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0ARHG2_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameARHGEF2
DescriptionRho/rac guanine nucleotide exchange factor 2 (gef-h1 protein) (proliferating cell nucleolar antigen p40).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005874 microtubule (ISS)
0008017 microtubule binding (ISS)
0048365 Rac GTPase binding (ISS)
0030676 Rac guanyl-nucleotide exchange factor activity (ISS)
0017048 Rho GTPase binding (ISS)
0005089 Rho guanyl-nucleotide exchange factor activity (ISS)
0008270 zinc ion binding (ISS)
0007015 actin filament organization (ISS)
0007166 cell surface receptor linked signal transdu... (TAS)
0000902 cellular morphogenesis (ISS)
0006886 intracellular protein transport (ISS)
0007026 negative regulation of microtubule depolyme... (ISS)
0042127 regulation of cell proliferation (ISS)
0035023 regulation of Rho protein signal transduction (ISS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
The pleckstrin homology (PH) domain is a domain of about 100 residues that occurs in a wide range of proteins involved in intracellular signaling or as constituents of the cytoskeleton .The function of this domain is not clear.everal putative functions have been suggested:binding to the beta/gamma subunit of heterotrimeric G proteins.inding to lipids..g. phosphatidylinositol-4.-bisphosphate.inding to phosphorylated Ser/Thr residues.ttachment to membranes by an unknown mechanism.It is possible that different PH domains have totally different ligand requirements.The 3D structure of several PH domains has been determined . All known cases have a common structure consisting of two perpendicular anti-parallel beta sheets.ollowed by a C-terminal amphipathic helix. The loops connecting the beta-strands differ greatly in length.aking the PH domain relatively difficult to detect. There are no totally invariant residues within the PH domain.Proteins reported to contain one more PH domains belong to the following families:Pleckstrin.he protein where this domain was first detected.s the major substrate of protein kinase C in platelets. Pleckstrin is one of the rare proteins to contains two PH domains.Ser/Thr protein kinases such as the Akt/Rac family.he beta-adrenergic receptor kinases.he mu isoform of PKC and the trypanosomal NrkA family.Tyrosine protein kinases belonging to the Btk/Itk/Tec subfamily.Insulin Receptor Substrate 1 (IRS-1).Regulators of small G-proteins like guanine nucleotide releasing factor GNRP (Ras-GRF) (which contains 2 PH domains).uanine nucleotide exchange proteins like vav.bl.oS and Saccharomyces cerevisiae CDC24.TPase activating proteins like rasGAP and BEM2/IPL2.nd the human break point cluster protein bcr.Cytoskeletal proteins such as dynamin (see ).aenorhabditis elegans kinesin-like protein unc-104 (see ).pectrin beta-chain.yntrophin (2 PH domains) and S. cerevisiae nuclear migration protein NUM1.Mammalian phosphatidylinositol-specific phospholipase C (PI-PLC) (see ) isoforms gamma and delta. Isoform gamma contains two PH domains.he second one is split into two parts separated by about 400 residues.Oxysterol binding proteins OSBP.. cerevisiae OSH1 and YHR073w.Mouse protein citron. putative rho/rac effector that binds to the GTP-bound forms of rho and rac.Several S. cerevisiae proteins involved in cell cycle regulation and bud formation like BEM2.EM3.UD4 and the BEM1-binding proteins BOI2 (BEB1) and BOI1 (BOB1).C. elegans protein MIG-10.C. elegans hypothetical proteins C04D8.1.06H7.4 and ZK632.12.S. cerevisiae hypothetical proteins YBR129c and YHR155w.
  IPR001849:Pleckstrin-like
Diacylglycerol (DAG) is an important second messenger. Phorbol esters (PE) are analogues of DAG and potent tumor promoters that cause a variety of physiological changes when administered to both cells and tissues. DAG activates a family of serine/threonine protein kinases.ollectively known as protein kinase C (PKC) . Phorbol esters can directly stimulate PKC. The N-terminal region of PKC.nown as C1.as been shown to bind PE and DAG in a phospholipid and zinc-dependent fashion. The C1 region contains one or two copies (depending on the isozyme of PKC) of a cysteine-rich domain.hich is about 50 amino-acid residues long.nd which is essential for DAG/PE-binding. The DAG/PE-binding domain binds two zinc ions; the ligands of these metal ions are probably the six cysteines and two histidines that are conserved in this domain.
