SynDB Home Page
SynDB Home Page

blue bulletSynDB protein details  

Parse error: syntax error, unexpected T_VARIABLE in /home/kongl/syndb/www/sdb_nats.php on line 52
0CENG2_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionCentaurin-gamma 2 (arf-gap with gtp-binding protein-like, ankyrin repeat and pleckstrin homology domains 1) (agap1).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
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
Mitochondrial Rho proteins (Miro-1 and atypical Rho GTPases. They have a unique domain organisation.ith tandem GTP-binding domains and two EF hand domains ().hat may bind calcium. They are also larger than classical small GTPases. It has been proposed that they are involved in mitochondrial homeostasis and apoptosis .
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.
Many members of the Ras superfamily of GTPases have been implicated in the regulation of hematopoietic cells.ith roles in growth.urvival.ifferentiation.ytokine production.hemotaxis.esicle-trafficking.nd phagocytosis. The Ras superfamily of proteins now includes over 150 small GTPases (distinguished from the large.eterotrimeric GTPases.he G-proteins). It comprises six subfamilies.he Kir/Rem/Rad subfamilies . They exhibit remarkable overall amino acid identities.specially in the regions interacting with the guanine nucleotide exchange factors that catalyze their activation .
  IPR001806:Ras GTPase
The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids. They occur in a large number of functionally diverse proteins mainly from eukaryotes. The few known examples from prokaryotes and viruses may be the result of horizontal gene transfers . The repeat has been found in proteins of diverse function such as transcriptional initiators.ell-cycle regulators.ytoskeletal.on transporters and signal transducers. The ankyrin fold appears to be defined by its structure rather than its function since there is no specific sequence or structure which is universally recognised by it. The conserved fold of the ankyrin repeat unit is known from several crystal and solution structures . Each repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90o angle. The repeats stack together to form an L-shaped structure .
Proteins with a small GTP-binding domain include Ras.hoA.ab11.ranslation elongation factor G.ranslation initiation factor IF-2.etratcycline resistance protein TetM.DC42.ra.DP-ribosylation factors.dhF.nd many others . In some proteins the domain occurs more than once. Among them there is a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model.
  IPR005225:Small GTP-binding protein domain
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
SequencesProtein: CENG2_HUMAN (857 aa)
mRNA: NM_001037131
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)
sdb:0247 cytoskeleton protein transport  (Evidence:keywords)
the generation of action potential at soma of neurons.
sdb:0313 generation of AP at soma  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 253 residues, 236067474-236068232Exon2: 21 residues, 236282561-236282620Exon3: 31 residues, 236290939-236291027Exon4: 30 residues, 236314345-236314431Exon5: 49 residues, 236318080-236318222Exon6: 47 residues, 236323736-236323871Exon7: 44 residues, 236371141-236371269Exon8: 54 residues, 236372749-236372905Exon9: 33 residues, 236380621-236380714Exon10: 37 residues, 236456727-236456832Exon11: 58 residues, 236482120-236482289Exon12: 55 residues, 236504147-236504306Exon13: 56 residues, 236541844-236542006Exon14: 53 residues, 236609943-236610098Exon15: 32 residues, 236614133-236614224Exon16: 76 residues, 236622441-236622664Exon17: 87 residues, 236693574-236693830Exon18: 519 residues, 236697301-236698853Exon19: 2 residues, -Jump to CENG2_HUMAN