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0EHD1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionEh-domain containing protein 1 (testilin) (hpast1).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005515 protein binding (IPI)
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)
Membrane transport between compartments in eukaryotic cells requires proteins that allow the budding and scission of nascent cargo vesicles from one compartment and their targeting and fusion with another. Dynamins are large GTPases that belong to a protein superfamily that.n eukaryotic cells.ncludes classical dynamins.ynamin-like proteins.PA1.x proteins.itofusins and guanylate-binding proteins/atlastins and are involved in the scission of a wide range of vesicles and organelles. They play a role in many processes including budding of transport vesicles.ivision of organelles.ytokinesis and pathogen resistance. The minimal distinguishing architectural features that are common to all dynamins and are distinct from other GTPases are the structure of the large GTPase domain (300 amino acids) and the presence of two additional domains; the middle domain and the GTPase effector domain (GED).hich are involved in oligomerization and regulation of the GTPase activity. The GTPase domain contains the GTP-binding motifs that are needed for guanine-nucleotide binding and hydrolysis. The conservation of these motifs is absolute except for the the final motif in guanylate-binding proteins. The GTPase catalytic activity can be stimulated by oligomerisation of the protein.hich is mediated by interactions between the GTPase domain.he middle domain and the GED.
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 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
SequencesProtein: EHD1_HUMAN (534 aa)
mRNA: AY007161 NM_006795
Local Annotation
Synapse Ontology
endosome of the presynaptic compartment. A cellular structure that is involved in the transport of proteins in the neuron after the proteins are endocytosed from the outside to the inside of the cell.
sdb:0088 endosome  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 119 residues, 64376783-64377137Exon2: 169 residues, 64378402-64378905Exon3: 57 residues, 64379369-64379534Exon4: 139 residues, 64383971-64384384Exon5: 34 residues, 64398468-64398566Exon6: 153 residues, 64402108-64402563Exon7: 2 residues, -Jump to EHD1_HUMANExon1: 708 residues, 64376783-64378905Exon2: 57 residues, 64379369-64379534Exon3: 139 residues, 64383971-64384384Exon4: 34 residues, 64398468-64398566Exon5: 221 residues, 64402108-64402767Exon6: 2 residues, -Jump to EHD1_HUMAN  
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Loci Cluster (Details)Loci: 2672 63498654-63500590 ~-2K 6992(COX8A)(+)Loci: 2673 63758841-63762834 ~-4K 7008(VEGFB)(+)Loci: 2674 63775570-63791969 ~-16K 7011(PLCB3)(+)Loci: 2675 63883200-63896262 ~-13K 7031(RPS6KA4)(+)Loci: 3958 64130223-64247236 ~-117K 7042(NRXN2)(-)Loci: 3959 64376783-64402767 ~-26K 7059(EHD1)(-)Loci: 2676 64551485-64564618 ~-13K 7071(SNX15)(+)Loci: 2677 64635935-64640274 ~-4K 7081(TM7SF2)(+)Loci: 2678 64705918-64736052 ~-30K 7088(CAPN1)(+)Loci: 2679 65049159-65062750 ~-14K 7102(+)Loci: 3960 65121802-65138296 ~-16K 7115(MAP3K11)(-)Loci: 3961 65407787-65412586 ~-5K 7136(FIBP)(-)Loci: 3962 65416267-65424573 ~-8K 7139(FOSL1)(-)Loci: 2680 65594399-65768789 ~-174K 7153(PACS1)(+)Loci: 2681 65792680-65801537 ~-9K 7155(RAB1B)(+)Loci: 2682 65815916-65820707 ~-5K 7159(+)Loci: 3963 65856117-65860576 ~-4K 7162(RIN1)(-)Loci: 2683 66140672-66151387 ~-11K 7189(RBM14)(+)Loci: 2684 66162753-66170514 ~-8K 7192(RBM4)(+)Loci: 3964 66209298-66245446 ~-36K 7194(SPTBN2)(-)Loci: 3965 66372572-66478456 ~-106K 7198(PC)(-)Loci: 2685 66547466-66574905 ~-27K 7200(SYT12)(+)Loci: 2686 66580896-66596059 ~-15K 7201(RHOD)(+)Loci: 3966 66922227-66925952 ~-4K 7219(PPP1CA)(-)Loci: 2687 66979393-66983261 ~-4K 7229(CABP4)(+)Loci: 2688 67130982-67136581 ~-6K 7239(NDUFV1)(+)Loci: 2689 67554684-67560690 ~-6K 7248(NDUFS8)(+)Loci: 2690 67836710-67973317 ~-137K 7259(LRP5)(+)Loci: 2671 63412650-63433621 ~-21K 6988(MARK2)(+)Link out to UCSC