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0AP3M1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionAdapter-related protein complex 3 mu 1 subunit (mu-adaptin 3a) (ap-3 adapter complex mu3a subunit).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005764 lysosome (TAS)
0006622 protein-lysosome targeting (TAS)

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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 assigned to SynO:
Membrane transport in eukaryotic cells is effected largely by intracellular vesicles that bud from donor membranes to transport cargo proteins selectively. One of the most thoroughly characterized budding reactions involves clathrin coats. Clathrin-coated vesicles mediate a variety of intracellular transport steps such as endocytosis.ransport of proteins from the trans-Golgi network to the endosomal/lysosomal system and budding from endosomes. Nerve terminal clathrin coats comprise clathrin.he adaptor complex AP-2 (a heterotetramer composed of alpha.eta2.u2 and sigma2 subunits) and the protein AP180. Mu2 and the core region of alpha-adaptin represent major interfaces of AP-2 with the membrane .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008968:Mu2 adaptin subunit (AP50) of AP2
VAMPs (and its homologue synaptobrevins) define a group of SNARE proteins that contain a C-terminal coiled-coil/SNARE motif.n combination with variable N-terminal domains that are used to classify VAMPs: those containing longin N-terminal domains (~150 aa) are referred to as longins.hile those with shorter N-termini are referred to as brevins . Longins are the only type of VAMP protein found in all eukaryotes.uggesting that their longin domain is essential. The longin domain is thought to exert a regulatory function. Longin domains have been shown to share the same structural fold. profilin-like globular domain consisting of a five-stranded antiparallel beta-sheet that is sandwiched by an alpha-helix on one side.nd two alpha-helices on the other (beta(2)-alpha-beta(3)-alpha(2)).Other families have been shown to contain domains that structurally resemble the VAMP longin domain. An example is the eukaryotic conserved protein.EDL.hich is a component of the transport protein particle (TRAPP).ritically involved in endoplasmic reticulum-to-Golgi vesicle transport; mutations in the SEDL gene are associated with an X-linked skeletal disorder.pondyloepiphyseal dysplasia tarda . Another example is the assembly domain of clathrin coat proteins.uch as Mu2 adaptin (AP50) and Sigma2 adaptin (AP17).hich structurally resemble the longin domain. AP50 and AP17 are two of the proteins that make up the core of AP2. complex that functions in clathrin-mediated endocytosis .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
InterPro domains unassigned to SynO:
Clathrin-coated pits and vesicles originate from the plasma membrane and the trans-Golgi.nd mediate the trafficking of proteins to and from the membranes . The different vesicle types transport different proteins. Plasma membrane vesicles are involved in the endocytosis of membrane proteins.uch as LDL and EGF receptors and trans-Golgi vesicles are involved in protein sorting and regulated secretion. The main components of the pits are clathrin.nd the clathrin-associated protein complex.P.also known as assembly or adaptor proteins) . Both trans-Golgi adaptor proteins.P-1.nd plasma membrane adaptor heterotetramers that consist of two large chains (beta and gamma in AP-1.nd alpha and beta in AP-2); a medium chain (AP47 in AP-1.nd AP50 in AP-2); and a small chain (AP19 in AP-1.nd AP17 in AP-2). The adaptor complexes are believed to couple clathrin lattices with particular membrane proteins by interacting with their cytoplasmic tails.eading to their selection and concentration: the medium chains regulate this process by self-phosphorylation via a mechanism that is still unclear . The medium chains possess a highly conserved N-terminal domain of around 230 amino acids.hich may be the region of interaction with other AP proteins; a linker region of between 10 and 42 amino acids; and a less well-conserved C-terminal domain of around 190 amino acids.hich may be the site of specific interaction with the protein being transported in the vesicle .
  IPR001392:Clathrin adaptor complex, medium chain
Clathrin coated vesicles (CCV) mediate intracellular membrane traffic such as receptor mediated endocytosis. In addition to clathrin.he CCV are composed of a number of other components including oligomeric complexes which are known as adaptor or clathrin assembly proteins (AP) complexes . The adaptor complexes are believed to interact with the cytoplasmic tails of membrane proteins.eading to their selection and concentration. In mammals two type of adaptor complexes are known.P-1 which is associated with the Golgi complex and AP-2 which is associated with the plasma membrane. Both AP-1 and AP-2 are heterotetramers that consist of two large chains.he adaptins.gamma and beta in AP-1; alpha and beta in AP-2); a medium chain (AP47 in AP-1; AP50 in AP-2) and a small chain (AP19 in AP-1; AP17 in AP-2). The small chains of AP-1 and AP-2 are evolutionary related proteins of about 18 kD. Homologs of AP17 and AP19 have also been found in yeast (genes APS1/YAP19 and APS2/YAP17) . AP17 and AP19 are also related to the zeta-chain of coatomer (zeta-cop). cytosolic protein complex that reversibly associates with Golgi membranes to form vesicles that mediate biosynthetic protein transport from the endoplasmic reticulum.ia the Golgi up to the trans Golgi network. Some members of this family are part of the AP-3 complex.n adapter-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to the vacuole.
  IPR000804:Clathrin adaptor complex, small chain
SequencesProtein: AP3M1_HUMAN (418 aa)
mRNA: NM_207012
Local Annotation
Synapse Ontology
transport of vesicles in the presynaptic neuron
sdb:0017 Mobilization: synapsins, CAM kinase I  (Evidence:keywords,domains)
Fusion of intracellular membrane-bound vesicles with the pre-synaptic membrane of the neuronal cell resulting in release of neurotransmitter into the synaptic cleft.
sdb:0049 synaptic vesicle fusion  (Evidence:keywords,domains)
priming for exocytosis prepares the calcium-dependent release and may involve partial fusion process. The vesicles are primed and become responsive to calcium.
sdb:0120 priming  (Evidence:keywords,domains)
clathrin-coat uncoating means clathrin was shed from the budding vesicle membrane.
sdb:0122 clathrin-coat uncoating  (Evidence:keywords,domains)
attachment of the vesicle filled with transmitters involves a specific interaction between the vesicle membrane and the presynaptic active zone.
sdb:0148 docking  (Evidence:keywords,domains)
budding from endosome intermidate to generate fresh synaptic vesicles.
sdb:0158 budding from endosome  (Evidence:keywords,domains)
synaptic vesicles fuse with early endosomes as an intermediate sorting compartment to eliminate aged or missorted proteins.
sdb:0159 endosome fusion  (Evidence:keywords,domains)
sdb:0260 coat recruitment  (Evidence:keywords,domains)
the generation of action potential at soma of neurons.
sdb:0313 generation of AP at soma  (Evidence:keywords,domains)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 718 residues, 75551522-75553674Exon2: 50 residues, 75554143-75554288Exon3: 71 residues, 75555911-75556119Exon4: 46 residues, 75558871-75559005Exon5: 30 residues, 75559670-75559756Exon6: 48 residues, 75563790-75563928Exon7: 59 residues, 75566395-75566567Exon8: 94 residues, 75567870-75568146Exon9: 44 residues, 75568569-75568695Exon10: 93 residues, 75580518-75580793Exon11: 2 residues, -Jump to AP3M1_HUMAN  
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Loci Cluster (Details)Loci: 3900 75242264-75304344 ~-62K 5158(CAMK2G)(-)Loci: 3901 75551522-75580793 ~-29K 5169(AP3M1)(-)Loci: 3899 75074650-75085838 ~-11K 5150(SYNPO2L)(-)Link out to UCSC