(8 nodes) Clathrin/coatomer adaptor, adaptin-like, N-terminal network (Beauveria bassiana ARSEF2860)

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Your Input:
	BBA_02410	Coatomer subunit gamma; The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin- coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. (917 aa)
	BBA_03134	AP-2 complex subunit alpha; 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, leading to their selection and concentration. (974 aa)
	BBA_07195	AP-3 complex subunit delta; Part of the AP-3 complex, an adaptor-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. (1017 aa)
	BBA_01770	AP complex subunit beta; 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, leading to their selection and concentration. (730 aa)
	BBA_07244	AP-1 complex subunit gamma. (852 aa)
	BBA_10192	Coatomer subunit beta; The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin- coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. (956 aa)
	BBA_01309	AP complex subunit beta; 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, leading to their selection and concentration. (748 aa)
	BBA_04557	AP-3 adaptor complex subunit beta. (778 aa)

Your Current Organism:

Beauveria bassiana ARSEF2860

NCBI taxonomy Id: 655819
Other names: B. bassiana ARSEF 2860, Beauveria bassiana ARSEF 2860

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
BBA_01309	BBA_03134	J4KQK1	J5JTX9	AP complex subunit beta; 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, leading to their selection and concentration.	AP-2 complex subunit alpha; 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, leading to their selection and concentration.	0.912
BBA_01309	BBA_04557	J4KQK1	J4UNH6	AP complex subunit beta; 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, leading to their selection and concentration.	AP-3 adaptor complex subunit beta.	0.651
BBA_01309	BBA_07195	J4KQK1	J5JL13	AP complex subunit beta; 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, leading to their selection and concentration.	AP-3 complex subunit delta; Part of the AP-3 complex, an adaptor-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.	0.923
BBA_01309	BBA_07244	J4KQK1	J4W068	AP complex subunit beta; 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, leading to their selection and concentration.	AP-1 complex subunit gamma.	0.954
BBA_01770	BBA_03134	J4WJ33	J5JTX9	AP complex subunit beta; 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, leading to their selection and concentration.	AP-2 complex subunit alpha; 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, leading to their selection and concentration.	0.979
BBA_01770	BBA_04557	J4WJ33	J4UNH6	AP complex subunit beta; 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, leading to their selection and concentration.	AP-3 adaptor complex subunit beta.	0.651
BBA_01770	BBA_07195	J4WJ33	J5JL13	AP complex subunit beta; 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, leading to their selection and concentration.	AP-3 complex subunit delta; Part of the AP-3 complex, an adaptor-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.	0.923
BBA_01770	BBA_07244	J4WJ33	J4W068	AP complex subunit beta; 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, leading to their selection and concentration.	AP-1 complex subunit gamma.	0.954
BBA_02410	BBA_07244	J5JUG6	J4W068	Coatomer subunit gamma; The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin- coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins.	AP-1 complex subunit gamma.	0.496
BBA_02410	BBA_10192	J5JUG6	J4KKQ2	Coatomer subunit gamma; The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin- coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins.	Coatomer subunit beta; The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin- coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins.	0.999
BBA_03134	BBA_01309	J5JTX9	J4KQK1	AP-2 complex subunit alpha; 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, leading to their selection and concentration.	AP complex subunit beta; 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, leading to their selection and concentration.	0.912
BBA_03134	BBA_01770	J5JTX9	J4WJ33	AP-2 complex subunit alpha; 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, leading to their selection and concentration.	AP complex subunit beta; 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, leading to their selection and concentration.	0.979
BBA_03134	BBA_07195	J5JTX9	J5JL13	AP-2 complex subunit alpha; 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, leading to their selection and concentration.	AP-3 complex subunit delta; Part of the AP-3 complex, an adaptor-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.	0.548
BBA_03134	BBA_07244	J5JTX9	J4W068	AP-2 complex subunit alpha; 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, leading to their selection and concentration.	AP-1 complex subunit gamma.	0.564
BBA_04557	BBA_01309	J4UNH6	J4KQK1	AP-3 adaptor complex subunit beta.	AP complex subunit beta; 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, leading to their selection and concentration.	0.651
BBA_04557	BBA_01770	J4UNH6	J4WJ33	AP-3 adaptor complex subunit beta.	AP complex subunit beta; 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, leading to their selection and concentration.	0.651
BBA_04557	BBA_07195	J4UNH6	J5JL13	AP-3 adaptor complex subunit beta.	AP-3 complex subunit delta; Part of the AP-3 complex, an adaptor-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.	0.998
BBA_04557	BBA_07244	J4UNH6	J4W068	AP-3 adaptor complex subunit beta.	AP-1 complex subunit gamma.	0.949
BBA_07195	BBA_01309	J5JL13	J4KQK1	AP-3 complex subunit delta; Part of the AP-3 complex, an adaptor-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.	AP complex subunit beta; 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, leading to their selection and concentration.	0.923
BBA_07195	BBA_01770	J5JL13	J4WJ33	AP-3 complex subunit delta; Part of the AP-3 complex, an adaptor-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.	AP complex subunit beta; 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, leading to their selection and concentration.	0.923