  IPR002219:Protein kinase C, phorbol ester/diacylglycerol binding
The Rho family GTPases Rho.ac and CDC42 regulate a diverse array of cellularprocesses. Like all members of the Ras superfamily.he Rho proteins cycle between active GTP-bound and inactive GDP-bound conformational states.Activation of Rho proteins through release of bound GDP and subsequentbinding of GTP.s catalyzed by guanine nucleotide exchange factors (GEFs) inthe Dbl family. The proteins encoded by members of the Dbl family share acommon domain.resented in this entry.f about 200 residues (designated the Dbl homology or DH domain)that has been shown to encode a GEF activity specific for a number of Rhofamily members. In addition.ll family members possess a second.hareddomain designated the pleckstrin homology (PH) domain (). Trioand its homolog UNC-73 are unique within the Dbl family insomuch as theyencode two distinct DH/PH domain modules. The PH domain is invariably locatedimmediately C-terminal to the DH domain and this invariant topography suggestsa functional interdependence between these two structural modules. Biochemicaldata have established the role of the conserved DH domain in Rho GTPaseinteraction and activation.nd the role of the tandem PH domain inintracellular targeting and/or regulation of DH domain function. The DH domainof Dbl has been shown to mediate oligomerization that is mostly homophilic innature. In addition to the tandem DH/PH domains Dbl family GEFs containdiverse structural motifs like serine/threonine kinase.BD.DZ.GS.Q.EM.dc25RasGEF.H.H2.H3.F.pectrin or Ig.The DH domain is composed of three structurally conserved regions separated bymore variable regions. It does not share significant sequence homology withother subtypes of small G-protein GEF motifs such as the Cdc25 domain and theSec7 domain.hich specifically interact with Ras and ARFfamily small GTPases.espectively.or with other Rho protein interactivemotifs.ndicating that the Dbl family proteins are evolutionarily unique. TheDH domain is composed of 11 alpha helices that are folded into a flattened.longated alpha-helix bundle in which two of the three conserved regions.onserved region 1 (CR1) and conserved region 3 (CR3).re exposed near thecenter of one surface. CR1 and CR3.ogether with a part of alpha-6 and theDH/PH junction site.onstitute the Rho GTPase interacting pocket.
  IPR000219:DH
Pleckstrin homology (PH) domains are small modular domains that occur once.r occasionally several times.n a large variety of signalling proteins.here they serve as simple targeting domains that recognize only phosphoinositide headgroups . PH domains can target their host protein to the plasma and internal membranes through its association with phosphoinositides. PH domains have a partly opened beta-barrel topology that is capped by an alpha helix. Proteins containing PH domains include pleckstrin (N-terminal).hospholipase C delta-1.eta-spectrin.ynamin.on-of-sevenless.rp1.nc-89.app1 and Rac-alpha kinase.The structure of PH domains is similar to the phosphotyrosine-binding domain (PTB) found in IRS-1 (insulin receptor substrate 1).hc adaptor and Numb; to the Ran-binding domain.ound in Nup nuclear pore complex and Ranbp1; to the Enabled/VASP homology domain 1 (EVH1 domain).ound in Enabled.ASP (vasodilator-stimulated phosphoprotein).omer and WASP actin regulatory protein; to the third domain of FERM.ound in moesin.adixin.zrin.erlin and talin; and to the PH-like domain of neurobeachin.
