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
0AP1M1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionAdaptor-related protein complex 1, mu 1 subunit (mu-adaptin 1) (adaptor protein complex ap-1 mu-1 subunit) (golgi adaptor ha1/ap1 adaptin mu-1 subunit) (clathrin assembly protein assembly protein complex 1 medium chain 1) (clathrin coat assembly protein ap47) (clathrin coat associated protein ap47) (ap-mu chain family member mu1a).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
Domain Architecture (Details)
InterPro domains assigned to SynO:
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
SequencesProtein: AP1M1_HUMAN (423 aa)
mRNA: AB209808 NM_032493
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)
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,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)
all the components of the clathrin coat, major ones are clathrin and clathrin adaptors.
sdb:0261 clathrin coat component  (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: 50 residues, 16169730-16169879Exon2: 54 residues, 16175269-16175426Exon3: 24 residues, 16178151-16178219Exon4: 45 residues, 16179829-16179960Exon5: 51 residues, 16180840-16180988Exon6: 44 residues, 16198231-16198358Exon7: 49 residues, 16199358-16199501Exon8: 26 residues, 16199947-16200019Exon9: 55 residues, 16200580-16200739Exon10: 44 residues, 16205303-16205429Exon11: 27 residues, 16206009-16206085Exon12: 310 residues, 16206223-16207149Exon13: 2 residues, -Jump to AP1M1_HUMANExon1: 46 residues, 16169744-16169879Exon2: 54 residues, 16175269-16175426Exon3: 24 residues, 16178151-16178219Exon4: 45 residues, 16179829-16179960Exon5: 51 residues, 16180840-16180988Exon6: 14 residues, 16182170-16182206Exon7: 44 residues, 16198231-16198358Exon8: 49 residues, 16199358-16199501Exon9: 26 residues, 16199947-16200019Exon10: 55 residues, 16200580-16200739Exon11: 44 residues, 16205303-16205429Exon12: 27 residues, 16206009-16206085Exon13: 313 residues, 16206223-16207156Exon14: 2 residues, -Jump to AP1M1_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 4372 14380630-14391171 ~-11K 18171(DDX39)(-)Loci: 3093 14430110-14443670 ~-14K 18178(+)Loci: 4373 14852137-14853264 ~-1K 18201(-)Loci: 4374 14921990-14944730 ~-23K 18203(SLC1A6)(-)Loci: 4375 15325340-15351603 ~-26K 18217(AKAP8)(-)Loci: 4376 15351858-15390833 ~-39K 18218(AKAP8L)(-)Loci: 3094 15699833-15700862 ~-1K 18230(OR10H2)(+)Loci: 4377 15778890-15779847 ~-1K 18231(OR10H1)(-)Loci: 3095 16083489-16105443 ~-22K 18238(RAB8A)(+)Loci: 3096 16169730-16207156 ~-37K 18242(AP1M1)(+)Loci: 4378 16333407-16443762 ~-110K 18245(EPS15L1)(-)Loci: 4371 14119550-14177997 ~-58K 18165(LPHN1)(-)Link out to UCSC