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1Q6PI83_HUMAN*   Trembl (?) | Description Local Annotation Link Reference
General Information
NameN/A
DescriptionRapgef3 protein.
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005952 cAMP-dependent protein kinase complex (IEA)
0008603 cAMP-dependent protein kinase regulator act... (IEA)
0007242 intracellular signaling cascade (IEA)
0006468 protein amino acid phosphorylation (IEA)

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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 dishevelled.gl-10.nd 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
Proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues . The best studied of these proteins is the prokaryotic catabolite gene activator (alsoknown as the cAMP receptor protein) (gene crp) where such a domain is known to be composed of three alpha-helices anda distinctive eight-stranded.ntiparallel beta-barrel structure. There are six invariant amino acids in this domain.hree of which are glycine residues that are thought to be essential for maintenance of the structural integrity ofthe beta-barrel. cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclicnucleotide-binding domain. The cAPKs are composed of two different subunits. catalytic chain and a regulatory chain.hich contains both copies of the domain. The cGPKs are single chain enzymes that include the two copies of the domainin their N-terminal section. Vertebrate cyclic nucleotide-gated ion-channels also contain this domain. Two suchcations channels have been fully characterized.ne is found in rod cells where it plays a role in visual signaltransduction.
  IPR000595:Cyclic nucleotide-binding
Cyclic AMP (cAMP) is a key intracellular regulator of cell function in both prokaryotes and eukaryotes. One of the ways in which it regulates enzymes is by binding to and causing activation of cAMP-dependent protein kinases.hich in turn activate or deactivate other enzymes by phosphorylating them . In the absence of cAMP.rotein Kinase A (PKA) exists as an equimolar tetramer of regulatory (R) and catalytic (C) subunits . In addition to its role as an inhibitor of the C subunit.he R subunit anchors the holoenzyme to specific intracellular locations and prevents the C subunit from entering the nucleus. All R subunits have a conserved domain structure consisting of the N-terminal dimerization domain.nhibitory region.AMP-binding domain A and cAMP-binding domain B. R subunits interact with C subunits primarily through the inhibitory site. The cAMP-binding domains show extensive sequence similarity and bind cAMP cooperatively. Two types of R subunit exist - Type I and Type II - which differ in molecular weight.equence.utophosphorylation cabaility.ellular location and tissue distribution. Types I and II were further sub-divided into alpha and beta subtypes.ased mainly on sequence similarity. Type I does not undergo such autophosphorylation.ut it can be phosphorylated slowly in vitro by cGMP-dependent protein kinases . cAMP-dependent protein kinases are activated by the binding of two cAMP molecules to specific areas at the C-terminus of each regulatory subunit of the enzyme. This causes in a conformational change in the structure.esulting in dissociation of the active catalytic domain from the regulatory domains.
  IPR002373:cAMP-dependent protein kinase
Small GTPases of the Ras family alternate between 2 conformations induced by the binding of either GTP or GDP. Guanine nucleotide exchange factors (GEFs) induce the dissociation of GDP to allow association of the more abundant GTP. The Ras-like family of small GTPases includes.mong others.as.ap1.-ras.nd Ral. The family is characterized by similarities in the effector domain. The Ras GTPase Rap1 is activated rapidly in response to activation of a variety of receptors. Rap1 activation is mediated by several second messengers.ncluding calcium.iacylglycerol.nd cAMP. GEFs have been identified that mediate these effects. One such GEF is Epac.n exchange protein directly activated by cAMP.hich represents a novel cAMP-induced.rotein kinase A-independent pathway .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008937:Ras guanine nucleotide exchange factor
Winged helix DNA-binding proteins share a related winged helix-turn-helix DNA-binding motif.here the "wings".r loops.re 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 differentiation.eat-shock 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 transposase.here the flexible wing of the enhancer-binding domain is essential for efficient transposition .
  IPR011991:Winged helix repressor DNA-binding
IPR000591:DEP 
Evalue:-20.5528411865234 
Location:68-142IPR000595:cNMP_binding 
Evalue:-13.958607673645 
Location:222-309
SequencesProtein: Q6PI83_HUMAN (321 aa)
mRNA: BC040534
Local Annotation
Synapse Ontology
transport of vesicles in the presynaptic neuron
sdb:0017 Mobilization: synapsins, CAM kinase I  (Evidence:keywords)
activation of protein kinase C
sdb:0206 activation of protein kinase C  (Evidence:keywords)
KO assignmentK08014
  Level 3 annotation:
    Rap guanine nucleotide exchange factor (GEF) 3
  Level 2 annotation:
    Leukocyte transendothelial migration
    Long-term potentiation
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 148 residues, 46417293-46417735Exon2: 26 residues, 46418071-46418143Exon3: 20 residues, 46418242-46418297Exon4: 23 residues, 46418739-46418804Exon5: 31 residues, 46419192-46419280Exon6: 19 residues, 46420190-46420241Exon7: 32 residues, 46420354-46420445Exon8: 62 residues, 46420691-46420873Exon9: 44 residues, 46420964-46421090Exon10: 34 residues, 46421554-46421652Exon11: 51 residues, 46423579-46423726Exon12: 29 residues, 46424036-46424118Exon13: 15 residues, 46426909-46426949Exon14: 29 residues, 46427593-46427676Exon15: 52 residues, 46427761-46427912Exon16: 28 residues, 46428123-46428202Exon17: 31 residues, 46428503-46428592Exon18: 39 residues, 46428868-46428981Exon19: 51 residues, 46429439-46429586Exon20: 27 residues, 46429790-46429867Exon21: 22 residues, 46429979-46430040Exon22: 30 residues, 46430390-46430475Exon23: 58 residues, 46431097-46431266Exon24: 42 residues, 46431448-46431570Exon25: 37 residues, 46431772-46431879Exon26: 20 residues, 46431965-46432019Exon27: 73 residues, 46437915-46438128Exon28: 76 residues, 46438600-46438822Exon29: 2 residues, -Jump to RPGF3_HUMANExon1: 144 residues, 46417306-46417735Exon2: 26 residues, 46418071-46418143Exon3: 20 residues, 46418242-46418297Exon4: 23 residues, 46418739-46418804Exon5: 31 residues, 46419192-46419280Exon6: 19 residues, 46420190-46420241Exon7: 32 residues, 46420354-46420445Exon8: 44 residues, 46420964-46421090Exon9: 34 residues, 46421554-46421652Exon10: 51 residues, 46423579-46423726Exon11: 29 residues, 46424036-46424118Exon12: 15 residues, 46426909-46426949Exon13: 29 residues, 46427593-46427676Exon14: 52 residues, 46427761-46427912Exon15: 28 residues, 46428123-46428202Exon16: 363 residues, 46428503-46429586Exon17: 27 residues, 46429790-46429867Exon18: 22 residues, 46429979-46430040Exon19: 30 residues, 46430390-46430475Exon20: 58 residues, 46431097-46431266Exon21: 42 residues, 46431448-46431570Exon22: 37 residues, 46431772-46431879Exon23: 20 residues, 46431965-46432019Exon24: 73 residues, 46437915-46438128Exon25: 98 residues, 46438600-46438888Exon26: 2 residues, -Jump to Q6PI83_HUMAN  
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Loci Cluster (Details)Loci: 2747 46453287-46462800 ~-10K 8718(+)Loci: 4026 46653017-46684528 ~-32K 8730(COL2A1)(-)Loci: 4025 46417293-46438888 ~-22K 8714(RAPGEF3)(-)Link out to UCSC