2 include polypeptidyl-tRNA translocase, EF-2, EEF2, and EF2.
 EFTUD2/SNRP116 The splicesome is the molecular machine responsible for catalyzing intron removal from pre-mRNA transcripts. The splicesome is composed of several small nuclear RNAs (snRNAs) complexed with their associated proteins [together termed snRNPs (small nuclear ribonucleoprotein)]. One of the major classes of snRNPs includes the U1, U2, U4, U5 and U6 snRNP. EFTUD2/SNRP116 is a component of the U5 snRNP. EFTUD2/SNRP116 is a GTPase that may play a role in disrupting U4/U6 helices prior to splicesome activation. Alternate names for EFTUD2/SNRP116 include 116 kDa U5 small nuclear ribonucleoprotein component, U5, snRNP-specific protein 116 kDa, U5-116 kDa, elongation factor Tu GTP-binding domain protein 2, hSNU114, KIAA0031, FLJ44695, and DKFZp686E24196.
 eIF5 Eukaryotic initiation factor 5 (eIF5) plays an important role in the assembly of the 43S pre-initiation complex. In this assembly, eIF5 interacts with eIF1 and eIF3 and binds the eIF2-GTP/Met-tRNA ternary complex along with the 40S ribosome subunit. eIF5 is also reported to form a complex with eIF2. This complex is suggested to serve as a cytoplasmic reservoir for eIF2 that restricts the guanine nucleotide exchange promoted by the eIF2 beta subunit for the initiation of translation.
 eIF5B/IF2 Eukaryotic initiation factor 5 subunit B (eIF5B) is the eukaryotic ortholog of the bacterial IF2 initiation factor. It is one of two essential GTPases required for translation initiation. eIF5B plays a role in facilitiating 60S and 40S ribosomal subunit joining to form the 80S ribosome in the final step of translation.
 EVI5 The EVI5 oncogene has been identified as a protein that is localized to the centrosome and mitotic spindle, and in association with the aurora B complex, facilitates cytokinesis. EVI5 also appears to prevent premature APC/C activation and mitotic progression by stabilizing the anaphase-promoting complex/cyclosome (APC/C) inhibitor, Emi1, as well as cyclin A. EVI5 has also been demonstrated to be a binding partner of the Rab11 GTPase that regulates intracellular transport and cytokinesis. Alternate names for EVI5 include ecotropic viral integration site 5 protein homolog, EV-I5, neuroblastoma stage 4S gene, and NB4S.
 Filamin A Filamin A is an actin-binding protein that crosslinks and promotes orthogonal branching of actin filaments and also functions to anchor transmembrane proteins and intracellular signaling proteins to the actin cytoskeleton. As a scaffolding protein, filamin A is able act as a link between cell membrane receptors and intracellular signaling proteins. Defects in Filamin A are associated with multiple human diseases characterized by abnormalities in bone and neurological development. Alternate names for Filamin A include filamin-A, alpha-filamin, filamin-1, endothelial actin-binding protein, actin-binding protein 280, ABP-280, nonmuscle filamin, FLNA, FLN, FLN1, FMD, MNS, OPD, ABPX, NHBP, OPD1, OPD2, and ABP-280.
 G3BP1 Ras-GAP SH3 domain binding protein (G3BP1) contains an RNA recognition motif (RRM) and an N-terminal nuclear transport factor 2-like (NTF2-like) domain. It was first identified in a screen for proteins that bind the SH3 domain of the Ras GTPase activating protein (RasGAP). It has been shown to function downstream of Ras and play a role in RNA metabolism, signal transduction, and proliferation. G3BP1 is primarily cytoplasmic but has also been localized to the nucleus. G3BP1 has been shown to be overexpressed in human cancers. Alternate names for G3BP1 include ATP-dependent DNA helicase VIII, and HDH-VIII.
