(19 nodes) Clathrin/coatomer adaptor, adaptin-like, N-terminal network (Entamoeba histolytica)

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Your Input:
	72.t00024	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. (862 aa)
	287.t00007	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. (961 aa)
	EHI_173180	Coatomer subunit beta, putative. (406 aa)
	EHI_081400	AP-2 complex protein, putative. (541 aa)
	261.t00008	AP-1 complex subunit gamma. (855 aa)
	EHI_083430	Adapter-related protein complex 3 (AP-3) subunit, putative. (855 aa)
	EHI_158840	AP-3 complex subunit delta-1, putative. (111 aa)
	21.t00044	Adaptor protein (AP) family protein. (735 aa)
	250.t00004	AP-1 complex subunit gamma. (837 aa)
	34.t00015	AP-3 complex subunit delta. (1030 aa)
	168.t00014	Adaptor protein (AP) family protein. (874 aa)
	13.t00051	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. (908 aa)
	1.t00046	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. (843 aa)
	51.t00032	Coatomer beta subunit, putative. (910 aa)
	518.t00002	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. (844 aa)
	66.t00035	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. (848 aa)
	322.t00004	AP complex subunit beta; Belongs to the adaptor complexes large subunit family. (724 aa)
	EHI_013040	Adaptor protein (AP) family protein. (1091 aa)
	EHI_014390	AP-2 complex protein, putative. (582 aa)

Your Current Organism:

Entamoeba histolytica

NCBI taxonomy Id: 5759
Other names: E. histolytica

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
1.t00046	13.t00051	Q1EQ39	Q1EQ21	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-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.	0.437
1.t00046	21.t00044	Q1EQ39	C4LUG0	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.	Adaptor protein (AP) family protein.	0.446
1.t00046	250.t00004	Q1EQ39	C4LVA7	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.	0.446
1.t00046	261.t00008	Q1EQ39	Q1EQ23	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.	0.446
1.t00046	287.t00007	Q1EQ39	Q1EQ22	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-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.	0.437
1.t00046	51.t00032	Q1EQ39	Q1EQ38	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 beta subunit, putative.	0.575
1.t00046	518.t00002	Q1EQ39	Q1EQ36	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.	0.959
1.t00046	66.t00035	Q1EQ39	Q1EQ35	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.	0.959
1.t00046	72.t00024	Q1EQ39	Q1EQ20	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-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.	0.437
1.t00046	EHI_173180	Q1EQ39	B1N3Z7	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 beta, putative.	0.621
13.t00051	1.t00046	Q1EQ21	Q1EQ39	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.	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.	0.437
13.t00051	168.t00014	Q1EQ21	C4M5F2	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.	Adaptor protein (AP) family protein.	0.775
13.t00051	21.t00044	Q1EQ21	C4LUG0	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.	Adaptor protein (AP) family protein.	0.601
13.t00051	250.t00004	Q1EQ21	C4LVA7	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.	0.632
13.t00051	261.t00008	Q1EQ21	Q1EQ23	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.	0.601
13.t00051	287.t00007	Q1EQ21	Q1EQ22	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-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.	0.607
13.t00051	322.t00004	Q1EQ21	Q1EQ27	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; Belongs to the adaptor complexes large subunit family.	0.774
13.t00051	34.t00015	Q1EQ21	C4M1X4	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.	0.661
13.t00051	51.t00032	Q1EQ21	Q1EQ38	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.	Coatomer beta subunit, putative.	0.459
13.t00051	72.t00024	Q1EQ21	Q1EQ20	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-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.	0.601