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0PLD1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NamePLD1
DescriptionPhospholipase d1 (ec 3.1.4.4) (pld 1) (choline phosphatase 1) (phosphatidylcholine-hydrolyzing phospholipase d1) (hpld1).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0016020 membrane (TAS)
0004630 phospholipase D activity (TAS)
0006935 chemotaxis (TAS)
0007265 Ras protein signal transduction (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
The PX (phox) domain occurs in a variety of eukaryotic proteins and have been implicated in highly diverse functions such as cell signalling.esicular trafficking.rotein sorting and lipid modification . PX domains are important phosphoinositide-binding modules that have varying lipid-binding specificities .The PX domain is approximately 120 residues long .nd folds into a three-stranded beta-sheet followed by three -helices and a proline-rich region that immediately preceeds a membrane-interaction loop and spans approximately eight hydrophobic and polar residues. The PX domain of p47phox binds to the SH3 domain in the same protein. Phosphorylation of p47(phox). cytoplasmic activator of the microbicidal phagocyte oxidase (phox).licits interaction of p47(phox) with phoinositides. The protein phosphorylation-driven conformational change of p47(phox) enables its PX domain to bind to phosphoinositides.he interaction of which plays a crucial role in recruitment of p47(phox) from the cytoplasm to membranes and subsequent activation of the phagocyte oxidase. The lipid-binding activity of this protein is normally suppressed by intramolecular interaction of the PX domain with the C-terminal Src homology 3 (SH3) domain .The PX domain is conserved from yeast to human. A recent multiple alignment of representative PX domain sequences can be found in .lthough showing relatively little sequence conservation.heir structure appears to be highly conserved. Although phosphatidylinositol-3-phosphate (PtdIns(3)P) is the primary target of PX domains.inding to phosphatidic acid.hosphatidylinositol-3.-bisphosphate (PtdIns(3.)P2).hosphatidylinositol-3.-bisphosphate (PtdIns(3.)P2).hosphatidylinositol-4.-bisphosphate (PtdIns(4.)P2).nd phosphatidylinositol-3..-trisphosphate (PtdIns(3..)P3) has been reported as well. The PX-domain is also a protein-protein interaction domain .
  IPR001683:Phox-like
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 vav.bl.oS 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.
  IPR001849:Pleckstrin-like
Phosphatidylcholine-hydrolyzing phospholipase D (PLD) isoforms are activated by ADP-ribosylation factors (ARFs). PLD produces phosphatidic acid from phosphatidylcholine.hich may be essential for the formation of certain types of transport vesicles or may be constitutive vesicular transport to signal transduction pathways. PC-hydrolyzing PLD is a homologue of cardiolipin synthase.hosphatidylserine synthase.acterial PLDs.nd viral proteins. Each of these appears to possess a domain duplication which is apparent by the presence of two motifs containing well-conserved histidine.ysine.nd/or asparagine residues which may contribute to the active site aspartic acid. An Escherichia coli endonuclease (nuc) and similar proteins appear to be PLD homologues but possess only one of these motifs .
  IPR001736:Phospholipase D/Transphosphatidylase
Pleckstrin homology (PH) domains are small modular domains that occur once.r occasionally several times.n a large variety of signalling proteins.here 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 delta-1.eta-spectrin.ynamin.on-of-sevenless.rp1.nc-89.app1 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
IPR001683:PX 
Evalue:-27.1739251972992 
Location:79-209IPR001849:PH 
Evalue:-12.180456161499 
Location:220-328IPR001736:PLDc 
Evalue:-8.28399658203125 
Location:459-486IPR001736:PLDc 
Evalue:-6.0915150642395 
Location:891-918IPR001849:PH_DOMAIN 
Evalue:0 
Location:0-0
SequencesProtein: PLD1_HUMAN (1074 aa)
mRNA: NM_002662
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)
activation of protein kinase C
sdb:0206 activation of protein kinase C  (Evidence:keywords)
KO assignmentK01115
  Level 3 annotation:
    phospholipase D
  Level 2 annotation:
    Glycerophospholipid metabolism
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 815 residues, 172801344-172803786Exon2: 41 residues, 172805782-172805900Exon3: 53 residues, 172812762-172812916Exon4: 47 residues, 172820869-172821004Exon5: 18 residues, 172843323-172843373Exon6: 40 residues, 172845393-172845507Exon7: 31 residues, 172859696-172859785Exon8: 39 residues, 172862543-172862654Exon9: 40 residues, 172874983-172875097Exon10: 41 residues, 172877198-172877317Exon11: 45 residues, 172878049-172878178Exon12: 40 residues, 172887168-172887282Exon13: 73 residues, 172887854-172888068Exon14: 69 residues, 172889159-172889360Exon15: 39 residues, 172892815-172892926Exon16: 29 residues, 172900228-172900310Exon17: 30 residues, 172909238-172909322Exon18: 52 residues, 172910043-172910193Exon19: 53 residues, 172914376-172914529Exon20: 33 residues, 172925179-172925272Exon21: 21 residues, 172926501-172926560Exon22: 24 residues, 172933927-172933993Exon23: 37 residues, 172935348-172935454Exon24: 50 residues, 172935975-172936121Exon25: 44 residues, 172938015-172938143Exon26: 65 residues, 172938375-172938566Exon27: 2 residues, -Jump to PLD1_HUMAN  
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