SynDB Home Page
SynDB Home Page
Browse
Search
Download
Help
People
links

blue bulletSynDB protein details  


Parse error: syntax error, unexpected T_VARIABLE in /home/kongl/syndb/www/sdb_nats.php on line 52
0PGTA_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameRABGGTA
DescriptionGeranylgeranyl transferase type ii alpha subunit (ec 2.5.1.60) (rab geranylgeranyltransferase alpha subunit) (rab geranyl- geranyltransferase alpha subunit) (rab gg transferase alpha) (rab ggtase alpha).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0004663 Rab-protein geranylgeranyltransferase activity (TAS)
0006464 protein modification (TAS)
0007601 visual perception (TAS)

Warning: fopen(/home/kongl/syndb/www/temp/1056461498.dot) [function.fopen]: failed to open stream: Permission denied in /home/kongl/syndb/www/sdb_pro.php on line 269

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 270

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 271

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 272

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 273

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 274

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 299

Warning: fclose(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 300
schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains assigned to SynO:
Rab geranylgeranyltransferase (RabGGT) catalyses the transfer of geranylgeranyl groups to the C-terminal cysteine residues of Rab proteins.as-related small GTPases that function in intracellular vesicular transport . RabGGT is only able to prenylate Rab when it is complexed to the Rab escort protein (REP).fter which REP remains bound to the prenylated Rab and delivers it to its target membrane. RabGGT is a member of the protein prenyltransferase family ().ll of which are heterodimers consisting of alpha and beta subunits. RabGGT is distinct from other members of the prenyltransferase family because of the presence of an Ig-like insert domain in the alpha subunit that is folded into an eight-stranded sandwich between two helices in the helical domain.
  IPR009087:Rab geranylgeranyltransferase, alpha subunit, insert
InterPro domains unassigned to SynO:
Protein prenylation is the posttranslational attachment of either a farnesyl group or a geranylgeranyl group via a thioether linkage (-C-S-C-) to a cysteine at or near the carboxyl terminus of the protein. Farnesyl and geranylgeranyl groups are polyisoprenes.nsaturated hydrocarbons with a multiple of five carbons; the chain is 15 carbons long in the farnesyl moiety and 20 carbons long in the geranylgeranyl moiety. There are three different protein prenyltransferases in humans: farnesyltransferase (FT) and geranylgeranyltransferase 1 (GGT1) share the same motif (the CaaX box) around the cysteine in their substrates.nd are thus called CaaX prenyltransferases.hereas geranylgeranyltransferase 2 (GGT2.lso called Rab geranylgeranyltransferase) recognizes a different motif and is thus called a non-CaaX prenyltransferase. Protein prenyltransferases are currently known only in eukaryotes.ut they are widespread.eing found in vertebrates.nsects.ematodes.lants.ungi and protozoa.ncluding several parasites. Each protein consists of two subunits.lpha and beta; the alpha subunit of FT and GGT1 is encoded by the same gene.NTA. The alpha subunit is thought to participate in a stable complex with the isoprenyl substrate; the beta subunit binds the peptide substrate. In the alpha subunits of both types of protein prenyltransferases.even tetratricopeptide repeats are formed by pairs of helices that are stabilized by conserved intercalating residues. The alpha subunits of GGT2 in mammals and plants also have an immunoglobulin-like domain between the fifth and sixth tetratricopeptide repeat.s well as leucine-rich repeats at the carboxyl terminus. The functions of these additional domains in GGT2 are as yet undefined.ut they are apparently not directly involved in the interaction with substrates and Rab escort proteins. The tetratricopeptide repeats of the alpha subunit form a right-handed superhelix.hich embraces the (alpha-alpha)6 barrel of the beta subunit .
  IPR002088:Protein prenyltransferase, alpha subunit
