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0CN108_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionProtein c14orf108 (putative hiv-1 infection-related protein).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
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
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: CN108_HUMAN (490 aa)
mRNA: NM_018229
Local Annotation
Synapse Ontology
clathrin-coat uncoating means clathrin was shed from the budding vesicle membrane.
sdb:0122 clathrin-coat uncoating  (Evidence:domains)
budding from endosome intermidate to generate fresh synaptic vesicles.
sdb:0158 budding from endosome  (Evidence:domains)
synaptic vesicles fuse with early endosomes as an intermediate sorting compartment to eliminate aged or missorted proteins.
sdb:0159 endosome fusion  (Evidence:domains)
sdb:0260 coat recruitment  (Evidence:domains)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 161 residues, 56805379-56805859Exon2: 217 residues, 56810714-56811360Exon3: 78 residues, 56816665-56816893Exon4: 48 residues, 56818559-56818699Exon5: 30 residues, 56819404-56819490Exon6: 41 residues, 56819582-56819701Exon7: 34 residues, 56822693-56822790Exon8: 426 residues, 56825272-56826544Exon9: 2 residues, -Jump to CN108_HUMAN  
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