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0DNMBP_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameDNMBP
DescriptionDynamin-binding protein (scaffold protein tuba).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GON/A
Domain Architecture (Details)
InterPro domains assigned to SynO:
Endocytosis and intracellular transport involve several mechanistic steps: (1) for the internalisation of cargo molecules.he membrane needs to bend to form a vesicular structure.hich requires membrane curvature and a rearrangement of the cytoskeleton; (2) following its formation.he vesicle has to be pinched off the membrane; (3) the cargo has to be subsequently transported through the cell and the vesicle must fuse with the correct cellular compartment.Members of the Amphiphysin protein family are key regulators in the early steps of endocytosis.nvolved in the formation of clathrin-coated vesicles by promoting the assembly of a protein complex at the plasma membrane and directly assist in the induction of the high curvature of the membrane at the neck of the vesicle. Amphiphysins contain a characteristic domain.nown as the BAR (BinAmphiphysinRvs)-domain.hich is required for their in vivo function and their ability to tubulate membranes . The crystal structure of these proteins suggest the domain forms a crescent-shaped dimer of a three-helix coiled coil with a characteristic set of conserved hydrophobic.romatic and hydrophilic amino acids. Proteins containing this domain have been shown to homodimerise.eterodimerise or.n a few cases.nteract with small GTPases.
  IPR004148:BAR
InterPro domains unassigned to SynO:
SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organisation. These were first described in the Src cytoplasmic tyrosine kinase . The structure is a partly opened beta barrel.
  IPR011511:Variant SH3
Phagocytes form the first line of defence against invasion by micro-organisms. Engulfing of bacteria by neutrophils is accompanied by theconsumption of large amounts of oxygen - a so-called respiratory burst.Defects in phagocytosis involving the lack of a respiratory burst giverise to chronic granulomatous disease (CGD).n which patients are pre-disposed to infection.ften from otherwise non-pathogenic bacteria .Regulation of the respiratory burst takes place at the phagocytic vacuole.The process is mediated by NADPH oxidase.hich transports electrons acrossthe plasma membrane to form superoxide (an oxygen molecule with an extraelectron that is toxic to normal cells) in the vacuole interior. Theelectrons are carried across the membrane by a short electron transportchain in the form of an unusual flavocytochrome b .To conserve NADPH and avoid the toxic effects of superoxide.he oxidase remains inactive until it receives an appropriate stimulus. Activationinvolves the participation of a number of cytosolic proteins.ome of which attach to the flavocytochrome. P47phox.67phox and p40phox arespecialised components of phagocytic cells.ll of which contain SH3domains .y means of which they attach to proline-rich regions of otherproteins. Upon activation.47phox and p67phox are phosphorylated and.ith p40phox.ranslocate to the region of the plasma membrane formingthe phagocytic vacuole.here they associates with hydrophilic regionsof the flavocytochrome .
  IPR000108:Neutrophil cytosol factor 2
The Rho family GTPases Rho.ac and CDC42 regulate a diverse array of cellularprocesses. Like all members of the Ras superfamily.he Rho proteins cycle between active GTP-bound and inactive GDP-bound conformational states.Activation of Rho proteins through release of bound GDP and subsequentbinding of GTP.s catalyzed by guanine nucleotide exchange factors (GEFs) inthe Dbl family. The proteins encoded by members of the Dbl family share acommon domain.resented in this entry.f about 200 residues (designated the Dbl homology or DH domain)that has been shown to encode a GEF activity specific for a number of Rhofamily members. In addition.ll family members possess a second.hareddomain designated the pleckstrin homology (PH) domain (). Trioand its homolog UNC-73 are unique within the Dbl family insomuch as theyencode two distinct DH/PH domain modules. The PH domain is invariably locatedimmediately C-terminal to the DH domain and this invariant topography suggestsa functional interdependence between these two structural modules. Biochemicaldata have established the role of the conserved DH domain in Rho GTPaseinteraction and activation.nd the role of the tandem PH domain inintracellular targeting and/or regulation of DH domain function. The DH domainof Dbl has been shown to mediate oligomerization that is mostly homophilic innature. In addition to the tandem DH/PH domains Dbl family GEFs containdiverse structural motifs like serine/threonine kinase.BD.DZ.GS.Q.EM.dc25RasGEF.H.H2.H3.F.pectrin or Ig.The DH domain is composed of three structurally conserved regions separated bymore variable regions. It does not share significant sequence homology withother subtypes of small G-protein GEF motifs such as the Cdc25 domain and theSec7 domain.hich specifically interact with Ras and ARFfamily small GTPases.espectively.or with other Rho protein interactivemotifs.ndicating that the Dbl family proteins are evolutionarily unique. TheDH domain is composed of 11 alpha helices that are folded into a flattened.longated alpha-helix bundle in which two of the three conserved regions.onserved region 1 (CR1) and conserved region 3 (CR3).re exposed near thecenter of one surface. CR1 and CR3.ogether with a part of alpha-6 and theDH/PH junction site.onstitute the Rho GTPase interacting pocket.
