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0APBA2_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameAPBA2
DescriptionAmyloid beta a4 precursor protein-binding family a member 2 (neuron- specific x11l protein) (neuronal munc18-1-interacting protein 2) (mint-2) (adapter protein x11beta).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005515 protein binding (IPI)
0007399 neurogenesis (TAS)

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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:
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
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
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
IPR006020:PID 
Evalue:-72.0222778320313 
Location:372-530IPR001478:PDZ 
Evalue:-22.5528411865234 
Location:568-652IPR001478:PDZ 
Evalue:-20.2596378326416 
Location:659-732
SequencesProtein: APBA2_HUMAN (749 aa)
mRNA: NM_005503
Local Annotation
Synapse Ontology
Various stages of the synaptic vesicle cycle, including attachment, prefusion, triggering, recycling and reloading of the vesicles with transmitter.
sdb:0098 synaptic vesicle cycling  (Evidence:keywords)
interaction between synaptic vesicle and the scaffold.
sdb:0106 transport of synaptic vesicle in the presynaptic axon  (Evidence:keywords)
priming for exocytosis prepares the calcium-dependent release and may involve partial fusion process. The vesicles are primed and become responsive to calcium.
sdb:0120 priming  (Evidence:keywords)
attachment of the vesicle filled with transmitters involves a specific interaction between the vesicle membrane and the presynaptic active zone.
sdb:0148 docking  (Evidence:keywords)
?
sdb:0329 actin in synaptic vesicle cycling  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 34 residues, 27001144-27001244Exon2: 20 residues, 27075247-27075301Exon3: 332 residues, 27133339-27134330Exon4: 29 residues, 27154415-27154496Exon5: 14 residues, 27155549-27155586Exon6: 50 residues, 27172569-27172715Exon7: 14 residues, 27173772-27173808Exon8: 31 residues, 27177984-27178071Exon9: 64 residues, 27181093-27181279Exon10: 62 residues, 27184873-27185053Exon11: 73 residues, 27186101-27186314Exon12: 42 residues, 27187764-27187884Exon13: 49 residues, 27193370-27193511Exon14: 418 residues, 27196556-27197806Exon15: 2 residues, -Jump to APBA2_HUMAN  
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