SynDB Home Page
SynDB Home Page
Browse
Search
Download
Help
People
links

blue bulletSynDB protein details  


Parse error: syntax error, unexpected T_VARIABLE in /home/kongl/syndb/www/sdb_nats.php on line 52
0RGS12_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameRGS12
DescriptionRegulator of g-protein signaling 12 (rgs12).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0000794 condensed nuclear chromosome (TAS)
0005096 GTPase activator activity (TAS)
0008277 regulation of G-protein coupled receptor pr... (TAS)

Warning: fopen(/home/kongl/syndb/www/temp/1172785668.dot) [function.fopen]: failed to open stream: Permission denied in /home/kongl/syndb/www/sdb_pro.php on line 269

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 270

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 271

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 272

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 273

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 274

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 299

Warning: fclose(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 300
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 PI domain has a similar structure to the insulin receptor substrate-1 PTB domain. 7-stranded beta-sandwich.apped by a C-terminal helix.However.he PI domain contains an additional short N-terminal helix and alarge insertion between strands 1 and 2.hich forms a helix and 2 longconnecting loops. The substrate peptide fits into a surface cleft formedfrom the C-terminal helix and strand 5 .
  IPR006020:Phosphotyrosine interaction region
This is the Ras-binding domain found in proteins related to Ras. It is foundin association with the PE-bind and pkinase domains.
  IPR003116:Raf-like Ras-binding
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
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
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
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
IPR000342:RGS 
Evalue:-42.4089353929735 
Location:715-832IPR006020:PTB 
Evalue:-31.267606240177 
Location:225-374IPR003116:RBD 
Evalue:-31.1249389648438 
Location:962-1032IPR003116:RBD 
Evalue:-24.8860569000244 
Location:1034-1104IPR001478:PDZ 
Evalue:-17.2596378326416 
Location:22-96IPR003109:GoLoco 
Evalue:-9.35654735565185 
Location:1187-1209
SequencesProtein: RGS12_HUMAN (1447 aa)
mRNA: NM_198229
Local Annotation
Synapse Ontology
the plasma membrane of the postsynaptic neuron. It apposes with presynaptic actiove zone.
sdb:0108 postsynaptic plasma membrane  (Evidence:keywords)
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: 268 residues, 3285671-3286474Exon2: 662 residues, 3287594-3289576Exon3: 41 residues, 3314461-3314578Exon4: 9 residues, 3357940-3357962Exon5: 58 residues, 3385596-3385766Exon6: 33 residues, 3386276-3386369Exon7: 50 residues, 3387502-3387646Exon8: 62 residues, 3388437-3388617Exon9: 53 residues, 3388912-3389066Exon10: 27 residues, 3392166-3392243Exon11: 67 residues, 3393900-3394095Exon12: 26 residues, 3394429-3394503Exon13: 44 residues, 3395039-3395166Exon14: 34 residues, 3396988-3397085Exon15: 28 residues, 3399614-3399694Exon16: 53 residues, 3400082-3400236Exon17: 185 residues, 3401931-3402480Exon18: 154 residues, 3410979-3411436Exon19: 2 residues, -Jump to RGS12_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3402 3285671-3411436 ~-126K 27271(RGS12)(+)Loci: 3403 3738093-3740049 ~-2K 27284(ADRA2C)(+)Loci: 3401 3046205-3215484 ~-169K 27267(HD)(+)Link out to UCSC