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0SNX27_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameSNX27
DescriptionSorting nexin-27.
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GON/A
Domain Architecture (Details)
InterPro domains unassigned to SynO:
The PX (phox) domain occurs in a variety of eukaryotic proteins and have been implicated in highly diverse functions such as cell signalling.esicular trafficking.rotein sorting and lipid modification . PX domains are important phosphoinositide-binding modules that have varying lipid-binding specificities .The PX domain is approximately 120 residues long .nd folds into a three-stranded beta-sheet followed by three -helices and a proline-rich region that immediately preceeds a membrane-interaction loop and spans approximately eight hydrophobic and polar residues. The PX domain of p47phox binds to the SH3 domain in the same protein. Phosphorylation of p47(phox). cytoplasmic activator of the microbicidal phagocyte oxidase (phox).licits interaction of p47(phox) with phoinositides. The protein phosphorylation-driven conformational change of p47(phox) enables its PX domain to bind to phosphoinositides.he interaction of which plays a crucial role in recruitment of p47(phox) from the cytoplasm to membranes and subsequent activation of the phagocyte oxidase. The lipid-binding activity of this protein is normally suppressed by intramolecular interaction of the PX domain with the C-terminal Src homology 3 (SH3) domain .The PX domain is conserved from yeast to human. A recent multiple alignment of representative PX domain sequences can be found in .lthough showing relatively little sequence conservation.heir structure appears to be highly conserved. Although phosphatidylinositol-3-phosphate (PtdIns(3)P) is the primary target of PX domains.inding to phosphatidic acid.hosphatidylinositol-3.-bisphosphate (PtdIns(3.)P2).hosphatidylinositol-3.-bisphosphate (PtdIns(3.)P2).hosphatidylinositol-4.-bisphosphate (PtdIns(4.)P2).nd phosphatidylinositol-3..-trisphosphate (PtdIns(3..)P3) has been reported as well. The PX-domain is also a protein-protein interaction domain .
  IPR001683:Phox-like
Proteins with this domain are mostly RasGTP effectors and include guanine-nucleotide releasing factor in mammals . This factor stimulates the dissociation of GDP from the Ras-related RALA and RALB GTPases which allows GTP binding and activation of the GTPases. It interacts and acts as an effector molecule for R-ras.-Ras and Rap .The domain is also present in a number of other proteins among them the sexual differentiation protein in yeast that is essential for mating and meiosis and yeast adenylate cyclase. These proteins contain repeated leucine-rich (LRR) segments.
  IPR000159:RA
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
IPR001683:PX 
Evalue:-21.4685211181641 
Location:68-172IPR000159:RA 
Evalue:-19.2146701812744 
Location:180-269IPR001478:PDZ 
Evalue:0 
Location:12-54
SequencesProtein: SNX27_HUMAN (435 aa)
mRNA: AY044866 NM_030918
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: 110 residues, 149851285-149851612Exon2: 79 residues, 149877987-149878219Exon3: 66 residues, 149897334-149897527Exon4: 23 residues, 149899897-149899962Exon5: 37 residues, 149901265-149901370Exon6: 28 residues, 149905032-149905111Exon7: 56 residues, 149907571-149907735Exon8: 32 residues, 149922455-149922545Exon9: 52 residues, 149931534-149931684Exon10: 45 residues, 149932010-149932139Exon11: 22 residues, 149932523-149932583Exon12: 1832 residues, 149932692-149938183Exon13: 2 residues, -Jump to SNX27_HUMANExon1: 89 residues, 149877955-149878219Exon2: 66 residues, 149897334-149897527Exon3: 23 residues, 149899897-149899962Exon4: 37 residues, 149901265-149901370Exon5: 28 residues, 149905032-149905111Exon6: 56 residues, 149907571-149907735Exon7: 32 residues, 149922455-149922545Exon8: 52 residues, 149931534-149931684Exon9: 45 residues, 149932010-149932139Exon10: 22 residues, 149932523-149932583Exon11: 5 residues, 149932692-149932701Exon12: 2 residues, -Jump to SNX27_HUMAN  
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Loci Cluster (Details)Loci: 2548 149493820-149506576 ~-13K 2556(PSMD4)(+)Loci: 3831 149531036-149566511 ~-35K 2560(PIK4CB)(-)Loci: 2549 149851285-149938183 ~-87K 2579(SNX27)(+)Loci: 3832 150010960-150029541 ~-19K 2590(TDRKH)(-)Loci: 3830 149370788-149385728 ~-15K 2543(SEMA6C)(-)Link out to UCSC