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
0COPB_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionCoatomer beta subunit (beta-coat protein) (beta-cop).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0030126 COPI vesicle coat (ISS)
0005829 cytosol (TAS)
0000139 Golgi membrane (TAS)
0005798 Golgi vesicle (TAS)
0005515 protein binding (ISS)
0006891 intra-Golgi transport (ISS)
0006890 retrograde transport, Golgi to ER (ISS)

Warning: fopen(/home/kongl/syndb/www/temp/ [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 domain is the N-terminal region of various alpha.eta and gamma subunits of the AP-1.P-2 and AP-3 adaptorprotein complexes. The adaptor protein (AP) complexes are involved inthe formation of clathrin-coated pits and vesicles .The N-terminal region of the various adaptor proteins (APs) is constantby comparison to the C-terminal which is variable within members of theAP-2 family ; and it has been proposed that this constant regioninteracts with another uniform component of the coated vesicles .
  IPR002553:Adaptin, N-terminal
Coatomer protein complex I (COPI)-coated vesicles are involved in transport between the endoplasmic reticulum and the Golgi but also participate in transport from early to late endosomes within the endocytic pathway . This domain is found at the C terminus of the coatamer beta subunit proteins (Beta-coat proteins). This C-terminal domain probably adapts the function of the N-terminal domain.
  IPR011710:Coatomer beta subunit, C-terminal
The AP2 adaptor is a heterotetramer that plays a central role in clathrin-mediated endocytosis by linking transmembrane receptors to be internalised to the clathrin lattice. During clathrin-mediated endocytosis.lathrin-coated vesicles are formed by pinching off a portion of the plasma membrane.long with its cargo molecules. The AP2 adaptor links the cargo to the clathrin coat.nd can interact with proteins involved in the formation of the clathrin-coated vesicles. The AP2 adaptor is composed of four subunits.f which alpha and beta2 are the largest. The alpha and beta2 adaptor subunits can each be divided into a trunk domain and the appendage domain (or ear domain).eparated by a linker region. Clathrin polymerisation is promoted by its binding to the beta2 appendage and hinge domains. The alpha appendage domain interacts with a number of accessory proteins.ncluding eps15.psin.mphiphysin.P180.uxilin.umb.nd Dab2.hereby regulating the translocation of these proteins to the bud site. The appendage domains of the alpha and beta2 subunits are structurally similar . The structure of this domain consists of a three-layer arrangement.lpha-beta-alpha.ith a bifurcated antiparallel beta-sheet. COP-I coatomer subunits.hich function in vesicle coat a weak sequence similarity to the AP2 clathrin adaptor .
  IPR009028:AP2 clathrin adaptor, alpha and beta chain, appendage
This domain consists of a multi-helical fold comprised of two curved layers of alpha helices arranged in a regular right-handed 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 armadillo repeat (found in beta-catenins and importins).he HEAT repeat (found in protein phosphatase 2a and initiation factor eIF4G).he PHAT domain (found in Smaug RNA-binding protein).he leucine-rich repeat variant.he Pumilo repeat.nd in the H regulatory subunit of V-type ATPases. The sequence similarity among these different repeats or domains is low.owever they exhibit considerable structural similarity. Furthermore.he number of repeats present in the superhelical structure can vary between orthologues.ndicating that rapid loss/gain of repeats has occurred frequently in evolution. A common phylogenetic origin has been proposed for the armadillo and HEAT repeats .
  IPR011989:Armadillo-like helical
SequencesProtein: COPB_HUMAN (953 aa)
mRNA: NM_016451
Local Annotation
Synapse Ontology
the clathrin located in the surface of the endocytotic intermediate.
sdb:0115 clathrin-coated pit  (Evidence:keywords)
all the components of the clathrin coat, major ones are clathrin and clathrin adaptors.
sdb:0261 clathrin coat component  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 126 residues, 14435628-14436005Exon2: 54 residues, 14436653-14436809Exon3: 32 residues, 14438329-14438419Exon4: 50 residues, 14439307-14439453Exon5: 42 residues, 14443032-14443152Exon6: 50 residues, 14444403-14444548Exon7: 62 residues, 14446802-14446982Exon8: 78 residues, 14447457-14447685Exon9: 42 residues, 14452616-14452737Exon10: 55 residues, 14453906-14454067Exon11: 34 residues, 14455040-14455137Exon12: 50 residues, 14457690-14457836Exon13: 51 residues, 14458880-14459027Exon14: 38 residues, 14459111-14459219Exon15: 42 residues, 14461153-14461273Exon16: 48 residues, 14464488-14464626Exon17: 33 residues, 14466613-14466706Exon18: 40 residues, 14468686-14468801Exon19: 58 residues, 14471763-14471933Exon20: 78 residues, 14472331-14472561Exon21: 51 residues, 14476959-14477107Exon22: 83 residues, 14477730-14477974Exon23: 2 residues, -Jump to COPB_HUMAN  
Tune and view alternative isoforms