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0DYN3_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionDynamin-3 (ec (dynamin, testicular) (t-dynamin).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Dynamin is a microtubule-associated force-producing protein of 100 Kdwhich is involved in the production of microtubule bundles. At the N terminus ofdynamin is a GTPase domain (see ).nd at the C-terminus is a PH domain (see ).Between these two domains lies a central region of unknown function.
  IPR000375:Dynamin central region
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.
Pleckstrin homology (PH) domains are small modular domains that occur once.r occasionally several times.n a large variety of signalling they serve as simple targeting domains that recognize only phosphoinositide headgroups . PH domains can target their host protein to the plasma and internal membranes through its association with phosphoinositides. PH domains have a partly opened beta-barrel topology that is capped by an alpha helix. Proteins containing PH domains include pleckstrin (N-terminal).hospholipase C and Rac-alpha kinase.The structure of PH domains is similar to the phosphotyrosine-binding domain (PTB) found in IRS-1 (insulin receptor substrate 1).hc adaptor and Numb; to the Ran-binding domain.ound in Nup nuclear pore complex and Ranbp1; to the Enabled/VASP homology domain 1 (EVH1 domain).ound in Enabled.ASP (vasodilator-stimulated phosphoprotein).omer and WASP actin regulatory protein; to the third domain of FERM.ound in moesin.adixin.zrin.erlin and talin; and to the PH-like domain of neurobeachin.
  IPR011993:Pleckstrin homology-type
Dynamin GTPase effector domain found in proteins related to dynamin. Dynamin is a GTP-hydrolysing protein that is an essential participant in clathrin-mediated endocytosis by cells. It self-assembles into collars in vivo at the necks of invaginated coated pits; the self-assembly of dynamin being coordinated by the GTPase domain. Mutation studies indicate that dynamin functions as a molecular regulator of receptor-mediated endocytosis .
  IPR003130:Dynamin GTPase effector
The pleckstrin homology (PH) domain is a domain of about 100 residues that occurs in a wide range of proteins involved in intracellular signaling or as constituents of the cytoskeleton .The function of this domain is not clear.everal putative functions have been suggested:binding to the beta/gamma subunit of heterotrimeric G proteins.inding to lipids..g. phosphatidylinositol-4.-bisphosphate.inding to phosphorylated Ser/Thr residues.ttachment to membranes by an unknown mechanism.It is possible that different PH domains have totally different ligand requirements.The 3D structure of several PH domains has been determined . All known cases have a common structure consisting of two perpendicular anti-parallel beta sheets.ollowed by a C-terminal amphipathic helix. The loops connecting the beta-strands differ greatly in length.aking the PH domain relatively difficult to detect. There are no totally invariant residues within the PH domain.Proteins reported to contain one more PH domains belong to the following families:Pleckstrin.he protein where this domain was first detected.s the major substrate of protein kinase C in platelets. Pleckstrin is one of the rare proteins to contains two PH domains.Ser/Thr protein kinases such as the Akt/Rac family.he beta-adrenergic receptor kinases.he mu isoform of PKC and the trypanosomal NrkA family.Tyrosine protein kinases belonging to the Btk/Itk/Tec subfamily.Insulin Receptor Substrate 1 (IRS-1).Regulators of small G-proteins like guanine nucleotide releasing factor GNRP (Ras-GRF) (which contains 2 PH domains).uanine nucleotide exchange proteins like and Saccharomyces cerevisiae CDC24.TPase activating proteins like rasGAP and BEM2/IPL2.nd the human break point cluster protein bcr.Cytoskeletal proteins such as dynamin (see ).aenorhabditis elegans kinesin-like protein unc-104 (see ).pectrin beta-chain.yntrophin (2 PH domains) and S. cerevisiae nuclear migration protein NUM1.Mammalian phosphatidylinositol-specific phospholipase C (PI-PLC) (see ) isoforms gamma and delta. Isoform gamma contains two PH domains.he second one is split into two parts separated by about 400 residues.Oxysterol binding proteins OSBP.. cerevisiae OSH1 and YHR073w.Mouse protein citron. putative rho/rac effector that binds to the GTP-bound forms of rho and rac.Several S. cerevisiae proteins involved in cell cycle regulation and bud formation like BEM2.EM3.UD4 and the BEM1-binding proteins BOI2 (BEB1) and BOI1 (BOB1).C. elegans protein MIG-10.C. elegans hypothetical proteins C04D8.1.06H7.4 and ZK632.12.S. cerevisiae hypothetical proteins YBR129c and YHR155w.