Leucine-rich repeats (LRR) consist of 2-45 motifs of 20-30 amino acids in length that generally folds into an arc or horseshoe shape . LRRs occur in proteins ranging from viruses to eukaryotes.nd appear to provide a structural framework for the formation of protein-protein interactions . Proteins containing LRRs include tyrosine kinase receptors.ell-adhesion molecules.irulence factors.nd extracellular matrix-binding glycoproteins.nd are involved in a variety of biological processes.ncluding signal transduction.ell adhesion.NA repair.ecombination.ranscription.NA processing.isease resistance.poptosis.nd the immune response.Sequence analyses of LRR proteins suggested the existence of several different subfamilies of LRRs. The significance of this classification is that repeats from different subfamilies never occur simultaneously and have most probably evolved independently. It is.owever.ow clear that all major classes of LRR have curved horseshoe structures with a parallel beta sheet on the concave side and mostly helical elements on the convex side. At least six families of LRR proteins.haracterized by different lengths and consensus sequences of the repeats.ave been identified. Eleven-residue segments of the LRRs (LxxLxLxxN/CxL).orresponding to the ß-strand and adjacent loop regions.re conserved in LRR proteins.hereas the remaining parts of the repeats (herein termed variable) may be very different. Despite the differences.ach of the variable parts contains two half-turns at both ends and a "linear" segment (as the chain follows a linear path overall).sually formed by a helix.n the middle. The concave face and the adjacent loops are the most common protein interaction surfaces on LRR proteins. 3D structure of some LRR proteins-ligand complexes show that the concave surface of LRR domain is ideal for interaction with alpha-helix.hus supporting earlier conclusions that the elongated and curved LRR structure provides an outstanding framework for achieving diverse protein-protein interactions . Molecular modeling suggests that the conserved pattern LxxLxL.hich is shorter than the previously proposed LxxLxLxxN/CxL is sufficient to impart the characteristic horseshoe curvature to proteins with 20- to 30-residue repeats .
  IPR001611:Leucine-rich repeat
Protein prenyltransferases catalyze the transfer of the carbon moiety of C15 farnesyl pyrophosphate or geranylgeranyl pyrophosphate synthase to a conserved cysteine residue in a CaaX motif of protein and peptide substrates. The addition of a farnesyl group is required to anchor proteins to the cell membrane. In the 3D structure of a mammalian Ras farnesyltransferases (Ftase).oth subunits are largely composed of alpha-helices. The alpha-2 to alpha-15 helices in the alpha subunit fold into a novel helical hairpin structure.esulting in a crescent-shape domain that envelopes part of the subunit. The 12 helices of the beta-subunit form an alpha-alpha barrel. Six additional helices connect the inner core of helices and form the outside of the helical barrel. A deep cleft surrounded by hydrophobic amino acids in the centre of the barrel is proposed as the FPP-binding pocket. A single Zn2+ ion is located at the junction between the hydrophilic surface groove near the subunit interface. The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008940:Protein prenyltransferase
IPR009087:RabGGT_insert 
Evalue:-70.7212448120117 
Location:241-350IPR002088:PPTA 
Evalue:-9.05060958862305 
Location:162-192IPR002088:PPTA 
Evalue:-8.60206031799316 
Location:91-121IPR002088:PPTA 
Evalue:-7.82390880584717 
Location:127-157IPR002088:PPTA 
Evalue:-7.60205984115601 
Location:210-240IPR002088:PPTA 
Evalue:-4.42021656036377 
Location:47-77IPR001611:LRR_1 
Evalue:-1.61978876590729 
Location:464-485IPR002088:PPTA 
Evalue:-0.677780687808991 
Location:366-396IPR001611:LEURICHRPT 
Evalue:0 
Location:507-520
SequencesProtein: PGTA_HUMAN (567 aa)
mRNA: NM_004581
Local Annotation
Synapse Ontology
attachment of the vesicle filled with transmitters involves a specific interaction between the vesicle membrane and the presynaptic active zone.
sdb:0148 docking  (Evidence:domains)
synaptic vesicles fuse with early endosomes as an intermediate sorting compartment to eliminate aged or missorted proteins.
sdb:0159 endosome fusion  (Evidence:domains)
KO assignmentK05956
  Level 3 annotation:
    
  Level 2 annotation:
    Other enzymes
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 75 residues, 23804585-23804809Exon2: 31 residues, 23805475-23805563Exon3: 40 residues, 23805821-23805935Exon4: 41 residues, 23806705-23806822Exon5: 31 residues, 23806915-23807004Exon6: 31 residues, 23807155-23807244Exon7: 19 residues, 23807414-23807466Exon8: 37 residues, 23807559-23807665Exon9: 36 residues, 23807770-23807872Exon10: 29 residues, 23807956-23808039Exon11: 30 residues, 23808125-23808209Exon12: 70 residues, 23808536-23808740Exon13: 64 residues, 23808998-23809186Exon14: 43 residues, 23809379-23809504Exon15: 39 residues, 23809882-23809993Exon16: 143 residues, 23810158-23810583Exon17: 2 residues, -Jump to PGTA_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 2827 23633322-23643177 ~-10K 10904(PCK2)(+)Loci: 4123 23748628-23755020 ~-6K 10927(CHMP4A)(-)Loci: 4124 23804585-23810583 ~-6K 10943(RABGGTA)(-)Loci: 2826 23610595-23617135 ~-7K 10902(CPNE6)(+)Link out to UCSC