 G3BP2 Ras-GAP SH3 domain binding protein (G3BP2) contains an RNA recognition motif (RRM) and an N-terminal nuclear transport factor 2-like (NTF2-like) domain. The G3BP family of proteins have been shown to function downstream of Ras and play a role in RNA metabolism, signal transduction, and proliferation.G3BP2 can interact with IkappaBalpha and IkappaBalpha/NFkappaB complexes. In this complex G3B2 is proposed to play a role in regulating the nucleocytoplasmic localization of NFkappaB as well as its activity.
 GAPex5 GAPex-5 was identified in a two-hybrid screen for interactors of CIP4 (Cdc42 interacting protein 4). GAPex-5 contains a Ras-GAP domain and a VPS9 (vacuolar sorting protein 9 (VPS9) domain. It functions as a GEF for RAB31 to influence GLUT4 trafficking. It has also been found to be involved in the trafficking and ubiquitination of EGFR. Alternate names for GAPex-5 include GTPase-activating protein and VPS9 domain-containing protein 1, Rab5-activating protein 6, GAPVD1, GAPEX5, RAP6, and KIAA1521.
 GBF1 GBF1 is a guanine nucleotide exchange factor (GEF) that promotes the exchange of GDP for GTP on ADP ribosylation factor 5(ARF5). GBF1 activity is inhibited by brefeldin, an antibiotic that interferes with protein transport. It has been show to be important to golgi assembly and the coordination of bidirectional transport. Due to these characteristics, GBF1 is also called Golgi-specific brefeldin A-resistance GEF 1.
 GEF-H1 GEF-H1 (guanine nucleotide exchange factor H1) is a microtubule regulated guanine nucleotide exchange factor for the RhoA GTPase. It catalyzes the exchange of GDP for GTP by Rho in response to microtubule destabilization. GEF-H1 has shown to be regulated during cytokinesis and plays a role in the cleavage furrow. Alternative names for GEF-H1 include Rho guanine nucleotide exchange factor 2, microtubule-regulated Rho-GEF, proliferating cell nucleolar antigen p40, ARHGEF2, LFP40, and KIAA0651.
 GRLF1/p190RhoGAP GRLF1 (glucocorticoid receptor DNA binding factor 1) was first identified as a factor that binds to the regulatory region of the human glucocorticoid receptor (GR) gene and represses GR transcription. Later, p190RhoGAP was identified as a protein that associates with p120RasGAP and through sequence comparison, p190RhoGAP and GRLF1 were determined to be one and the same. GRLF1/P190RhoGAP functions as a GTPase activating protein (GAP) for the Rho GTPase and plays an essential role in mediating cytoskeletal reorganization in response to growth factor signals. p190RhoGAP possesses an unusual GTP binding domain that may serve to regulate its GAP activity and the subsequent modulation of RhoGTPase activity. P190RhoGAP forms a significant complex with p120RasGAP. This association has been suggested to represent a method for the coordination of the Ras and Rho signaling pathways. Alternate names for GRLF/P190RhoGAP include Rho GAP p190A, p190-A, GRF1, MGC10745, and KIAA1722.
 HERC1 HERC1 (HECT domain and RCC1-like domain-containing protein 1) belongs to the HERC family of ubiquitin ligases. It is involved in membrane traffic via its ability to bind clathrin and its guanine nucleotide exchange factor (GEF) activity for Arf and Rab. HERC1 has been found to interact with TSC2 (tuberous sclerosis complex 2) and may be involved with its destabilization. Alternative names for HERC1 include p532 and p619.
 HERC2 HERC2 (HECT domain and RCC1-like domain-containing protein 2) belongs to the HERC family of ubiquitin ligases. A single nucleotide polymorphism (SNP) in an evolutionarily conserved region of the HERC2 gene is associated with blue eye color. Additionally, it has been reported that gene-gene interactions between HERC2, OCA2, and MC1R may influence eye, skin, and hair color.
