Relation Results

Summary

Name AP-1 complex
Primary ID SIGNOR-C248
Links CPX-5047
Type complex
Formed by AP1M1, AP1S1, AP1G1, AP1B1
Relations 8

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Type: Score: Layout: SPV 
0.20.8160.4420.8880.8140.8630.4910.2RAB38AP-1 complexAP1G1SORT1AP1M1AP1B1AP1S1AP-1/clathrin vescicleRAB32

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Relations
Regulator
Mechanism
target
score ℹ
+ RAB38up-regulates activity img/direct-activation.png relocalization AP-1 complex 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-260701 Homo sapiens
pmid sentence
Rab32 and Rab38 interact physically and colocalize with BLOC-2, AP-1 and AP-3|These results indicate that Rab32 and Rab38 operate in the same pathways previously defined for AP-1, AP-3 and BLOC-2 and suggest they are the specific proteins that divert AP-1, AP-3 and BLOC-2-dependent cargoes to maturing melanosomes and away from lysosomes.
Publications: 1 Organism: Homo Sapiens
+ AP1G1form complex img/form-complex.png binding AP-1 complex 0.816
Identifier Residue Sequence Organism Cell Line
SIGNOR-260687 Homo sapiens
pmid sentence
Key components of this system are the heterotetrameric adaptor protein (AP)4 complexes, AP-1 (gamma-beta1-mi1-sigma1), AP-2 (α-beta2-mi2-sigma2), AP-3 (delta-beta3-mi3-sigma3), and AP-4 (epsilon-beta4-mi4-sigma4) (subunit composition shown in parentheses)
Publications: 1 Organism: Homo Sapiens
+ AP-1 complexup-regulates quantity img/direct-activation.png binding SORT1 0.442
Identifier Residue Sequence Organism Cell Line
SIGNOR-273720 Homo sapiens HEK-293 Cell
pmid sentence
The short intracellular domain of sortilin binds several cytoplasmic adaptor proteins (e.g., the AP-1 complex and GGA1 to -3), most of which target two well-defined motifs: a C-terminal acidic cluster dileucine motif and a YXXΦ motif in the proximal third of the domain. Both motifs contribute to endocytosis as well as Golgi-endosome trafficking of sortilin.
Publications: 1 Organism: Homo Sapiens
+ AP1M1form complex img/form-complex.png binding AP-1 complex 0.888
Identifier Residue Sequence Organism Cell Line
SIGNOR-260686 Homo sapiens
pmid sentence
Key components of this system are the heterotetrameric adaptor protein (AP)4 complexes, AP-1 (gamma-beta1-mi1-sigma1), AP-2 (α-beta2-mi2-sigma2), AP-3 (delta-beta3-mi3-sigma3), and AP-4 (epsilon-beta4-mi4-sigma4) (subunit composition shown in parentheses)
Publications: 1 Organism: Homo Sapiens
+ AP1B1form complex img/form-complex.png binding AP-1 complex 0.814
Identifier Residue Sequence Organism Cell Line
SIGNOR-260685 Homo sapiens
pmid sentence
Key components of this system are the heterotetrameric adaptor protein (AP)4 complexes, AP-1 (gamma-beta1-mi1-sigma1), AP-2 (α-beta2-mi2-sigma2), AP-3 (delta-beta3-mi3-sigma3), and AP-4 (epsilon-beta4-mi4-sigma4) (subunit composition shown in parentheses)
Publications: 1 Organism: Homo Sapiens
+ AP1S1form complex img/form-complex.png binding AP-1 complex 0.863
Identifier Residue Sequence Organism Cell Line
SIGNOR-260684 Homo sapiens
pmid sentence
Key components of this system are the heterotetrameric adaptor protein (AP)4 complexes, AP-1 (gamma-beta1-mi1-sigma1), AP-2 (α-beta2-mi2-sigma2), AP-3 (delta-beta3-mi3-sigma3), and AP-4 (epsilon-beta4-mi4-sigma4) (subunit composition shown in parentheses)
Publications: 1 Organism: Homo Sapiens
+ AP-1 complexform complex img/form-complex.png binding AP-1/clathrin vescicle 0.491
Identifier Residue Sequence Organism Cell Line
SIGNOR-260674 Homo sapiens
pmid sentence
Clathrin-coated pits and vesicles are diffraction-limited objects with typical diameters ranging between 75 and 130 nm. The smaller ∼75 nm coats contain at least 36 copies of clathrin, a heterohexameric protein of three heavy chains and three light chains, and about half that number of copies of the heterotetrameric AP adaptor complex | Intracellular clathrin-coated vesicles contain AP1 or AP3 adaptors
Publications: 1 Organism: Homo Sapiens
+ RAB32up-regulates activity img/direct-activation.png relocalization AP-1 complex 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-260700 Homo sapiens
pmid sentence
Rab32 and Rab38 interact physically and colocalize with BLOC-2, AP-1 and AP-3|These results indicate that Rab32 and Rab38 operate in the same pathways previously defined for AP-1, AP-3 and BLOC-2 and suggest they are the specific proteins that divert AP-1, AP-3 and BLOC-2-dependent cargoes to maturing melanosomes and away from lysosomes.
Publications: 1 Organism: Homo Sapiens
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