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0ARHGB_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameARHGEF11
DescriptionRho guanine nucleotide exchange factor 11 (pdz-rhogef).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005622 intracellular (IC)
0005515 protein binding (IPI)
0005089 Rho guanyl-nucleotide exchange factor activity (TAS)
0030036 actin cytoskeleton organization and biogenesis (NAS)
0006928 cell motility (NAS)
0000910 cytokinesis (NAS)
0030010 establishment of cell polarity (NAS)
0007186 G-protein coupled receptor protein signalin... (TAS)
0045893 positive regulation of transcription, DNA-d... (IDA)
0001558 regulation of cell growth (NAS)
0007266 Rho protein signal transduction (IDA)
0006941 striated muscle contraction (NAS)

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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:
PDZ domains are found in diverse signaling proteins in bacteria.easts.lants.nsects and vertebrates . PDZ domains can occur in one or multiple copies and are nearly always found in cytoplasmic proteins. They bind either the carboxyl-terminal sequences of proteins or internal peptide sequences . In most cases.nteraction between a PDZ domain and its target is constitutive.ith a binding affinity of 1 to 10 ┬ÁM. However.gonist-dependent activation of cell surface receptors is sometimes required to promote interaction with a PDZ protein. PDZ domain proteins are frequently associated with the plasma membrane. compartment where high concentrations of phosphatidylinositol 4.-bisphosphate (PIP2) are found. Direct interaction between PIP2 and a subset of class II PDZ domains (syntenin.ASK.iam-1) has been demonstrated. PDZ domains consist of 80 to 90 amino acids comprising six beta-strands (betaA to betaF) and two alpha-helices. and B.ompactly arranged in a globular structure. Peptide binding of the ligand takes place in an elongated surface groove as an antiparallel beta-strand interacts with the betaB strand and the B helix. The structure of PDZ domains allows binding to a free carboxylate group at the end of a peptide through a carboxylate-binding loop between the betaA and betaB strands.
  IPR001478:PDZ/DHR/GLGF
RGS (Regulator of G Protein Signalling) proteins are multi-functional.TPase-accelerating proteins that promote GTP hydrolysis by the alpha subunit of heterotrimeric G proteins.hereby inactivating the G protein and rapidly switching off G protein-coupled receptor signalling pathways . Upon activation by GPCRs.eterotrimeric G proteins exchange GDP for GTP.re released from the receptor.nd dissociate into free.ctive GTP-bound alpha subunit and beta-gamma dimer.oth of which activate downstream effectors. The response is terminated upon GTP hydrolysis by the alpha subunit ().hich can then bind the beta-gamma dimer (. and the receptor. RGS proteins markedly reduce the lifespan of GTP-bound alpha subunits by stabilising the G protein transition state.All RGS proteins contain an RGS-box (or RGS domain).hich is required for activity. Some small RGS proteins such as RGS1 and RGS4 are comprised of little more than an RGS domain.hile others also contain additional domains that confer further functionality . RGS domains can be found in conjunction with a variety of domains.ncluding: DEP for membrane targeting ().DZ for binding to GPCRs ().TB for phosphotyrosine-binding ().BD for Ras-binding ().oLoco for guanine nucleotide inhibitor activity ().X for phosphatidylinositol-binding ().XA that is associated with PX ().H for stimulating guanine nucleotide exchange ().nd GGL (G protein gamma subunit-like) for binding G protein beta subunits () . Those RGS proteins that contain GGL domains can interact with G protein beta subunits to form novel dimers that prevent G protein gamma subunit binding and G protein alpha subunit association.hereby preventing heterotrimer formation.
