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
0COPE_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameCOPE
DescriptionCoatomer epsilon subunit (epsilon-coat protein) (epsilon-cop).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0030126 COPI vesicle coat (ISS)
0006891 intra-Golgi transport (ISS)
0006890 retrograde transport, Golgi to ER (ISS)

Warning: fopen(/home/kongl/syndb/www/temp/1842032744.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 unassigned to SynO:
This family represents the epsilon subunit of the coatomer complex.hich is involved in the regulation of intracellular protein trafficking between the endoplasmic reticulum and the Golgi complex .
  IPR006822:Coatomer epsilon subunit
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
This domain consists of a multi-helical fold comprised of two curved layers of alpha helices arranged in a regular right-handed superhelix.here the repeats that make up this structure are arranged about a common axis . These superhelical structures present an extensive solvent-accessible surface that is well suited to binding large substrates such as proteins and nucleic acids. This topology has been found with a number of repeats and domains.ncluding the tetratricopeptide repeat (TPR) (found in kinesin light chains.NAP regulatory proteins.lathrin heavy chains and bacterial aspartyl-phosphate phosphatases).nd the pentatricopeptide repeat (PPR) (RNA-processing proteins). The TRP is likely to be an ancient repeat.ince it is found in eukaryotes.acteria and archaea.hereas the PPR repeat is found predominantly in higher plants. The superhelix formed from these repeats can bind ligands at a number of different regions.nd has the ability to acquire multiple functional roles .
  IPR011990:Tetratricopeptide-like helical
IPR006822:Coatomer_E 
Evalue:-189.026870727539 
Location:14-304
SequencesProtein: COPE_HUMAN (307 aa)
mRNA: NM_007263
Local Annotation
Synapse Ontology
the clathrin located in the surface of the endocytotic intermediate.
sdb:0115 clathrin-coated pit  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 71 residues, 18871323-18871535Exon2: 27 residues, 18871681-18871756Exon3: 25 residues, 18872189-18872258Exon4: 54 residues, 18875076-18875232Exon5: 29 residues, 18876579-18876661Exon6: 20 residues, 18877384-18877438Exon7: 53 residues, 18878768-18878921Exon8: 35 residues, 18882779-18882880Exon9: 23 residues, 18884792-18884855Exon10: 58 residues, 18891031-18891199Exon11: 2 residues, -Jump to COPE_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 4381 18754582-18763114 ~-9K 18371(COMP)(-)Loci: 3100 18803787-18840038 ~-36K 18373(RENT1)(+)Loci: 4382 18871323-18891199 ~-20K 18381(COPE)(-)Loci: 4383 18901011-18912983 ~-12K 18385(HOMER3)(-)Loci: 3101 19035807-19084697 ~-49K 18393(+)Loci: 3099 18655487-18749762 ~-94K 18368(MECT1)(+)Link out to UCSC