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0PREX1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionPhosphatidylinositol 3,4,5-trisphosphate-dependent rac exchanger 1 protein (p-rex1 protein).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005829 cytosol (IDA)
0005886 plasma membrane (TAS)
0019899 enzyme binding (TAS)
0005543 phospholipid binding (IDA)
0005100 Rho GTPase activator activity (TAS)
0005089 Rho guanyl-nucleotide exchange factor activity (TAS)
0030041 actin filament polymerization (TAS)
0042119 neutrophil activation (TAS)
0006801 superoxide metabolism (TAS)

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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:
This is a domain of unknown function present in signaling proteins including pleckstrinproteins. Segment polarity dishevelled protein is required to establish coherent arrays of polarized cells andsegments in embryos.nd plays a role in wingless signaling. Egl-10 regulates G-protein signaling in the centralnervous system. Mammalian regulators of G-protein signaling also contain these domains.nd regulate signaltransduction by increasing the GTPase activity of G-protein alpha subunits.hereby driving them into theirinactive GDP-bound form.
  IPR000591:Pleckstrin/ G-protein, interacting region
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 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.
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.
The Rho family GTPases 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.
Winged helix DNA-binding proteins share a related winged helix-turn-helix DNA-binding the "wings".r small beta-sheets. The winged helix motif consists of two wings (W1.2).hree alpha helices (H1.2.3) and three beta-sheets (S1.2.3) arranged in the order H1-S1-H2-H3-S2-W1-S3-W2 . The DNA-recognition helix makes sequence-specific DNA contacts with the major groove of DNA.hile the wings make different DNA contacts.ften with the minor groove or the backbone of DNA. Several winged-helix proteins display an exposed patch of hydrophobic residues thought to mediate protein-protein interactions.Many different proteins with diverse biological functions contain a winged helix DNA-binding domain.ncluding transcriptional repressors such as biotin repressor.exA repressor and the arginine repressor ; transcription factors such as the hepatocyte nuclear factor-3 proteins involved in cell transcription factor.nd the general transcription factors TFIIE and TFIIF . helicases such as RuvB that promotes branch migration at the Holliday junction.nd CDC6 in the pre-replication complex . endonucleases such as FokI and TnsA ; histones; and Mu the flexible wing of the enhancer-binding domain is essential for efficient transposition .
  IPR011991:Winged helix repressor DNA-binding
SequencesProtein: PREX1_HUMAN (1659 aa)
mRNA: NM_020820
Local Annotation
Synapse Ontology
intermediate filaments of the presynaptic compartments. Both microtubles and intermediate filaments represent the main structural scaffold of axons.
sdb:0086 intermediate filaments  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 558 residues, 46674199-46675872Exon2: 24 residues, 46677492-46677560Exon3: 36 residues, 46677805-46677908Exon4: 59 residues, 46679393-46679566Exon5: 24 residues, 46680672-46680739Exon6: 40 residues, 46682221-46682336Exon7: 50 residues, 46682440-46682584Exon8: 35 residues, 46684620-46684720Exon9: 75 residues, 46686407-46686628Exon10: 16 residues, 46687655-46687697Exon11: 45 residues, 46689710-46689839Exon12: 32 residues, 46692112-46692203Exon13: 29 residues, 46692351-46692434Exon14: 31 residues, 46694353-46694442Exon15: 71 residues, 46695795-46696002Exon16: 94 residues, 46699244-46699521Exon17: 72 residues, 46699940-46700151Exon18: 56 residues, 46700838-46701000Exon19: 64 residues, 46701340-46701528Exon20: 42 residues, 46702530-46702651Exon21: 47 residues, 46703305-46703442Exon22: 30 residues, 46705234-46705320Exon23: 51 residues, 46706984-46707133Exon24: 33 residues, 46708080-46708173Exon25: 49 residues, 46709863-46710006Exon26: 26 residues, 46716227-46716300Exon27: 27 residues, 46726137-46726213Exon28: 18 residues, 46729304-46729354Exon29: 36 residues, 46729595-46729699Exon30: 35 residues, 46731179-46731280Exon31: 51 residues, 46738601-46738749Exon32: 52 residues, 46740891-46741041Exon33: 41 residues, 46742616-46742735Exon34: 46 residues, 46750697-46750831Exon35: 56 residues, 46758204-46758366Exon36: 36 residues, 46776233-46776335Exon37: 37 residues, 46784489-46784594Exon38: 43 residues, 46794968-46795091Exon39: 26 residues, 46797752-46797824Exon40: 82 residues, 46877585-46877827Exon41: 2 residues, -Jump to PREX1_HUMAN  
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