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1Q5T1N8_HUMAN*   Trembl (?) | Description Local Annotation Link Reference
General Information
NameN/A
DescriptionG-protein signalling modulator 2 (ags3-like, c. elegans).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005488 binding (IEA)
0005096 GTPase activator activity (IEA)
0007165 signal transduction (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:
In heterotrimeric G-protein signalling.ell surface receptors (GPCRs) arecoupled to membrane-associated heterotrimers comprising a GTP-hydrolyzingsubunit G-alpha and a G-beta/G-gamma dimer. The inactive form contains thealpha subunit bound to GDP and complexes with the beta and gamma subunit. Whenthe ligand is associated to the receptor.DP is displaced from G-alpha andGTP is bound. GTP/G-alpha complex dissociates from the trimer and associatesto an effector until the intrinsic GTPase activity of G-alpha returns theprotein to GDP bound form. Reassociation of GDP bound G-alpha withG-beta/G-gamma dimer terminates the signal. Several mechanisms regulate thesignal output at different stage of the G-protein cascade. Two classes ofintracellular proteins act as inhibitors of G protein activation: GTPaseactivating proteins (GAPs).hich enhance GTP hydrolysis (see ).nd guanine dissociation inhibitors (GDIs).hich inhibit GDP dissociation.The GoLoco or G-protein regulatory (GPR) motif found in various G-proteinregulators .cts as a GDI on G-alpha(i) .The crystal structure of the GoLoco motif in complex with G-alpha(i) has beensolved . It consists of three small alpha helices. Thehighly conserved Asp-Gln-Arg triad within the GoLoco motif participatesdirectly in GDP binding by extending the arginine side chain into thenucleotide binding pocket.ighly reminiscent of the catalytic arginine fingeremployed in GTPase-activating protein (see ). This addition of anarginine in the binding pocket affects the interaction of GDP with G-alpha andtherefore is certainly important for the GoLoco GDI activity .Some proteins known to contain a GoLoco motif are listed below: Mammalian regulators of G-protein signaling 12 and 14 (RGS12 and RGS14).ultifaceted signal transduction regulators. Loco.he drosophila RGS12 homologue. Mammalian Purkinje-cell protein-2 (Pcp2). It may function as a cell-type specific modulator for G protein-mediated cell signaling. It is uniquely expressed in cerebellar Purkinje cells and in retinal bipolar neurons. Eukaryotic Rap1GAP. A GTPase activator for the nuclear ras-related regulatory protein RAP-1A. Drosophila protein Rapsynoid (also known as Partner of Inscuteable.ins) and its mammalian homologues AGS3 and LGN. They form a G-protein regulator family that also contains TPR repeats.
  IPR003109:GoLoco
The tetratrico peptide repeat region (TPR) is a structural motif present in a wide range of proteins . It mediates proteinprotein interactions and the assembly of multiprotein complexes . The TPR motif consists of 316 tandem-repeats of 34 amino acids residues.lthough individual TPR motifs can be dispersed in the protein sequence. Sequence alignment of the TPR domains reveals a consensus sequence defined by a pattern of small and large amino acids. TPR motifs have been identified in various different organisms.anging from bacteria to humans. Proteins containing TPRs are involved in a variety of biological processes.uch as cell cycle regulation.ranscriptional control.itochondrial and peroxisomal protein transport.eurogenesis and protein folding. The X-ray structure of a domain containing three TPRs from protein phosphatase 5 revealed that TPR adopts a helixturnhelix arrangement.ith adjacent TPR motifs packing in a parallel fashion.esulting in a spiral of repeating anti-parallel alpha-helices . The two helices are denoted helix A and helix B. The packing angle between helix A and helix B is ~24° within a single TPR and generates a right-handed superhelical shape. Helix A interacts with helix B and with helix A of the next TPR. Two protein surfaces are generated: the inner concave surface is contributed to mainly by residue on helices A.nd the other surface presents residues from both helices A and B.
