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0AP2A1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameAP2A1
DescriptionAdapter-related protein complex 2 alpha 1 subunit (alpha-adaptin a) (adaptor protein complex ap-2 alpha-1 subunit) (clathrin assembly protein complex 2 alpha-a large chain) (100 kda coated vesicle protein a) (plasma membrane adaptor ha2/ap2 adaptin alpha a subunit).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0030122 AP-2 adaptor complex (NAS)
0030130 clathrin coat of trans-Golgi network vesicle (NAS)
0006897 endocytosis (NAS)
0006895 Golgi to endosome transport (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:-217.136672973633 
Location:29-591IPR003164:Alpha_adaptin_C 
Evalue:-97.2839965820313 
Location:864-976IPR008152:Alpha_adaptinC2 
Evalue:-34.7212448120117 
Location:745-858IPR003006:IG_MHC 
Evalue:0 
Location:0-0
SequencesProtein: AP2A1_HUMAN (977 aa)
mRNA: NM_014203
Local Annotation
Synapse Ontology
all
sdb:0004 Presynaptic compartment  (Evidence:keywords)
A clathrin coat found on a synaptic vesicle.
sdb:0076 clathrin coat of synaptic vesicle  (Evidence:keywords)
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)
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)
Various stages of the synaptic vesicle cycle, including attachment, prefusion, triggering, recycling and reloading of the vesicles with transmitter.
sdb:0098 synaptic vesicle cycling  (Evidence:keywords)
interaction between synaptic vesicle and the scaffold.
sdb:0106 transport of synaptic vesicle in the presynaptic axon  (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)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 93 residues, 54961991-54962269Exon2: 25 residues, 54976825-54976894Exon3: 49 residues, 54977015-54977158Exon4: 66 residues, 54977599-54977793Exon5: 45 residues, 54987003-54987133Exon6: 36 residues, 54988059-54988161Exon7: 38 residues, 54990698-54990807Exon8: 52 residues, 54993870-54994021Exon9: 58 residues, 54994395-54994564Exon10: 48 residues, 54994697-54994835Exon11: 63 residues, 54995036-54995219Exon12: 34 residues, 54996029-54996127Exon13: 79 residues, 54996458-54996690Exon14: 58 residues, 54996790-54996958Exon15: 55 residues, 54997049-54997210Exon16: 24 residues, 54997602-54997668Exon17: 21 residues, 54998017-54998074Exon18: 29 residues, 54998175-54998258Exon19: 32 residues, 54998355-54998445Exon20: 43 residues, 55000521-55000645Exon21: 41 residues, 55000729-55000846Exon22: 25 residues, 55000940-55001010Exon23: 47 residues, 55001187-55001322Exon24: 145 residues, 55001749-55002179Exon25: 2 residues, -Jump to AP2A1_HUMAN  
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Loci Cluster (Details)Loci: 3124 53589943-53639205 ~-49K 19224(GRIN2D)(+)Loci: 3125 53656317-53661179 ~-5K 19226(KCNJ14)(+)Loci: 3126 53747240-53794495 ~-47K 19229(SULT2B1)(+)Loci: 4406 53833083-53841263 ~-8K 19240(CA11)(-)Loci: 4407 53990131-54006113 ~-16K 19255(BCAT2)(-)Loci: 4408 54262487-54268010 ~-6K 19284(-)Loci: 3127 54309429-54313528 ~-4K 19290(LIN7B)(+)Loci: 3128 54314474-54346090 ~-32K 19292(PPFIA3)(+)Loci: 4409 54484705-54520286 ~-36K 19297(SLC6A16)(-)Loci: 3129 54669297-54681299 ~-12K 19311(FLT3LG)(+)Loci: 4410 54854641-54860926 ~-6K 19323(IRF3)(-)Loci: 3130 54886218-54908800 ~-23K 19334(CPT1C)(+)Loci: 3131 54961991-55002179 ~-40K 19337(AP2A1)(+)Loci: 3132 55124271-55129003 ~-5K 19355(ATF5)(+)Loci: 4411 55510576-55524446 ~-14K 19365(KCNC3)(-)Loci: 4412 55817047-55833114 ~-16K 19382(SYT3)(-)Loci: 4413 55856895-55912007 ~-55K 19383(SHANK1)(-)Loci: 3123 53559468-53571439 ~-12K 19220(SYNGR4)(+)Link out to UCSC