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0PICAL_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionPhosphatidylinositol-binding clathrin assembly protein (clathrin assembly lymphoid myeloid leukemia protein).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005905 coated pit (IDA)
0030276 clathrin binding (IDA)
0005545 phosphatidylinositol binding (ISS)
0006461 protein complex assembly (TAS)
0006898 receptor mediated endocytosis (IDA)
0016192 vesicle-mediated transport (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 assigned to SynO:
AP180 is an endocytotic accessory protein that has been implicated in the formation of clathrin-coated pits. The domain is involved in phosphatidylinositol 4.-bisphosphate binding and is a universal adaptor for nucleation of clathrin coats .
Clathrin-mediated endocytosis plays a major role in retrieving synaptic vesicles from the plasma membrane following exocytosis. This endocytic process requires the clathrin coat assembly protein AP180 (or a homologue).hich promotes the assembly and restricts the size of clathrin-coated vesicles. The highly conserved 33 kDa amino-terminal domain of AP180 plays a critical role in binding to phosphoinositides and in regulating the clathrin assembly activity of AP180. The crystal structure of the amino-terminal domain reveals a novel fold consisting of a large double layer of sheets of ten alpha helices and a unique site for binding phosphoinositides. The clathrin-box motif is mostly buried and lies in a helix that participates in an intramolecular leucine zipper and a three-helix coiled coil .
  IPR008943:Phosphoinositide-binding clathrin adaptor, N-terminal
InterPro domains unassigned to SynO:
The ENTH (Epsin N-terminal homology) domain is approximately 150 amino acids in length and is always found located at the N-termini of proteins. The domain forms a compact globular structure.omposed of 9 alpha-helices connected by loops of varying length. The general topology is determined by three helical hairpins that are stacked consecutively with a right hand twist . An N-terminal helix folds back.orming a deep basic groove thatforms the binding pocket for the Ins(1..)P3 ligand . The ligand is coordinated by residues from surrounding alpha-helices and all three phosphates are multiply coordinated. The coordination of Ins(1..)P3 suggests that ENTH is specific for particular head groups. Proteins containing this domain have been found to bind PtdIns(4.)P2 and PtdIns(1..)P3 suggesting that the domain may be a membrane interacting module. The main function of proteins containing this domain appears to be to act as accessory clathrin adaptors in endocytosis.psin is able to recruit and promote clathrin polymerisation ona lipid monolayer.ut may have additional roles in signalling and actin regulation . Epsin causes a strong degree of membrane curvature andtubulation.ven fragmentation of membranes with a high PtdIns(4.)P2 content. Epsin binding tomembranes facilitates their deformation by insertion of the N-terminal helix into the outer leaflet of the bilayer.ushing the head groupsapart. This would reduce the energy needed to curve the membrane into a vesicle.aking it easier for the clathrin cage tofix and stabilise the curved membrane. This points to a pioneering role for epsin in vesiclebudding as it provides both a driving force and a link between membrane invagination and clathrin polymerisation.
  IPR013809:Epsin-like, N-terminal
SequencesProtein: PICAL_HUMAN (652 aa)
mRNA: NM_007166
Local Annotation
Synapse Ontology
the clathrin located in the surface of the endocytotic intermediate.
sdb:0115 clathrin-coated pit  (Evidence:keywords,domains)
endocytotic reaction via coated pits
sdb:0119 endocytotic reaction  (Evidence:keywords,domains)
clathrin-coat uncoating means clathrin was shed from the budding vesicle membrane.
sdb:0122 clathrin-coat uncoating  (Evidence:keywords,domains)
the molecules that link the clathrin lattice to the membrane.
sdb:0259 clathrin adapter  (Evidence:keywords,domains)
sdb:0260 coat recruitment  (Evidence:keywords,domains)
the generation of action potential at soma of neurons.
sdb:0313 generation of AP at soma  (Evidence:keywords,domains)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 540 residues, 85346133-85347751Exon2: 37 residues, 85363398-85363503Exon3: 22 residues, 85365313-85365373Exon4: 35 residues, 85369819-85369919Exon5: 12 residues, 85370435-85370466Exon6: 46 residues, 85370562-85370694Exon7: 38 residues, 85372556-85372664Exon8: 52 residues, 85378940-85379090Exon9: 36 residues, 85385516-85385620Exon10: 47 residues, 85389333-85389470Exon11: 43 residues, 85389725-85389849Exon12: 30 residues, 85392056-85392142Exon13: 16 residues, 85396232-85396274Exon14: 37 residues, 85399720-85399827Exon15: 39 residues, 85400971-85401083Exon16: 33 residues, 85403560-85403654Exon17: 36 residues, 85411057-85411160Exon18: 27 residues, 85414981-85415057Exon19: 49 residues, 85420158-85420301Exon20: 140 residues, 85457340-85457756Exon21: 2 residues, -Jump to PICAL_HUMAN  
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Loci Cluster (Details)Loci: 3981 85346133-85457756 ~-112K 7529(PICALM)(-)Loci: 3980 85082914-85146692 ~-64K 7513(SYTL2)(-)Link out to UCSC