15 items (Manihot esculenta) - STRING interaction network

Nodes:

Network nodes represent proteins

splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.

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query proteins and first shell of interactors

white nodes:
second shell of interactors

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proteins of unknown 3D structure

filled nodes:
a 3D structure is known or predicted

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Edges represent protein-protein associations

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Predicted Interactions

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Your Input:
	A0A2C9V1B9	Tr-type G domain-containing protein. (1027 aa)
	A0A251J2Y7	Elongation factor 1-alpha; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. (449 aa)
	A0A251LAK3	Elongation factor 1-alpha; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. (449 aa)
	A0A2C9UI51	Tr-type G domain-containing protein. (843 aa)
	A0A2C9UJF2	Elongation factor Tu; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. (495 aa)
	A0A2C9UKD2	Elongation factor Tu; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. (489 aa)
	A0A2C9ULJ3	Tr-type G domain-containing protein. (989 aa)
	A0A2C9URU7	Elongation factor G, mitochondrial; Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. (758 aa)
	A0A2C9VQ15	Tr-type G domain-containing protein. (439 aa)
	A0A2C9VRM1	Tr-type G domain-containing protein. (843 aa)
	A0A2C9W7J6	Elongation factor 1-alpha; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. (449 aa)
	A0A2C9W915	Elongation factor 1-alpha; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. (449 aa)
	A0A2C9WAH3	Elongation factor G, chloroplastic; Chloroplast-localized elongation factor EF-G involved in protein synthesis in plastids. Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl- tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. (787 aa)
	A0A2C9WIK3	Elongation factor G, chloroplastic; Chloroplast-localized elongation factor EF-G involved in protein synthesis in plastids. Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl- tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. (787 aa)
	A0A2C9WN85	Tr-type G domain-containing protein. (464 aa)

Your Current Organism:

Manihot esculenta

NCBI taxonomy Id: 3983
Other names: M. esculenta, Manihot esculenta Crantz, Manihot utilissima, cassava, manioc, tapioca, yuca

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Browse interactions in tabular form:

node1	node2	node1 annotation	node2 annotation	score
A0A251J2Y7	A0A2C9UI51	Elongation factor 1-alpha; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis.	Tr-type G domain-containing protein.	0.736
A0A251J2Y7	A0A2C9ULJ3	Elongation factor 1-alpha; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis.	Tr-type G domain-containing protein.	0.695
A0A251J2Y7	A0A2C9URU7	Elongation factor 1-alpha; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis.	Elongation factor G, mitochondrial; Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.	0.632
A0A251J2Y7	A0A2C9V1B9	Elongation factor 1-alpha; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis.	Tr-type G domain-containing protein.	0.660
A0A251J2Y7	A0A2C9VRM1	Elongation factor 1-alpha; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis.	Tr-type G domain-containing protein.	0.736
A0A251J2Y7	A0A2C9WAH3	Elongation factor 1-alpha; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis.	Elongation factor G, chloroplastic; Chloroplast-localized elongation factor EF-G involved in protein synthesis in plastids. Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl- tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.	0.632
A0A251J2Y7	A0A2C9WIK3	Elongation factor 1-alpha; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis.	Elongation factor G, chloroplastic; Chloroplast-localized elongation factor EF-G involved in protein synthesis in plastids. Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl- tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.	0.632
A0A251J2Y7	A0A2C9WN85	Elongation factor 1-alpha; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis.	Tr-type G domain-containing protein.	0.465
A0A251LAK3	A0A2C9UI51	Elongation factor 1-alpha; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis.	Tr-type G domain-containing protein.	0.736
A0A251LAK3	A0A2C9ULJ3	Elongation factor 1-alpha; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis.	Tr-type G domain-containing protein.	0.695
A0A251LAK3	A0A2C9URU7	Elongation factor 1-alpha; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis.	Elongation factor G, mitochondrial; Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.	0.632
A0A251LAK3	A0A2C9V1B9	Elongation factor 1-alpha; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis.	Tr-type G domain-containing protein.	0.660
A0A251LAK3	A0A2C9VRM1	Elongation factor 1-alpha; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis.	Tr-type G domain-containing protein.	0.736
A0A251LAK3	A0A2C9W7J6	Elongation factor 1-alpha; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis.	Elongation factor 1-alpha; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis.	0.900
A0A251LAK3	A0A2C9W915	Elongation factor 1-alpha; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis.	Elongation factor 1-alpha; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis.	0.900
A0A251LAK3	A0A2C9WAH3	Elongation factor 1-alpha; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis.	Elongation factor G, chloroplastic; Chloroplast-localized elongation factor EF-G involved in protein synthesis in plastids. Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl- tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.	0.632
A0A251LAK3	A0A2C9WIK3	Elongation factor 1-alpha; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis.	Elongation factor G, chloroplastic; Chloroplast-localized elongation factor EF-G involved in protein synthesis in plastids. Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl- tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.	0.632
A0A251LAK3	A0A2C9WN85	Elongation factor 1-alpha; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis.	Tr-type G domain-containing protein.	0.465
A0A2C9UI51	A0A251J2Y7	Tr-type G domain-containing protein.	Elongation factor 1-alpha; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis.	0.736
A0A2C9UI51	A0A251LAK3	Tr-type G domain-containing protein.	Elongation factor 1-alpha; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis.	0.736