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0SNX19_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionSorting nexin-19.
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
Domain Architecture (Details)
InterPro domains unassigned to SynO:
This domain is found associated with PX domains. The PX (phox) domain occurs in a variety of eukaryotic proteins associated with intracellular signaling pathways.
This domain is found associated with PX domains. The PX (phox) domain occurs in a variety of eukaryotic proteins associated with intracellular signaling pathways.
  IPR013996:PX-associated, sorting nexin 13
This region is found at the C terminus of proteins belonging to the nexin family. It is found on proteins which also contain .
  IPR013937:Sorting nexin, C-terminal
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 .
The fundamental activity of the ribosome is two-fold: to decode the message of the mRNA in the small subunit.nd to form a peptide bond between peptidyl-tRNA and aminoacyl-tRNA by a peptidyl transferase activity in the large subunit. Several prokaryotic and eukaryotic proteins that are involved in the translation process contain an SH3-like domain. The structure of the translation protein SH3-like domain is a partly opened beta the last strand is interrupted by a 3-10 helical turn. The structure of the RNA-binding C-terminal domain of the Bacillus stearothermophilus ribosomal protein L2 has been shown to adopt the SH3-like barrel topology . The L2 protein is located near the peptidyl transferase centre in the large ribosomal subunit where it may contribute to peptidyl transferase activity.nd is involved in the assembly of the 23SrRNA. Likewise.he N-terminal domain of the ubiquitous eukaryotic initiation translation factor 5a (IF-5A) protein adopts the SH3-like barrel topology . IF-5A is involved in the initial step of peptide bond formation in translation and in cell-cycle regulation. IF-5A acts as a cofactor of the Rev protein in HIV-1-infected cells and of the Rex protein in T-cell leukaemia virus 1-infected cells. The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008991:Translation protein SH3-like
SequencesProtein: SNX19_HUMAN (992 aa)
mRNA: NM_014758
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: 892 residues, 130250984-130253659Exon2: 31 residues, 130254728-130254816Exon3: 63 residues, 130255726-130255911Exon4: 45 residues, 130278359-130278489Exon5: 62 residues, 130281057-130281238Exon6: 34 residues, 130281729-130281826Exon7: 45 residues, 130283057-130283188Exon8: 42 residues, 130285122-130285242Exon9: 35 residues, 130285374-130285475Exon10: 48 residues, 130286737-130286876Exon11: 736 residues, 130289370-130291572Exon12: 2 residues, -Jump to SNX19_HUMAN  
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