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0LAP2_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameERBB2IP
DescriptionLap2 protein (erbb2-interacting protein) (erbin) (densin-180-like protein).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0009925 basal plasma membrane (NAS)
0005737 cytoplasm (IDA)
0030056 hemidesmosome (IDA)
0005634 nucleus (IDA)
0005176 ErbB-2 class receptor binding (TAS)
0005178 integrin binding (IPI)
0005515 protein binding (IPI)
0005200 structural constituent of cytoskeleton (NAS)
0045175 basal protein localization (NAS)
0007155 cell adhesion (NAS)
0007049 cell cycle (NAS)
0016049 cell growth (NAS)
0007173 epidermal growth factor receptor signaling ... (TAS)
0045197 establishment and/or maintenance of epithel... (NAS)
0007229 integrin-mediated signaling pathway (NAS)
0045104 intermediate filament cytoskeleton organiza... (NAS)

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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:
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 µM. 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
Leucine-rich repeats (LRR) consist of 2-45 motifs of 20-30 amino acids in length that generally folds into an arc or horseshoe shape . LRRs occur in proteins ranging from viruses to eukaryotes.nd appear to provide a structural framework for the formation of protein-protein interactions . Proteins containing LRRs include tyrosine kinase receptors.ell-adhesion molecules.irulence factors.nd extracellular matrix-binding glycoproteins.nd are involved in a variety of biological processes.ncluding signal transduction.ell adhesion.NA repair.ecombination.ranscription.NA processing.isease resistance.poptosis.nd the immune response.Sequence analyses of LRR proteins suggested the existence of several different subfamilies of LRRs. The significance of this classification is that repeats from different subfamilies never occur simultaneously and have most probably evolved independently. It is.owever.ow clear that all major classes of LRR have curved horseshoe structures with a parallel beta sheet on the concave side and mostly helical elements on the convex side. At least six families of LRR proteins.haracterized by different lengths and consensus sequences of the repeats.ave been identified. Eleven-residue segments of the LRRs (LxxLxLxxN/CxL).orresponding to the ß-strand and adjacent loop regions.re conserved in LRR proteins.hereas the remaining parts of the repeats (herein termed variable) may be very different. Despite the differences.ach of the variable parts contains two half-turns at both ends and a "linear" segment (as the chain follows a linear path overall).sually formed by a helix.n the middle. The concave face and the adjacent loops are the most common protein interaction surfaces on LRR proteins. 3D structure of some LRR proteins-ligand complexes show that the concave surface of LRR domain is ideal for interaction with alpha-helix.hus supporting earlier conclusions that the elongated and curved LRR structure provides an outstanding framework for achieving diverse protein-protein interactions . Molecular modeling suggests that the conserved pattern LxxLxL.hich is shorter than the previously proposed LxxLxLxxN/CxL is sufficient to impart the characteristic horseshoe curvature to proteins with 20- to 30-residue repeats .
  IPR001611:Leucine-rich repeat
IPR001478:PDZ 
Evalue:-16.397940008672 
Location:1330-1410IPR001611:LRR_1 
Evalue:-2.28399658203125 
Location:369-390IPR001611:LRR_1 
Evalue:-1.88605666160583 
Location:93-114IPR001611:LRR_1 
Evalue:-1.6020599603653 
Location:47-68IPR001611:LRR_1 
Evalue:-1.32790219783783 
Location:185-206IPR001611:LRR_1 
Evalue:-1.26760625839233 
Location:70-91IPR001611:LEURICHRPT 
Evalue:0 
Location:232-245IPR001611:LRR_1 
Evalue:0.278753608465195 
Location:254-275IPR001611:LRR_1 
Evalue:0.431363761425018 
Location:346-367IPR001611:LRR_1 
Evalue:0.462397992610931 
Location:139-160IPR001611:LRR_1 
Evalue:0.477121263742447 
Location:300-321IPR001611:LRR_1 
Evalue:0.491361707448959 
Location:162-183IPR001611:LRR_1 
Evalue:0.724275887012482 
Location:277-298
SequencesProtein: LAP2_HUMAN (1412 aa)
mRNA: AF276423 NM_018695
Local Annotation
Synapse Ontology
Any process that modulates the physical form of a synapse, the junction between a neuron and a target (neuron, muscle, or secretory cell).
sdb:0033 regulation of synapse structure  (Evidence:keywords)
intermediate filaments of the presynaptic compartments. Both microtubles and intermediate filaments represent the main structural scaffold of axons.
sdb:0086 intermediate filaments  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 84 residues, 65258139-65258390Exon2: 18 residues, 65320218-65320266Exon3: 68 residues, 65324293-65324491Exon4: 41 residues, 65326330-65326448Exon5: 28 residues, 65343632-65343711Exon6: 32 residues, 65345132-65345222Exon7: 21 residues, 65346252-65346309Exon8: 23 residues, 65352905-65352969Exon9: 27 residues, 65354873-65354948Exon10: 50 residues, 65355889-65356034Exon11: 26 residues, 65357063-65357136Exon12: 45 residues, 65357431-65357561Exon13: 40 residues, 65357885-65358001Exon14: 25 residues, 65359857-65359927Exon15: 35 residues, 65369966-65370066Exon16: 42 residues, 65374660-65374782Exon17: 60 residues, 65375720-65375894Exon18: 64 residues, 65377936-65378122Exon19: 40 residues, 65380250-65380365Exon20: 63 residues, 65382366-65382550Exon21: 517 residues, 65384989-65386535Exon22: 71 residues, 65406607-65406814Exon23: 33 residues, 65407899-65407992Exon24: 27 residues, 65408458-65408533Exon25: 868 residues, 65410006-65412606Exon26: 2 residues, -Jump to LAP2_HUMANExon1: 29 residues, 65258304-65258390Exon2: 18 residues, 65320218-65320266Exon3: 68 residues, 65324293-65324491Exon4: 41 residues, 65326330-65326448Exon5: 28 residues, 65343632-65343711Exon6: 32 residues, 65345132-65345222Exon7: 21 residues, 65346252-65346309Exon8: 23 residues, 65352905-65352969Exon9: 27 residues, 65354873-65354948Exon10: 50 residues, 65355889-65356034Exon11: 26 residues, 65357063-65357136Exon12: 45 residues, 65357431-65357561Exon13: 40 residues, 65357885-65358001Exon14: 25 residues, 65359857-65359927Exon15: 35 residues, 65369966-65370066Exon16: 42 residues, 65374660-65374782Exon17: 60 residues, 65375720-65375894Exon18: 64 residues, 65377936-65378122Exon19: 40 residues, 65380250-65380365Exon20: 63 residues, 65382366-65382550Exon21: 517 residues, 65384989-65386535Exon22: 43 residues, 65403752-65403875Exon23: 71 residues, 65406607-65406814Exon24: 33 residues, 65407899-65407992Exon25: 27 residues, 65408458-65408533Exon26: 509 residues, 65410006-65411529Exon27: 2 residues, -Jump to LAP2_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3457 65053840-65155143 ~-101K 28898(NLN)(+)Loci: 3458 65258139-65412606 ~-154K 28902(ERBB2IP)(+)Loci: 3459 65489710-65512393 ~-23K 28906(SFRS12)(+)Loci: 4715 64921264-64955943 ~-35K 28891(TRIM23)(-)Link out to UCSC