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0AP1G1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionAdapter-related protein complex 1 gamma 1 subunit (gamma-adaptin) (adaptor protein complex ap-1 gamma-1 subunit) (golgi adaptor ha1/ap1 adaptin gamma-1 subunit) (clathrin assembly protein complex 1 gamma-1 large chain).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005794 Golgi apparatus (IDA)
0030119 membrane coat adaptor complex (TAS)
0005215 transporter activity (TAS)
0006886 intracellular protein transport (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 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
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
This domain consists of a multi-helical fold comprised of two curved layers of alpha helices arranged in a regular right-handed 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
SequencesProtein: AP1G1_HUMAN (821 aa)
mRNA: NM_001128
Local Annotation
Synapse Ontology
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)
all the components of the clathrin coat, major ones are clathrin and clathrin adaptors.
sdb:0261 clathrin coat component  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 1386 residues, 70320407-70324563Exon2: 35 residues, 70326012-70326111Exon3: 55 residues, 70330345-70330506Exon4: 38 residues, 70330637-70330745Exon5: 44 residues, 70336547-70336674Exon6: 49 residues, 70336876-70337018Exon7: 37 residues, 70337991-70338096Exon8: 44 residues, 70339654-70339782Exon9: 32 residues, 70341297-70341387Exon10: 43 residues, 70341613-70341736Exon11: 20 residues, 70345236-70345291Exon12: 49 residues, 70347422-70347563Exon13: 40 residues, 70350211-70350325Exon14: 20 residues, 70352915-70352971Exon15: 35 residues, 70355753-70355852Exon16: 29 residues, 70356049-70356130Exon17: 34 residues, 70356892-70356988Exon18: 27 residues, 70361026-70361103Exon19: 34 residues, 70362559-70362656Exon20: 49 residues, 70364624-70364766Exon21: 43 residues, 70365871-70365996Exon22: 70 residues, 70380682-70380886Exon23: 105 residues, 70400166-70400477Exon24: 2 residues, -Jump to AP1G1_HUMAN  
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