 LARG LARG (leukemia-associated RhoGEF) is homologous to PDZ-RhoGEF and functions as a RhoA-specific guanine nucleotide exchange factor. RhoGEFs catalyze the exchange of GDP for GTP on the GTPase, Rho, to activate downstream signaling pathways. LARG contains a PDZ [post synaptic density protein (PSD95), Drosophila discs-large tumor suppressor (DIgA), and zonula occludens-1 protein (zo-1)] domain which is an 80-90 amino acid structural domain found in signaling proteins in bacteria, yeast, plants, and animals. LARG is proposed to play a role in cell polarity and microtubule dynamics and may act as a GTPase-activating protein (GAP) for the heterotrimeric Galpha(12) and Galpha(13) proteins. Alternative names for LARG include Rho guanine nucleotide exchange factor 12, ARHGEF12, PRO02792, and KIAA0382.
 NF1 Inactivating mutations in NF1 (neurofibromin 1) result in neurofibromatosis type I (NF1) which is characterized by Schwann cell neurofibromas, café-au-lait spots, and benign lesions of the iris. At the cellular level, NF1 functions as a negative regulator of Ras activity. Loss of NF1 leads to increased levels of active Ras-GTP which is important for the formation and maintenance of Schwann cell tumors. Alternate names for NF1 include neurofibromatosis-related protein NF-1, neurofibromin truncated, WSS, NFNS, VRNF, and DKFZp686J1293.
 PARG1 PARG1 (PTPL1-associated RhoGAP protein 1) is a GTPase-activating protein (GAP) for Rho and Rap2. PARG1 has recently been identified as a candidate tumor suppressor in mantle-cell lymphoma. Alternative names for PARG1 include Rho GTPase-activating protein 29 and ARHGAP29.
 PDZ-GEF1 PDZ-GEF1 is a guanine nucleotide exchange factor (GEF) for Rap GTPases. It contains one PDZ-signaling domain, a Ras-association (RA) domain, and a region related to a cyclic nucleotide binding domain (RCBD). PDZ-GEF1 functions to catalyze the exchange of GDP for GTP and activate Rap1A, Rap1B, and Rap2B GTPase activity. Alternative names for PDZ-GEF1 include Rap guanine nucleotide exchange factor 2, neural RAP GEF, nRap GEP, RA-GEF, RAPGEF2, NRAPGEP, and KIAA0313.
 PDZ-GEF2 PDZ-GEF2 is a guanine nucleotide exchange factor (GEF) for Rap GTPases. It contains one PDZ-signaling domain, a Ras-association (RA) domain, and a region related to a cyclic nucleotide binding domain (RCBD). PDZ-GEF1 functions to catalyze the exchange of GDP for GTP and activate Rap1A, Rap1B, and Rap2B GTPase activity. PDZ-GEF2 has been shown to activate Rap1A and Rap1B to promote the maturation of cell-cell adherens junctions. Alternative names for PDZ-GEF2 include Rap guanine nucleotide exchange factor 6, PDZ domain-containing guanine nucleotide exchange factor 2, RAPGEF6, RA-GEF-2, RAGEF2, PDZGEF2, and KIA001LB.
 PDZ-RhoGEF PDZ-RhoGEF (PDZ domain-containing Rho guanine nucleotide exchange factor) catalyzes the exchange of GDP for GTP on the GTPase, Rho, to activate downstream signaling pathways. It contains a PDZ [post synaptic density protein (PSD95), Drosophila dis large tumor suppressor (DIgA), and zonula occludens-1 protein (zo-1)] domain which is an 80-90 amino acid structural domain found in signaling proteins in bacteria, yeast, plants, and animals. PDZ-RhoGEF has been shown to be important to cell migration and the regulation of adhesion movement and trailing edge retraction. Alternative names for PDZ-RhoGEF include ARHGEF11, GTRAP48, and KIAA0380.
 PLEKHG2 PLEKHG2 (pleckstrin homology domain-containing family G member 2) contains a RhoGEF/DH domain and a pleckstrin homology (PH) domain. PH domains are found in proteins involved in cell signaling. PLEKHG2 is proposed to be a guanine-nucleotide exchange factor (GEF) for RAC1/CDC42. Due its identification as a site for proviral integration in leukemias, PLEKHG2 is also known as Clg (common-site lymphoma/leukemia guanine nucleotide exchange factor).
