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1Q8IYW4_HUMAN*   Trembl (?) | Description Local Annotation Link Reference
General Information
NameN/A
DescriptionHypothetical protein flj25421 (dj172b20.3 protein).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GON/A
Domain Architecture (Details)
InterPro domains assigned to SynO:
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.
  IPR001026:Epsin, N-terminal
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
IPR001026:ENTH 
Evalue:-65.0315170288086 
Location:14-137
SequencesProtein: Q8IYW4_HUMAN (607 aa)
mRNA: NM_152512
Local Annotation
Synapse Ontology
endocytotic reaction via coated pits
sdb:0119 endocytotic reaction  (Evidence:domains)
clathrin-coat uncoating means clathrin was shed from the budding vesicle membrane.
sdb:0122 clathrin-coat uncoating  (Evidence:domains)
the molecules that link the clathrin lattice to the membrane.
sdb:0259 clathrin adapter  (Evidence:domains)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 414 residues, 38468995-38470234Exon2: 131 residues, 38491173-38491560Exon3: 42 residues, 38546943-38547064Exon4: 41 residues, 38561790-38561909Exon5: 83 residues, 38587715-38587958Exon6: 170 residues, 38613349-38613853Exon7: 34 residues, 38619644-38619740Exon8: 2 residues, -Jump to Q8IYW4_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3318 38075899-38111525 ~-36K 24775(SYNGR1)(+)Loci: 3319 38296703-38415684 ~-119K 24788(CACNA1I)(+)Loci: 4573 38468995-38619740 ~-151K 24792(-)Loci: 4572 37949664-37970936 ~-21K 24769(PDGFB)(-)Link out to UCSC