Ribosomes are the particles that catalyze mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This leads to the incorporation of amino acids into the growing polypeptide chain in accordance with the genetic information. Incoming amino acid monomers enter the ribosomal A site in the form of aminoacyl-tRNAs complexed with elongation factor Tu (EF-Tu) and GTP. The growing polypeptide chain.ituated in the P site as peptidyl-tRNA.s then transferred to aminoacyl-tRNA and the new peptidyl-tRNA.xtended by one residue.s translocated to the P site with the aid the elongation factor G (EF-G) and GTP as the deacylated tRNA is released from the ribosome through one or more exit sites . About 2/3 of the mass of the ribosome consists of RNA and 1/3 of protein. The proteins are named in accordance with the subunit of the ribosome which they belong to - the small (S1 to S31) and the large (L1 to L44). Usually they decorate the rRNA cores of the subunits. Many of ribosomal proteins.articularly those of the large composed of a globular.urfaced-exposed domain with long finger-like projections that extend into the rRNA core to stabilize its structure. Most of the proteins interact with multiple RNA elements.ften from different domains. In the large subunit.bout 1/3 of the 23S rRNA nucleotides are at least in van der Waals contact with protein.nd L22 interacts with all six domains of the 23S rRNA. Proteins S4 and S7.hich initiate assembly of the 16S located at junctions of five and four RNA helices.espectively. In this way proteins serve to organize and stabilize the rRNA tertiary structure. While the crucial activities of decoding and peptide transfer are RNA based.roteins play an active role in functions that may have evolved to streamline the process of protein synthesis. In addition to their function in the ribosome.any ribosomal proteins have some function outside the ribosome .Evidence suggests that.n prokaryotes.he peptidyl transferase reaction is performed by the large subunit 23S rRNA.hereas proteins probably have a greater role in eukaryotic ribosomes. Most of the proteins lie close to.r on the surface of.he 30S subunit.rranged peripherally around the rRNA . The small subunit ribosomal proteins can be categorised as primary binding proteins.hich bind directly and independently to 16S rRNA; secondary binding proteins.hich display no specific affinity for 16S rRNA.ut its assembly is contingent upon the presence of one or more primary binding proteins; and tertiary binding proteins.hich require the presence of one or more secondary binding proteins and sometimes other tertiary binding proteins.The small ribosomal subunit protein S10 consists of about 100 amino acid residues. In Escherichia coli.10 is involved in binding tRNA to the ribosome.nd also operates as a transcriptional elongation factor . Experimental evidence has revealed that S10 has virtually no groups exposed on the ribosomal surface.nd is one of the "split proteins": these are a discrete group that are selectively removed from 30S subunits under low salt conditions and are required for the formation of activated 30S reconstitution intermediate (RI*) particles. S10 belongs to a family of proteins that includes: bacteria S10; algal chloroplast S10; cyanelle S10; archaebacterial S10; Marchantia polymorpha and Prototheca wickerhamii mitochondrial S10; Arabidopsis thaliana mitochondrial S10 (nuclear encoded); vertebrate S20; plant S20; and yeast URP2.