 RanBP1 Ran-binding protein 1 (RanBP1) binds to the GTP-binding protein, Ran, when it is specifically complexed with GTP. RanBP1 binding to GTP-charged RAN increases the catalytic efficiency of GTP hydrolysis activated by RanGAP, the Ran specific GTPase-activating protein. RanBP1 is also a negative regulator of RCC1 which functions in the nuclear pore transport process and cell cycle progression. RanBP1 is also known as Ran-specific GTPase-activating protein, and MGC88701.
 RanBP2 Ran binding protein 2 (RanBP2) is a large multi-modular nucleoporin protein (also called NUP358) that bears several structural domains including a cyclophilin-type rotamase domain, four RanBD1 domains, eight RanBP2-type zinc fingers, and one TPR repeat. This variety of structural domains imparts pleiotropic qualities to RanBP2. RanBP2 has been shown to function as an E3 SUMO-protein ligase and is also part of the nuclear export pathway. Alternate names for RanBP2 include nucleoporin Nup358, p270, TRP1, and TRP2.
 RanBP3 Ran binding protein 3 (RanBP3) is a Ran (ras-related nuclear protein) binding protein and a component of a nuclear transport complex that functions to export proteins out of the nucleus. RanBP3 binds the nucleocytoplasmic transport receptor, CRM1, and facilitates the export of CRM1 substrates. Recently it has been shown that RanBP3 function is regulated by the Ras/ERK/RSK and PI3K/Akt signaling pathway. This finding has provided a link between nuclear transport, cell signaling, and cell fate.
 RanBP8 Ran-binding protein 8 (RanBP8), also known as importin-8, bears sequence motifs related to the Ran-binding site of the nucleocytoplasmic transport protein, importin-beta (KPNB1). The Ran-GTPase, along with importin-alpha/beta complexes, provides the energy and directionality for the transport of macromolecules between the cytoplasm and nucleus. RanBP8 seems to have functional properties similar to importin-beta. Alternate names for RanBP8 include importin-8, IPO8, and FLJ26580.
 RanGAP1 The regulation of GTPase activity is achieved via activators called GEFs (guanine-nucleotide exchange factors) and inactivators called GAPs (GTPase-activating proteins). Ran-specific GTPase-activating protein 1 (RanGAP1) induces the GTPase activity of the RAN small GTPase. The Ran GTPase plays a role in spatial information and nucleocytoplasmic transport. RanGAP1 is the antagonist of the GEF RCC1 which keeps RAN in the active GTP-bound state. Alternative names for RanGAP1 include segregation distorter homolog, SD, and KIAA1835.
 RASAL2 RAS protein activator like 2 (RASAL2) contains a GAP-related domain which is a characteristic domain of GTPase-activating proteins (GAPs). RASAL2 is highly homologous to Ras-specific GTPase activating proteins (RasGAPs). RASAL2 is also known as NGAP..
 RCC1 RCC1 (regulator of chromosome condensation 1) is a chromatin associated guanine-nucleotide exchange factor (GEF) for the small nuclear G-protein, Ran. RCC1 is important to the nuclear pore transport process as well as chromosome condensation during S-phase of mitosis. The RCC1/Ran complex may also function to communicate the status of chromosomal replication to the events of cell cycle progression. RCC1 is also known as chromosome condensation protein 1, cell cycle regulatory protein, guanine nucleotide-releasing protein, and CHC1.
 Sin1 Stress-activated map kinase-interacting protein 1 (Sin1) is highly similar to the yeast stress- activated protein kinase SIN1. Sin1 is an essential mTORC2 subunit that is required to act as the PDK2 that phosphorylates Akt/PKB at Ser 473. Sin1 has been implicated as a scaffolding protein. Sin1 is required for rictor binding in the mTORC2 complex. Sin1 has also been shown to be important to the SAPK (stress-activated kinase) signaling pathway and in the nucleus may act as a scaffold between ATF-2 and p38 to facilitate p38-induced phosphorylation of ATF-2. Sin1 is also found to form a complex with c-Jun N-terminal kinase (JNK) and may similarly function as a scaffolding protein in JNK signaling. Sin1 is also known as SAPK-interacting protein 1, putative ras inhibitor JC310, MAPKAP1, MIP1, SIN1b, SIN1g, and MGC2745.
