node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
BcDW1_2811 | BcDW1_4855 | M7UNJ1 | M7TS73 | 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 |
BcDW1_2811 | BcDW1_5923 | M7UNJ1 | M7TW30 | 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. | 0.503 |
BcDW1_3553 | BcDW1_5923 | M7ULQ2 | M7TW30 | 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. | 0.956 |
BcDW1_3553 | BcDW1_7101 | M7ULQ2 | M7UC83 | 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. | Putative ap-3 adaptor complex subunit beta protein. | 0.675 |
BcDW1_3553 | BcDW1_7890 | M7ULQ2 | M7TIX3 | 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. | 0.909 |
BcDW1_3553 | BcDW1_98 | M7ULQ2 | M7U624 | 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. | 0.973 |
BcDW1_4855 | BcDW1_2811 | M7TS73 | M7UNJ1 | 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. | 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. | 0.999 |
BcDW1_4855 | BcDW1_5923 | M7TS73 | M7TW30 | 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. | AP-1 complex subunit gamma. | 0.747 |
BcDW1_4855 | BcDW1_7890 | M7TS73 | M7TIX3 | 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. | 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. | 0.681 |
BcDW1_5923 | BcDW1_2811 | M7TW30 | M7UNJ1 | AP-1 complex subunit gamma. | 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. | 0.503 |
BcDW1_5923 | BcDW1_3553 | M7TW30 | M7ULQ2 | AP-1 complex subunit gamma. | 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. | 0.956 |
BcDW1_5923 | BcDW1_4855 | M7TW30 | M7TS73 | AP-1 complex subunit gamma. | 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. | 0.747 |
BcDW1_5923 | BcDW1_6995 | M7TW30 | M7TSU8 | AP-1 complex subunit gamma. | 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. | 0.956 |
BcDW1_5923 | BcDW1_7101 | M7TW30 | M7UC83 | AP-1 complex subunit gamma. | Putative ap-3 adaptor complex subunit beta protein. | 0.961 |
BcDW1_5923 | BcDW1_7890 | M7TW30 | M7TIX3 | AP-1 complex subunit gamma. | 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. | 0.537 |
BcDW1_5923 | BcDW1_98 | M7TW30 | M7U624 | AP-1 complex subunit gamma. | 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. | 0.558 |
BcDW1_6995 | BcDW1_5923 | M7TSU8 | M7TW30 | 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. | 0.956 |
BcDW1_6995 | BcDW1_7101 | M7TSU8 | M7UC83 | 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. | Putative ap-3 adaptor complex subunit beta protein. | 0.675 |
BcDW1_6995 | BcDW1_7890 | M7TSU8 | M7TIX3 | 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. | 0.909 |
BcDW1_6995 | BcDW1_98 | M7TSU8 | M7U624 | 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. | 0.902 |