  IPR000342:Regulator of G protein signalling
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
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:-65.1549019599858 
Location:738-922IPR001478:PDZ 
Evalue:-17.6197887582884 
Location:55-123IPR000342:RGS 
Evalue:-13.0409586076789 
Location:313-432IPR001849:PH 
Evalue:-7.49485002168009 
Location:966-1081IPR001331:DH_1 
Evalue:0 
Location:0-0
SequencesProtein: ARHGB_HUMAN (1522 aa)
mRNA: NM_014784 NM_198236
Local Annotation
Synapse Ontology
A process that increases long-term neuronal synaptic plasticity, the ability of neuronal synapses to change long-term as circumstances require. Long-term neuronal synaptic plasticity generally involves increase or decrease in actual synapse numbers.
sdb:0039 positive regulation of long-term neuronal synaptic plasticity  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 407 residues, 155171256-155172474Exon2: 65 residues, 155173231-155173421Exon3: 84 residues, 155173664-155173912Exon4: 34 residues, 155174833-155174929Exon5: 123 residues, 155175963-155176326Exon6: 75 residues, 155176622-155176841Exon7: 22 residues, 155177787-155177849Exon8: 44 residues, 155178279-155178405Exon9: 32 residues, 155179105-155179196Exon10: 58 residues, 155180350-155180518Exon11: 27 residues, 155180773-155180849Exon12: 61 residues, 155181434-155181613Exon13: 41 residues, 155182460-155182578Exon14: 44 residues, 155183077-155183203Exon15: 28 residues, 155183351-155183431Exon16: 51 residues, 155183719-155183866Exon17: 64 residues, 155184184-155184372Exon18: 18 residues, 155184596-155184644Exon19: 62 residues, 155184734-155184914Exon20: 44 residues, 155187988-155188115Exon21: 12 residues, 155191307-155191337Exon22: 34 residues, 155192118-155192215Exon23: 50 residues, 155192835-155192980Exon24: 10 residues, 155194207-155194231Exon25: 43 residues, 155195157-155195280Exon26: 34 residues, 155195461-155195558Exon27: 16 residues, 155196833-155196876Exon28: 35 residues, 155198092-155198191Exon29: 36 residues, 155199618-155199720Exon30: 27 residues, 155199935-155200010Exon31: 48 residues, 155204402-155204540Exon32: 27 residues, 155205697-155205774Exon33: 17 residues, 155206413-155206459Exon34: 42 residues, 155208112-155208232Exon35: 26 residues, 155213398-155213470Exon36: 61 residues, 155214619-155214798Exon37: 21 residues, 155215644-155215702Exon38: 18 residues, 155216852-155216902Exon39: 35 residues, 155220754-155220853Exon40: 32 residues, 155222497-155222589Exon41: 359 residues, 155280714-155281786Exon42: 2 residues, -Jump to ARHGB_HUMANExon1: 407 residues, 155171256-155172474Exon2: 65 residues, 155173231-155173421Exon3: 84 residues, 155173664-155173912Exon4: 34 residues, 155174833-155174929Exon5: 123 residues, 155175963-155176326Exon6: 75 residues, 155176622-155176841Exon7: 22 residues, 155177787-155177849Exon8: 44 residues, 155178279-155178405Exon9: 32 residues, 155179105-155179196Exon10: 58 residues, 155180350-155180518Exon11: 27 residues, 155180773-155180849Exon12: 61 residues, 155181434-155181613Exon13: 41 residues, 155182460-155182578Exon14: 44 residues, 155183077-155183203Exon15: 28 residues, 155183351-155183431Exon16: 51 residues, 155183719-155183866Exon17: 64 residues, 155184184-155184372Exon18: 18 residues, 155184596-155184644Exon19: 62 residues, 155184734-155184914Exon20: 44 residues, 155187988-155188115Exon21: 12 residues, 155191307-155191337Exon22: 34 residues, 155192118-155192215Exon23: 50 residues, 155192835-155192980Exon24: 10 residues, 155194207-155194231Exon25: 43 residues, 155195157-155195280Exon26: 34 residues, 155195461-155195558Exon27: 16 residues, 155196833-155196876Exon28: 35 residues, 155198092-155198191Exon29: 36 residues, 155199618-155199720Exon30: 27 residues, 155199935-155200010Exon31: 48 residues, 155204402-155204540Exon32: 27 residues, 155205697-155205774Exon33: 17 residues, 155206413-155206459Exon34: 26 residues, 155213398-155213470Exon35: 61 residues, 155214619-155214798Exon36: 21 residues, 155215644-155215702Exon37: 18 residues, 155216852-155216902Exon38: 35 residues, 155220754-155220853Exon39: 32 residues, 155222497-155222589Exon40: 359 residues, 155280714-155281786Exon41: 2 residues, -Jump to ARHGB_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