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0AP2A2_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameAP2A2
DescriptionAdapter-related protein complex 2 alpha 2 subunit (alpha-adaptin c) (adaptor protein complex ap-2 alpha-2 subunit) (clathrin assembly protein complex 2 alpha-c large chain) (100 kda coated vesicle protein c) (plasma membrane adaptor ha2/ap2 adaptin alpha c subunit) (huntingtin-interacting protein hypj).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0030122 AP-2 adaptor complex (NAS)
0006886 intracellular protein transport (NAS)

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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
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 alpha adaptor subunit can be divided into a trunk domain and the C-terminal appendage domain (or ear domain).eparated by a linker region. The C-terminal appendage domain regulates translocation of endocytic accessory proteins to the bud site .
  IPR003164:AP2 clathrin adaptin, alpha chain, C-terminal
Adaptins are components of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins.eading to their selection and concentration. Gamma-adaptin is a subunit of the golgi adaptor. Alpha adaptin is a heterotetramer that regulates clathrin-bud formation. The carboxyl-terminal appendage of the alpha subunit regulates translocation of endocytic accessory proteins to the bud site. This Ig-fold domain is found in alpha.eta and gamma adaptins and consists of a beta-sandwich containing 7 strands in 2 beta-sheets in a greek-key topology . The adaptor appendage contains an additional N-terminal strand.
  IPR008152:Alpha/gamma adaptin, 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 assembly.how 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 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 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
IPR002553:Adaptin_N 
Evalue:-212.657577514648 
Location:29-590IPR003164:Alpha_adaptin_C 
Evalue:-96.259635925293 
Location:826-938IPR008152:Alpha_adaptinC2 
Evalue:-35.8239097595215 
Location:707-820
SequencesProtein: AP2A2_HUMAN (939 aa)
mRNA: AK223558 NM_012305
Local Annotation
Synapse Ontology
Typical ecretory organelles, some 50 nm in diameter, of presynaptic nerve terminals; accumulate high concentrations of nonpeptide neurotransmitters and secrete these into the synaptic cleft by fusion with the 'active zone' of the presynaptic plasma membrane.
sdb:0094 typical synaptic vesicle  (Evidence:keywords)
all the components of the clathrin coat, major ones are clathrin and clathrin adaptors.
sdb:0261 clathrin coat component  (Evidence:keywords)
the generation of action potential at soma of neurons.
sdb:0313 generation of AP at soma  (Evidence:keywords)
?
sdb:0329 actin in synaptic vesicle cycling  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 83 residues, 915840-916088Exon2: 25 residues, 949436-949505Exon3: 49 residues, 960168-960311Exon4: 66 residues, 962061-962255Exon5: 45 residues, 967094-967224Exon6: 36 residues, 971197-971299Exon7: 38 residues, 974644-974753Exon8: 51 residues, 975434-975582Exon9: 58 residues, 976784-976953Exon10: 48 residues, 978551-978689Exon11: 63 residues, 982502-982685Exon12: 34 residues, 983283-983381Exon13: 79 residues, 983753-983985Exon14: 60 residues, 984071-984245Exon15: 57 residues, 990431-990598Exon16: 29 residues, 993721-993804Exon17: 32 residues, 996527-996617Exon18: 43 residues, 998011-998135Exon19: 41 residues, 999099-999216Exon20: 25 residues, 999327-999397Exon21: 47 residues, 999682-999817Exon22: 566 residues, 1000547-1002239Exon23: 2 residues, -Jump to AP2A2_HUMANExon1: 70 residues, 915880-916088Exon2: 25 residues, 949436-949505Exon3: 49 residues, 960168-960311Exon4: 66 residues, 962061-962255Exon5: 45 residues, 967094-967224Exon6: 36 residues, 971197-971299Exon7: 38 residues, 974644-974753Exon8: 52 residues, 975431-975582Exon9: 58 residues, 976784-976953Exon10: 48 residues, 978551-978689Exon11: 63 residues, 982502-982685Exon12: 34 residues, 983283-983381Exon13: 79 residues, 983753-983985Exon14: 60 residues, 984071-984245Exon15: 57 residues, 990431-990598Exon16: 29 residues, 993721-993804Exon17: 32 residues, 996527-996617Exon18: 43 residues, 998011-998135Exon19: 41 residues, 999099-999216Exon20: 25 residues, 999327-999397Exon21: 47 residues, 999682-999817Exon22: 126 residues, 1000547-1000919Exon23: 2 residues, -Jump to AP2A2_HUMAN  
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Loci Cluster (Details)Loci: 2642 627304-630703 ~-3K 6078(DRD4)(+)Loci: 3928 780475-786221 ~-6K 6091(SLC25A22)(-)Loci: 3929 789178-795245 ~-6K 6092(-)Loci: 2643 915840-1002239 ~-86K 6112(AP2A2)(+)Loci: 3927 192923-197383 ~-4K 6029(-)Link out to UCSC