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0EP15R_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameEPS15L1
DescriptionEpidermal growth factor receptor substrate 15-like 1 (eps15-related protein) (eps15r).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GON/A
Domain Architecture (Details)
InterPro domains unassigned to SynO:
The EH (for Eps15 Homology) domain is a protein-protein interaction module of approximately 95 residues which was originally identified as a repeated sequence present in three copies at the N-terminus of the tyrosine kinase substrates Eps15 and Eps15R . The EH domain was subsequently found in several proteins implicated in endocytosis.esicle transport and signal transduction in organisms ranging from yeast to mammals. EH domains are present in one to three copies and they may include calcium-binding domains of the EF-hand type . Eps15 is divided into three domains: domain I contains signatures of a regulatory domain.ncluding a candidate tyrosine phosphorylation site and EF-hand-type calcium-binding domains.omain II presents the characteristic heptad repeats of coiled-coil rod-like proteins.nd domain III displays a repeated aspartic acid-proline-phenylalanine motif similar to a consensus sequence of several methylases .EH domains have been shown to bind specifically but with moderate affinity to peptides containing short.nmodified motifs through predominantly hydrophobic interactions. The target motifs are divided into three classes: class I consists of the concensus Asn-Pro-Phe (NPF) sequence; class II consists of aromatic and hydrophobic di- and tripeptide motifs.ncluding the Phe-Trp (FW).rp-Trp (WW).nd Ser-Trp-Gly (SWG) motifs; and class III contains the His-(Thr/Ser)-Phe motif (HTF/HSF) . The structure of several EH domains has been solved by NMR spectroscopy. The fold consists of two helix-loop-helix characteristic of EF-hand domains.onnected by a short antiparallel beta-sheet. The target peptide is bound in a hydrophobic pocket between two alpha helices. Sequence analysis and structural data indicate that not all the EF-hands are capable of binding calcium because of substitutions of the calcium-liganding residues in the loop . This domain is often implicated in the regulation of protein transport/sorting and membrane trafficking. Messenger RNA translation initiation and cytoplasmic poly(A) tail shortening require the poly(A)-binding protein (PAB) in yeast. The PAB-dependent poly(A) ribonuclease (PAN) is organised into distinct domains containing repeated sequence elements .
  IPR000261:EPS15 homology (EH)
Many calcium-binding proteins belong to the same evolutionary family and share a type of calcium-binding domain known as the EF-hand. This type of domain consists of a twelve residue loop flanked on both side by a twelve residue alpha-helical domain. In an EF-hand loop the calcium ion is coordinated in a pentagonal bipyramidal configuration. The six residues involved in the binding are in positions 1.... and 12; these residues are denoted by X...Y.X and -Z. The invariant Glu or Asp at position 12 provides two oxygens for liganding Ca (bidentate ligand).
  IPR002048:Calcium-binding EF-hand
This domain consists of a duplication of two EF-hand units.here each unit is composed of two helices connected by a twelve-residue calcium-binding loop. The calcium ion in the EF-hand loop is coordinated in a pentagonal bipyramidal configuration. Many calcium-binding proteins contain an EF-hand type calcium-binding domain . These include: calbindin D9K.100 proteins such as calcyclin.olcalcin phl p 7 (a calcium-binding pollen allergen).steonectin.arvalbumin.almodulin family of proteins (troponin C.altractin.dc4p.yosin essential chain.alcineurin.ecoverin.eurocalcin).lasmodial-specific CaII-binding protein Cbp40.enta-EF-Hand proteins (sorcin.rancalcin.alpain).s well as multidomain proteins such as phosphoinositide-specific phospholipase C.ystrophin.b1 and alpha-actinin. The fold consists of four helices and an open array of two hairpins.
  IPR011992:EF-Hand type
IPR000261:EH 
Evalue:-46.4948500216801 
Location:120-214IPR000261:EH 
Evalue:-43.2839966563652 
Location:268-364IPR000261:EH 
Evalue:-19.0705810742857 
Location:8-103IPR000727:T_SNARE 
Evalue:0 
Location:0-0
SequencesProtein: EP15R_HUMAN (864 aa)
mRNA: NM_021235
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,domains)
the clathrin located in the surface of the endocytotic intermediate.
sdb:0115 clathrin-coated pit  (Evidence:keywords,domains)
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,domains)
all the components of the clathrin coat, major ones are clathrin and clathrin adaptors.
sdb:0261 clathrin coat component  (Evidence:keywords,domains)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 130 residues, 16333407-16333795Exon2: 46 residues, 16348932-16349065Exon3: 29 residues, 16356939-16357022Exon4: 22 residues, 16357981-16358042Exon5: 47 residues, 16364114-16364251Exon6: 19 residues, 16365761-16365812Exon7: 43 residues, 16367154-16367278Exon8: 57 residues, 16374131-16374296Exon9: 68 residues, 16375543-16375741Exon10: 56 residues, 16376398-16376560Exon11: 26 residues, 16385583-16385656Exon12: 30 residues, 16389362-16389448Exon13: 54 residues, 16389758-16389915Exon14: 54 residues, 16393129-16393287Exon15: 80 residues, 16396893-16397127Exon16: 22 residues, 16400512-16400572Exon17: 44 residues, 16406175-16406301Exon18: 23 residues, 16408747-16408810Exon19: 34 residues, 16409580-16409676Exon20: 18 residues, 16412672-16412720Exon21: 32 residues, 16413702-16413792Exon22: 16 residues, 16413988-16414030Exon23: 15 residues, 16443723-16443762Exon24: 2 residues, -Jump to EP15R_HUMAN  
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Loci Cluster (Details)Loci: 4372 14380630-14391171 ~-11K 18171(DDX39)(-)Loci: 3093 14430110-14443670 ~-14K 18178(+)Loci: 4373 14852137-14853264 ~-1K 18201(-)Loci: 4374 14921990-14944730 ~-23K 18203(SLC1A6)(-)Loci: 4375 15325340-15351603 ~-26K 18217(AKAP8)(-)Loci: 4376 15351858-15390833 ~-39K 18218(AKAP8L)(-)Loci: 3094 15699833-15700862 ~-1K 18230(OR10H2)(+)Loci: 4377 15778890-15779847 ~-1K 18231(OR10H1)(-)Loci: 3095 16083489-16105443 ~-22K 18238(RAB8A)(+)Loci: 3096 16169730-16207156 ~-37K 18242(AP1M1)(+)Loci: 4378 16333407-16443762 ~-110K 18245(EPS15L1)(-)Loci: 4371 14119550-14177997 ~-58K 18165(LPHN1)(-)Link out to UCSC