  IPR011993:Pleckstrin homology-type
IPR000219:RhoGEF 
Evalue:-62.5086383061657 
Location:238-430IPR001849:PH 
Evalue:-14.7212467193604 
Location:472-570IPR002219:C1 
Evalue:-8.36653154442041 
Location:40-86IPR001331:DH_1 
Evalue:0 
Location:0-0
SequencesProtein: ARHG2_HUMAN (893 aa)
mRNA: BC020567 NM_004723
Local Annotation
Synapse Ontology
microtubules of the presynaptic compartment function as the tracks for the intense traffic of organelles from cell body to axon terminals and vice versa. It is generally excluded from the presynaptic vesicle cluster.Microtubules do not directly regulate synapse morphology or function
sdb:0087 microtubules  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 388 residues, 154183269-154184430Exon2: 63 residues, 154186713-154186897Exon3: 150 residues, 154187243-154187687Exon4: 19 residues, 154187897-154187948Exon5: 14 residues, 154188155-154188191Exon6: 24 residues, 154188333-154188401Exon7: 42 residues, 154188530-154188650Exon8: 69 residues, 154189042-154189243Exon9: 24 residues, 154191316-154191384Exon10: 58 residues, 154194127-154194297Exon11: 27 residues, 154194734-154194811Exon12: 85 residues, 154198075-154198324Exon13: 41 residues, 154198519-154198637Exon14: 44 residues, 154199007-154199133Exon15: 85 residues, 154199347-154199598Exon16: 49 residues, 154201402-154201543Exon17: 38 residues, 154201717-154201827Exon18: 45 residues, 154202045-154202175Exon19: 23 residues, 154202830-154202894Exon20: 24 residues, 154203234-154203302Exon21: 50 residues, 154205570-154205715Exon22: 33 residues, 154214481-154214575Exon23: 2 residues, -Jump to ARHG2_HUMANExon1: 375 residues, 154183308-154184430Exon2: 63 residues, 154186713-154186897Exon3: 150 residues, 154187243-154187687Exon4: 19 residues, 154187897-154187948Exon5: 14 residues, 154188155-154188191Exon6: 24 residues, 154188333-154188401Exon7: 42 residues, 154188530-154188650Exon8: 69 residues, 154189042-154189243Exon9: 24 residues, 154191316-154191384Exon10: 58 residues, 154194127-154194297Exon11: 27 residues, 154194734-154194811Exon12: 85 residues, 154198075-154198324Exon13: 41 residues, 154198519-154198637Exon14: 44 residues, 154199007-154199133Exon15: 85 residues, 154199347-154199598Exon16: 50 residues, 154201402-154201546Exon17: 38 residues, 154201717-154201827Exon18: 45 residues, 154202045-154202175Exon19: 23 residues, 154202830-154202894Exon20: 24 residues, 154203234-154203302Exon21: 50 residues, 154205570-154205715Exon22: 56 residues, 154214779-154214942Exon23: 2 residues, -Jump to ARHG2_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3833 152220753-152225430 ~-5K 2681(RAB13)(-)Loci: 2551 152511662-152514973 ~-3K 2706(HAX1)(+)Loci: 2552 152806880-152815707 ~-9K 2720(CHRNB2)(+)Loci: 3834 152821158-152847306 ~-26K 2722(ADAR)(-)Loci: 3835 153201398-153209847 ~-8K 2739(SHC1)(-)Loci: 2553 153412983-153424069 ~-11K 2783(TRIM46)(+)Loci: 2554 153513997-153526262 ~-12K 2831(HCN3)(+)Loci: 3836 153526253-153537835 ~-12K 2833(PKLR)(-)Loci: 2555 153669594-153670676 ~-1K 2846(POU5FLC1)(+)Loci: 2556 154095923-154121459 ~-26K 2875(SYT11)(+)Loci: 3837 154183269-154214942 ~-32K 2882(ARHGEF2)(-)Loci: 2557 154297589-154306917 ~-9K 2890(RAB25)(+)Loci: 2558 154362603-154374280 ~-12K 2897(+)Loci: 2559 154855709-154862142 ~-6K 2944(HAPLN2)(+)Loci: 2560 154878363-154895942 ~-18K 2945(BCAN)(+)Loci: 3838 154905181-154913813 ~-9K 2947(NES)(-)Loci: 2561 155097294-155118266 ~-21K 2961(NTRK1)(+)Loci: 3839 155171256-155281786 ~-111K 2965(ARHGEF11)(-)Loci: 2550 151897823-151900928 ~-3K 2658(SNAPAP)(+)Link out to UCSC