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0CENA2_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameCENTA2
DescriptionCentaurin-alpha 2.
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GON/A
Domain Architecture (Details)
InterPro domains unassigned to SynO:
This entry describes a family of small GTPase activating proteins.or example ARF1-directed GTPase-activating protein.he cycle control GTPaseactivating protein (GAP) GCS1 which is important for the regulation ofthe ADP ribosylation factor ARF. member of the Ras superfamily of GTP-bindingproteins . The GTP-bound form of ARF is essential for the maintenance of normalGolgi morphology.t participates in recruitment of coat proteins which arerequired for budding and fission of membranes. Before the fusion with anacceptor compartment the membrane must be uncoated. This step required thehydrolysis of GTP associated to ARF. These proteins contain a characteristic zinc finger motif(Cys-x2-Cys-x(16.7)-x2-Cys) which displays some similarity to the C4-typeGATA zinc finger. The ARFGAP domain display no obvious similarity to other GAPproteins. The 3D structure of the ARFGAP domain of the PYK2-associated protein beta hasbeen solved . It consists of a three-stranded beta-sheet surrounded by 5alpha helices. The domain is organized around a central zinc atom which iscoordinated by 4 cysteines. The ARFGAP domain is clearlyunrelated to the other GAP proteins structures which are exclusively helical.Classical GAP proteins accelerate GTPase activity by supplying an argininefinger to the active site. The crystal structure of ARFGAP bound to ARFrevealed that the ARFGAP domain does not supply an arginine to the active sitewhich suggests a more indirect role of the ARFGAP domain in the GTPasehydrolysis . The Rev protein of human immunodeficiency virus type 1 (HIV-1) facilitates nuclear export of unspliced and partly-spliced viral RNAs . Rev contains an RNA-binding domain and an effector domain; the latter is believed to interact with a cellular cofactor required for the Rev response and hence HIV-1 replication. Human Rev interacting protein (hRIP) specifically interacts with the Rev effector. The amino acid sequence of hRIP is characterised by an N-terminal.-4 class zinc finger motif.
  IPR001164:Arf GTPase activating protein
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
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
IPR001164:ArfGap 
Evalue:-47.4814872741699 
Location:9-130IPR001849:PH 
Evalue:-14.2596368789673 
Location:256-361IPR001849:PH 
Evalue:-7.408935546875 
Location:133-233
SequencesProtein: CENA2_HUMAN (381 aa)
mRNA: BC033758 DQ288859 NM_018404
Local Annotation
Synapse Ontology
introduce the substructure of the synapse and the location where the molecule can be seen. It will contain all the constructive special organelle and molecule we known.
sdb:0001 Structure/Biochemistry of synapse  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 65 residues, 26273058-26273252Exon2: 45 residues, 26274083-26274214Exon3: 32 residues, 26277970-26278062Exon4: 28 residues, 26283032-26283112Exon5: 39 residues, 26285328-26285441Exon6: 51 residues, 26296050-26296197Exon7: 30 residues, 26300430-26300514Exon8: 23 residues, 26304431-26304494Exon9: 28 residues, 26305621-26305699Exon10: 78 residues, 26307384-26307613Exon11: 454 residues, 26308978-26310335Exon12: 2 residues, -Jump to CENA2_HUMANExon1: 64 residues, 26273063-26273252Exon2: 45 residues, 26274083-26274214Exon3: 32 residues, 26277970-26278062Exon4: 28 residues, 26283032-26283112Exon5: 39 residues, 26285328-26285441Exon6: 51 residues, 26296050-26296197Exon7: 30 residues, 26300430-26300514Exon8: 23 residues, 26304431-26304494Exon9: 27 residues, 26305624-26305699Exon10: 78 residues, 26307384-26307613Exon11: 243 residues, 26308978-26309702Exon12: 2 residues, -Jump to CENA2_HUMANExon1: 60 residues, 26273075-26273252Exon2: 45 residues, 26274083-26274214Exon3: 38 residues, 26277952-26278062Exon4: 28 residues, 26283032-26283112Exon5: 39 residues, 26285328-26285441Exon6: 51 residues, 26296050-26296197Exon7: 30 residues, 26300430-26300514Exon8: 23 residues, 26304431-26304494Exon9: 28 residues, 26305621-26305699Exon10: 78 residues, 26307384-26307613Exon11: 129 residues, 26308978-26309359Exon12: 2 residues, -Jump to CENA2_HUMAN  
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Loci Cluster (Details)Loci: 2994 25828551-25877957 ~-49K 15450(GOSR1)(+)Loci: 2995 26273058-26310335 ~-37K 15466(CENTA2)(+)Loci: 2996 26446242-26725609 ~-279K 15473(NF1)(+)Loci: 2997 26742767-26889352 ~-147K 15482(RAB11FIP4)(+)Loci: 4279 25549033-25586831 ~-38K 15444(SLC6A4)(-)Link out to UCSC