  IPR001848:Ribosomal protein S10
Protein kinases () catalyze the phosphotransfer reaction fundamental to most signalling and regulatory processes in the eukaryotic cell . The catalytic subunit contains a core that is common to both serine/threonine and tyrosine protein kinases. The catalytic domain contains the nucleotide-binding site and the catalytic apparatus in an inter-lobe cleft. Structurally it shares functional and structural similarities with the ATP-grasp fold.hich is found in enzymes that catalyse the formation of an amide bond.nd with PIPK (phosphoinositol phosphate kinase). The three-dimensional fold of the protein kinase catalytic domain is similar to domains found in several other proteins. These include the catalytic domain of actin-fragmin kinase.n atypical protein kinase that regulates the F-actin capping activity in plasmodia ; the catalytic domain of phosphoinositide-3-kinase (PI3K).hich phosphorylates phosphoinositides and as such is involved in a number of fundamental cellular processes such as apoptosis.roliferation.otility and adhesion ; the catalytic domain of the MHCK/EF2 kinase.n atypical protein kinase that includes the TRP (transient channel potential) calcium-channel kinase involved in the modulation of calcium channels in eukaryotic cells in response to external signals ; choline kinase.hich catalyses the ATP-dependent phosphorylation of choline during the biosynthesis of phosphatidylcholine ; and 3.-aminoglycoside phosphotransferase type IIIa. bacterial enzyme that confers resistance to a range of aminoglycoside antibiotics .
  IPR011009:Protein kinase-like
SequencesProtein: DYN3_HUMAN (859 aa)
mRNA: AB020627 NM_015569
Local Annotation
Synapse Ontology
Postsynaptic compartment is represented by a patch of plasma membrane containing a packed array of neurotransmitter receptors and by an underlying dense matrix, the postsynaptic density (PSD).
sdb:0005 Postsynaptic compartment  (Evidence:keywords)
endocytosis may be initiated or blocked by all kinds of signal.
sdb:0257 regulation of endocytosis  (Evidence:keywords)
the cycle of the clathrin coat
sdb:0258 The cycle of the clathrin coat  (Evidence:keywords)
sdb:0328 transmitters release and endocytosis  (Evidence:keywords)
KO assignmentK01528
  Level 3 annotation:
    dynamin GTPase
  Level 2 annotation:
    Other enzymes
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 107 residues, 170077260-170077580Exon2: 26 residues, 170157510-170157584Exon3: 52 residues, 170223418-170223568Exon4: 70 residues, 170224707-170224911Exon5: 35 residues, 170268164-170268263Exon6: 55 residues, 170268867-170269028Exon7: 49 residues, 170274081-170274224Exon8: 47 residues, 170277771-170277907Exon9: 24 residues, 170280147-170280215Exon10: 48 residues, 170284374-170284513Exon11: 31 residues, 170304581-170304668Exon12: 25 residues, 170317594-170317665Exon13: 19 residues, 170328586-170328638Exon14: 40 residues, 170366937-170367051Exon15: 38 residues, 170489335-170489445Exon16: 39 residues, 170544490-170544602Exon17: 6 residues, 170559091-170559103Exon18: 57 residues, 170614780-170614945Exon19: 77 residues, 170622895-170623122Exon20: 81 residues, 170624335-170624572Exon21: 1650 residues, 170643534-170648479Exon22: 2 residues, -Jump to DYN3_HUMANExon1: 98 residues, 170077289-170077580Exon2: 26 residues, 170157510-170157584Exon3: 52 residues, 170223418-170223568Exon4: 70 residues, 170224707-170224911Exon5: 35 residues, 170268164-170268263Exon6: 55 residues, 170268867-170269028Exon7: 49 residues, 170274081-170274224Exon8: 47 residues, 170277771-170277907Exon9: 24 residues, 170280147-170280215Exon10: 48 residues, 170284374-170284513Exon11: 31 residues, 170304581-170304668Exon12: 25 residues, 170317594-170317665Exon13: 19 residues, 170328586-170328638Exon14: 40 residues, 170366937-170367051Exon15: 38 residues, 170489335-170489445Exon16: 39 residues, 170544490-170544602Exon17: 57 residues, 170614780-170614945Exon18: 77 residues, 170622895-170623122Exon19: 81 residues, 170624335-170624572Exon20: 1257 residues, 170643534-170647301Exon21: 2 residues, -Jump to DYN3_HUMAN  
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