 SIPA1 The regulation of GTPase activity is achieved via activators called GEFs (guanine-nucleotide exchange factors) and inactivators called GAPs (GTPase-activating proteins). Signal-induced proliferation-associated protein 1 (SIPA1) is a GTPase activating protein (GAP) for the Rap1 and Rap2 small GTPases. Spa-1 has been found to play an important role in hematopoietic cell development and the invasion and metastasis of human cancers. SIPA1 is also known as spa-1.
 SOS1 SOS1 (son of sevenless homolog 1) is a human paralog of the drosophila SOS gene. Drosophila SOS was originally identified as a gene that functioned downstream of the sevenless gene in the Ras/MAP kinase signaling pathway. SOS and its paralogs, SOS1 and SOS2, function as guanine nucleotide exchange factors that act on Ras-GTPases to cause release of GDP in exchange for GTP. Mutations in SOS1 are the cause of Noonan syndrome type 4 and gingival fibromatosis.
 SOS2 SOS2 (son of sevenless homolog 2) is a human paralog of the Drosophila SOS gene. Drosophila SOS was originally identified as a gene that functioned downstream of the sevenless gene in the Ras/MAP kinase signaling pathway. SOS and its paralogs, SOS1 and SOS2, function as guanine nucleotide exchange factors that act on Ras-GTPases to cause release of GDP in exchange for GTP. Although targeted disruption of SOS1 results in embryonic lethality, disruption of SOS2 does not have any effects on mouse development, growth, or fertility.
 SRGAP1/ARHGAP13 SRGAP1/ARHGAP13 is a member of the srGAP family of proteins that contain a RhoGAP domain, an SH3 domain, and a Fes/CIP4 homology domain and interact with the intracellular domain of roundabout 1 (Robo1). Robo1 is the receptor for Slit signaling and is involved in neuronal cell migration and axon tract positioning. SRGAP1/ARHGAP13 functions to bind and decrease the level of active Cdc42 and RhoA small GTPases during Slit-Robo signaling. Alternate names for SRGAP1/ARHGAP13 include Rho GTPase-activating protein 13, and KIAA1304.
 TBC1D9/MDR1 TBC1D9, also known as MDR1 (multidrug resistance 1), is a P-glycoprotein implicated in the mechanism of multidrug resistance to chemotherapeutic agents. TBC1D9 functions as an energy-dependent membrane efflux pump for lipophilic compounds. Alternate names for TBC1D9 include TBC1 domain family member 9 (with GRAM domain), and KIAA0882.
 TIAM1 T lymphoma invasion and metastasis-inducing protein 1 (TIAM1) is a guanine-nucleotide exchange factor (GEF) that positively regulates the Rac1-GTPase. Through Rac1, TIAM1 promotes cell migration and adhesion by modulating the actin cytoskeleton. TIAM1 was originally identified as a gene that induced invasion of lymphocytes. Alternate designations for TIAM1 are TIAM-1 protein, and FLJ36302.
 TSC1 Tuberous sclerosis 1 protein (TSC1) forms a heterodimer with TSC2 to integrate cellular growth and stress signals. Defects in the TSC1 and TSC2 gene are responsible for the genetic disorder tuberous sclerosis. The TSC1/TSC2 complex functions in the mTOR pathway by negatively regulating mTOR activity via the small GTP-binding protein Rheb. TSC1 is also called hamartin, LAM, TSC, KIAA0243, and MGC86987.
 TSC2 Tuberous sclerosis 2 protein (TSC2) forms a heterodimer with TSC1 to integrate cellular growth and stress signals. Defects in the TSC1 and TSC2 gene are responsible for the genetic disorder tuberous sclerosis. The TSC1/TSC2 complex functions in the mTOR pathway by negatively regulating mTOR activity via the small GTP-binding protein Rheb. TSC2 also been shown to interact with FOXO1 transcription factor. TSC2 is also called tuberin, LAM, TSC4, and FLJ43106.


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