  IPR013026:Tetratricopeptide region
The tetratrico peptide repeat (TPR) is a structural motif present in a wide range of proteins . It mediates proteinprotein interactions and the assembly of multiprotein complexes . The TPR motif consists of 316 tandem-repeats of 34 amino acids residues.lthough individual TPR motifs can be dispersed in the protein sequence. Sequence alignment of the TPR domains reveals a consensus sequence defined by a pattern of small and large amino acids. TPR motifs have been identified in various different organisms.anging from bacteria to humans. Proteins containing TPRs are involved in a variety of biological processes.uch as cell cycle regulation.ranscriptional control.itochondrial and peroxisomal protein transport.eurogenesis and protein folding. The X-ray structure of a domain containing three TPRs from protein phosphatase 5 revealed that TPR adopts a helixturnhelix arrangement.ith adjacent TPR motifs packing in a parallel fashion.esulting in a spiral of repeating anti-parallel alpha-helices . The two helices are denoted helix A and helix B. The packing angle between helix A and helix B is ~24° within a single TPR and generates a right-handed superhelical shape. Helix A interacts with helix B and with helix A of the next TPR. Two protein surfaces are generated: the inner concave surface is contributed to mainly by residue on helices A.nd the other surface presents residues from both helices A and B.
  IPR001440:Tetratricopeptide TPR_1
This domain consists of a multi-helical fold comprised of two curved layers of alpha helices arranged in a regular right-handed superhelix.here the repeats that make up this structure are arranged about a common axis . These superhelical structures present an extensive solvent-accessible surface that is well suited to binding large substrates such as proteins and nucleic acids. This topology has been found with a number of repeats and domains.ncluding the tetratricopeptide repeat (TPR) (found in kinesin light chains.NAP regulatory proteins.lathrin heavy chains and bacterial aspartyl-phosphate phosphatases).nd the pentatricopeptide repeat (PPR) (RNA-processing proteins). The TRP is likely to be an ancient repeat.ince it is found in eukaryotes.acteria and archaea.hereas the PPR repeat is found predominantly in higher plants. The superhelix formed from these repeats can bind ligands at a number of different regions.nd has the ability to acquire multiple functional roles .
  IPR011990:Tetratricopeptide-like helical
IPR003109:GoLoco 
Evalue:-11.2441253662109 
Location:489-511IPR003109:GoLoco 
Evalue:-11.1674909591675 
Location:594-616IPR003109:GoLoco 
Evalue:-10.1426677703857 
Location:628-650IPR003109:GoLoco 
Evalue:-8.408935546875 
Location:544-566IPR001440:TPR_1 
Evalue:-5.82390880584717 
Location:102-135IPR001440:TPR_1 
Evalue:-5 
Location:242-275IPR001440:TPR_1 
Evalue:-4.38721609115601 
Location:282-315IPR013026:TPR 
Evalue:-2.09691001300806 
Location:62-95IPR001440:TPR_1 
Evalue:-2.06048083305359 
Location:142-157IPR013026:TPR 
Evalue:-2 
Location:322-355IPR013026:TPR 
Evalue:-1.79588001734408 
Location:202-235
SequencesProtein: Q5T1N8_HUMAN (684 aa)
mRNA: BC027732
Local Annotation
Synapse Ontology
Calcium release from RyR (Ryanodine Receptor) in the SR (Sarcoplasmic Reticulum) is activated by the calcium induced-calcium-release
sdb:0325 RyR-CICR  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 9 residues, 109221349-109221373Exon2: 103 residues, 109229419-109229723Exon3: 76 residues, 109241008-109241230Exon4: 47 residues, 109241636-109241772Exon5: 49 residues, 109242103-109242246Exon6: 43 residues, 109242786-109242910Exon7: 40 residues, 109243023-109243139Exon8: 54 residues, 109245934-109246090Exon9: 38 residues, 109247270-109247379Exon10: 45 residues, 109248269-109248399Exon11: 25 residues, 109258482-109258553Exon12: 61 residues, 109262757-109262934Exon13: 55 residues, 109266561-109266721Exon14: 73 residues, 109268144-109268359Exon15: 234 residues, 109273845-109274541Exon16: 2 residues, -Jump to Q5T1N8_HUMAN  
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Loci Cluster (Details)Loci: 2532 109221349-109274541 ~-53K 2049(+)Loci: 2533 109594163-109619895 ~-26K 2068(CELSR2)(+)Loci: 3813 109653714-109742086 ~-88K 2077(SORT1)(-)Loci: 2534 109810622-109826277 ~-16K 2079(SYPL2)(+)Loci: 3814 109850969-109853827 ~-3K 2087(AMIGO1)(-)Loci: 2531 109090830-109153671 ~-63K 2044(STXBP3)(+)Link out to UCSC