  IPR000219:DH
SH3 (src Homology-3) domains are small protein modules containing approximately 50 amino acid residues . They are found in a great variety of intracellular or membrane-associated proteins for example.n a variety of proteins with enzymatic activity.n adaptor proteins that lack catalytic sequences and in cytoskeletal proteins.uch as fodrin and yeast actin binding protein ABP-1. The SH3 domain has a characteristic fold which consists of five or six beta-strands arranged as two tightly packed anti-parallel beta sheets. The linker regions may contain short helices . The surface of the SH2-domain bears a flat.ydrophobic ligand-binding pocket which consists of three shallow grooves defined by conservative aromatic residues in which the ligand adopts an extended left-handed helical arrangement. The ligand binds with low affinity but this may be enhanced by multiple interactions.The region bound by the SH3 domain is in all cases proline-rich and contains PXXP as a core-conserved binding motif. The function of the SH3 domain is not well understood but they may mediate many diverse processes such as increasing local concentration of proteins.ltering their subcellular location and mediating the assembly of large multiprotein complexes .
  IPR001452:Src homology-3
IPR004148:BAR 
Evalue:-73.5528411865234 
Location:997-1207IPR000219:RhoGEF 
Evalue:-35.5228787452803 
Location:788-966IPR001452:SH3 
Evalue:-15.1191864077192 
Location:246-301IPR001452:SH3 
Evalue:-14.8538719643218 
Location:148-203IPR001452:SH3_1 
Evalue:-13.3767509460449 
Location:5-59IPR001452:SH3 
Evalue:-13.0362121726544 
Location:1516-1575IPR011511:SH3_2 
Evalue:-7.43179845809936 
Location:1289-1346IPR011511:SH3_2 
Evalue:-6.38721609115601 
Location:70-124
SequencesProtein: DNMBP_HUMAN (1577 aa)
mRNA: AL833283
Local Annotation
Synapse Ontology
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)
actin exists in two states within the cell: as polymerized two-stranded helical filaments (F-actin) or as monomers (Gactin), which provide the building blocks for filament assembly.
sdb:0283 G-actin  (Evidence:keywords,domains)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 587 residues, 101625324-101627083Exon2: 185 residues, 101629557-101630108Exon3: 68 residues, 101633757-101633956Exon4: 62 residues, 101635433-101635613Exon5: 113 residues, 101636046-101636379Exon6: 45 residues, 101638571-101638700Exon7: 37 residues, 101644692-101644797Exon8: 45 residues, 101646013-101646144Exon9: 68 residues, 101647832-101648032Exon10: 8 residues, 101648489-101648507Exon11: 51 residues, 101649665-101649813Exon12: 35 residues, 101657741-101657841Exon13: 66 residues, 101658699-101658893Exon14: 666 residues, 101704960-101706952Exon15: 43 residues, 101718861-101718984Exon16: 53 residues, 101721726-101721881Exon17: 29 residues, 101759584-101759666Exon18: 2 residues, -Jump to DNMBP_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3916 101461595-101481890 ~-20K 5514(COX15)(-)Loci: 2628 101532562-101601571 ~-69K 5517(ABCC2)(+)Loci: 3917 101625324-101759666 ~-134K 5519(DNMBP)(-)Loci: 2629 102096761-102114577 ~-18K 5532(SCD)(+)Loci: 3918 102273487-102279626 ~-6K 5541(NDUFB8)(-)Loci: 3919 102727568-102737262 ~-10K 5557(MRPL43)(-)Loci: 3915 101146617-101180336 ~-34K 5507(GOT1)(-)Link out to UCSC