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0EPN1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameEPN1
DescriptionEpsin-1 (eps-15 interacting protein 1) (eh domain-binding mitotic phosphoprotein).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0006897 endocytosis (TAS)
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 Ubiquitin Interacting Motif (UIM) was first described in the 26S proteasome subunit PSD4/RPN-10 . It is known to bind multiple ubiquitin and was also found in many proteins involved in the endocytic pathway.ncludingthe PSD4/RPN-10/S5a multiubiquitin binding subunit of the 26S proteasome; the VPS27 vacuolar sorting protein; and ataxin-3. protein involved in ataxia disease.
  IPR003903:Ubiquitin interacting motif
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:-81.3767471313477 
Location:17-140IPR003903:UIM 
Evalue:-3.21467018127441 
Location:182-199IPR003903:UIM 
Evalue:-0.275724130399211 
Location:208-227
SequencesProtein: EPN1_HUMAN (551 aa)
mRNA: AF073727 AK022454 NM_013333
Local Annotation
Synapse Ontology
introduce the substructure of the synapse and the location where the molecule can be seen. It will contain all the constructive special organelle and molecule we known.
sdb:0001 Structure/Biochemistry of synapse  (Evidence:keywords,domains)
all
sdb:0004 Presynaptic compartment  (Evidence:keywords,domains)
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)
endocytosis may be initiated or blocked by all kinds of signal.
sdb:0257 regulation of endocytosis  (Evidence:keywords,domains)
the molecules that link the clathrin lattice to the membrane.
sdb:0259 clathrin adapter  (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: 71 residues, 60878403-60878613Exon2: 111 residues, 60881704-60882033Exon3: 85 residues, 60888573-60888823Exon4: 43 residues, 60892047-60892172Exon5: 27 residues, 60892474-60892549Exon6: 30 residues, 60893044-60893128Exon7: 103 residues, 60894931-60895235Exon8: 39 residues, 60895863-60895974Exon9: 31 residues, 60896128-60896215Exon10: 88 residues, 60897903-60898161Exon11: 208 residues, 60898325-60898944Exon12: 2 residues, -Jump to EPN1_HUMANExon1: 71 residues, 60878403-60878613Exon2: 111 residues, 60881704-60882033Exon3: 85 residues, 60888573-60888823Exon4: 43 residues, 60892047-60892172Exon5: 30 residues, 60893044-60893128Exon6: 103 residues, 60894931-60895235Exon7: 39 residues, 60895863-60895974Exon8: 30 residues, 60896131-60896215Exon9: 88 residues, 60897903-60898161Exon10: 208 residues, 60898325-60898944Exon11: 2 residues, -Jump to EPN1_HUMANExon1: 199 residues, 60879802-60880396Exon2: 63 residues, 60880727-60880912Exon3: 111 residues, 60881704-60882033Exon4: 85 residues, 60888573-60888823Exon5: 43 residues, 60892047-60892172Exon6: 30 residues, 60893044-60893128Exon7: 103 residues, 60894931-60895235Exon8: 39 residues, 60895863-60895974Exon9: 31 residues, 60896128-60896215Exon10: 88 residues, 60897903-60898161Exon11: 100 residues, 60898325-60898619Exon12: 2 residues, -Jump to EPN1_HUMAN  
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Loci Cluster (Details)Loci: 4417 60376280-60382727 ~-6K 19696(SYT5)(-)Loci: 4418 60558092-60566432 ~-8K 19713(C19orf16)(-)Loci: 3140 60878403-60898944 ~-21K 19736(EPN1)(+)Loci: 3139 60109319-60119319 ~-10K 19661(NCR1)(+)Link out to UCSC