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0EP15_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionEpidermal growth factor receptor substrate 15 (protein eps15) (af-1p protein).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005905 coated pit (TAS)
0008283 cell proliferation (TAS)
0007173 epidermal growth factor receptor signaling ... (TAS)
0016050 vesicle organization and biogenesis (TAS)

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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)
This domain consists of a duplication of two EF-hand 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
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
The Prefoldin/GimC family of proteins are found in eukaryotes and archaea . Prefoldin is part of a molecular chaperone system that promotes the correct folding of nascent polypeptide chains. Prefoldin/GimC interacts with the nascent chain to stabilise it prior to its folding within the central cavity of a chaperonin. Prefoldin/GimC is a hexamer consisting of two types of subunits.lpha and beta. Archaeal prefoldin contains one type of alpha and one type of beta subunit .hile eukaryotic prefoldin/GimC contains two different but related alpha subunits and four related beta subunits .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
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
SequencesProtein: EP15_HUMAN (896 aa)
mRNA: NM_001981
Local Annotation
Synapse Ontology
transport of vesicles in the presynaptic neuron
sdb:0017 Mobilization: synapsins, CAM kinase I  (Evidence:keywords)
endocytosis may be initiated or blocked by all kinds of signal.
sdb:0257 regulation of endocytosis  (Evidence:keywords)
sdb:0329 actin in synaptic vesicle cycling  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 862 residues, 51592523-51595106Exon2: 63 residues, 51599430-51599615Exon3: 56 residues, 51602125-51602288Exon4: 27 residues, 51604212-51604289Exon5: 24 residues, 51632640-51632707Exon6: 46 residues, 51637291-51637425Exon7: 14 residues, 51639177-51639213Exon8: 32 residues, 51640694-51640785Exon9: 40 residues, 51641678-51641792Exon10: 70 residues, 51644164-51644368Exon11: 68 residues, 51646394-51646592Exon12: 56 residues, 51647794-51647956Exon13: 26 residues, 51660045-51660118Exon14: 30 residues, 51678606-51678692Exon15: 54 residues, 51683148-51683305Exon16: 50 residues, 51685219-51685365Exon17: 32 residues, 51686305-51686395Exon18: 22 residues, 51699350-51699410Exon19: 44 residues, 51701932-51702058Exon20: 24 residues, 51703520-51703586Exon21: 34 residues, 51706732-51706828Exon22: 18 residues, 51709949-51709997Exon23: 32 residues, 51711118-51711208Exon24: 16 residues, 51719532-51719574Exon25: 43 residues, 51757458-51757583Exon26: 2 residues, -Jump to EP15_HUMAN  
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