33 items (Caenorhabditis elegans) - 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.

Node Color

colored nodes:
query proteins and first shell of interactors

white nodes:
second shell of interactors

Node Content

empty nodes:
proteins of unknown 3D structure

filled nodes:
a 3D structure is known or predicted

Edges:

Edges represent protein-protein associations

associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.

Known Interactions

from curated databases

experimentally determined

Predicted Interactions

gene neighborhood

gene fusions

gene co-occurrence

Others

textmining

co-expression

protein homology

Your Input:
	pfd-1	Probable prefoldin subunit 1; Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins (By similarity). Has a role in gonadogenesis; Belongs to the prefoldin subunit beta family. (117 aa)
	fkb-4	Peptidylprolyl isomerase. (259 aa)
	agef-1	SEC7 domain-containing protein. (1594 aa)
	mau-8	Phosducin domain-containing protein. (258 aa)
	cct-8	T-complex protein 1 subunit theta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity). Required for correct subcellular localization of pgl-1; Belongs to the TCP-1 chaperonin family. (548 aa)
	cct-2	T-complex protein 1 subunit beta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin; Belongs to the TCP-1 chaperonin family. (529 aa)
	T11G6.5	Uncharacterized protein. (1406 aa)
	cct-7	T-complex protein 1 subunit eta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. (535 aa)
	pfd-3	Probable prefoldin subunit 3; Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins (By similarity); Belongs to the prefoldin subunit alpha family. (185 aa)
	cct-1	T-complex protein 1 subunit alpha; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. (549 aa)
	kin-10	Casein kinase II subunit beta; Participates in Wnt signaling. Plays a complex role in regulating the basal catalytic activity of the alpha subunit (By similarity). Modulates two aspects of male mating behavior; response to hermaphrodite contact and vulval location, acting in the same pathway as lov-1 and pkd-2; Belongs to the casein kinase 2 subunit beta family. (235 aa)
	pfd-5	Probable prefoldin subunit 5; Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins (By similarity); Belongs to the prefoldin subunit alpha family. (152 aa)
	R09H10.5	Uncharacterized protein. (1621 aa)
	pfd-2	Prefoldin subunit 2; Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins (By similarity); Belongs to the prefoldin subunit beta family. (141 aa)
	egl-30	Heterotrimeric G protein alpha subunit. (355 aa)
	gpc-1	Guanine nucleotide-binding protein subunit gamma; Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. (62 aa)
	cct-3	T-complex protein 1 subunit gamma; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis (By similarity). Known to play a role, in vitro, in the folding of actin and tubulin (By similarity). Plays a role in microtubule polymerization. (543 aa)
	apm-3	MHD domain-containing protein; Belongs to the adaptor complexes medium subunit family. (414 aa)
	gpb-2	Guanine nucleotide-binding protein subunit beta-2; Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. (369 aa)
	egl-10	Regulator of G-protein signaling egl-10; Involved in egg-laying and locomotion. May regulate G protein goa-1 signaling. (639 aa)
	pfd-6	Probable prefoldin subunit 6; Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins (By similarity). Required for positioning of the mitotic spindle. (126 aa)
	gpb-1	Guanine nucleotide-binding protein subunit beta-1; Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. In the early embryo, controls the magnitude of the forces acting on centrosomes but is not required for generating asymmetric forces. (340 aa)
	gpc-2	G protein gamma domain-containing protein. (62 aa)
	cct-6	T-complex protein 1 subunit zeta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity). (539 aa)
	fkb-5	Peptidylprolyl isomerase. (300 aa)
	eat-16	Uncharacterized protein. (473 aa)
	cct-5	T-complex protein 1 subunit epsilon; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. (542 aa)
	C05D12.3	Uncharacterized protein. (1039 aa)
	C05D12.2	Uncharacterized protein. (1036 aa)
	fkb-3	Peptidylprolyl isomerase. (261 aa)
	kin-3	Casein kinase II subunit alpha; Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. The alpha chain contains the catalytic site. May participate in Wnt signaling. Modulates two aspects of male mating behavior; response to hermaphrodite contact and vulval location, acting in the same pathway as lov-1 and pkd-2. (360 aa)
	pfd-4	Probable prefoldin subunit 4; Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins (By similarity); Belongs to the prefoldin subunit beta family. (126 aa)
	cct-4	T-complex protein 1 subunit delta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. (540 aa)

Your Current Organism:

Caenorhabditis elegans

NCBI taxonomy Id: 6239
Other names: C. elegans, Rhabditis elegans, roundworm

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
C05D12.2	T11G6.5	C05D12.2.1	T11G6.5a.1	Uncharacterized protein.	Uncharacterized protein.	0.436
C05D12.2	cct-1	C05D12.2.1	T05C12.7.1	Uncharacterized protein.	T-complex protein 1 subunit alpha; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.	0.559
C05D12.2	cct-2	C05D12.2.1	T21B10.7.2	Uncharacterized protein.	T-complex protein 1 subunit beta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin; Belongs to the TCP-1 chaperonin family.	0.566
C05D12.2	cct-3	C05D12.2.1	F54A3.3.1	Uncharacterized protein.	T-complex protein 1 subunit gamma; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis (By similarity). Known to play a role, in vitro, in the folding of actin and tubulin (By similarity). Plays a role in microtubule polymerization.	0.568
C05D12.2	cct-4	C05D12.2.1	K01C8.10.1	Uncharacterized protein.	T-complex protein 1 subunit delta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.	0.599
C05D12.2	cct-5	C05D12.2.1	C07G2.3a.1	Uncharacterized protein.	T-complex protein 1 subunit epsilon; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.	0.479
C05D12.2	cct-6	C05D12.2.1	F01F1.8a.1	Uncharacterized protein.	T-complex protein 1 subunit zeta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity).	0.441
C05D12.2	cct-7	C05D12.2.1	T10B5.5a.2	Uncharacterized protein.	T-complex protein 1 subunit eta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.	0.551
C05D12.2	cct-8	C05D12.2.1	Y55F3AR.3a.1	Uncharacterized protein.	T-complex protein 1 subunit theta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity). Required for correct subcellular localization of pgl-1; Belongs to the TCP-1 chaperonin family.	0.476
C05D12.2	pfd-2	C05D12.2.1	H20J04.5.1	Uncharacterized protein.	Prefoldin subunit 2; Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins (By similarity); Belongs to the prefoldin subunit beta family.	0.857
C05D12.2	pfd-3	C05D12.2.1	T06G6.9.1	Uncharacterized protein.	Probable prefoldin subunit 3; Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins (By similarity); Belongs to the prefoldin subunit alpha family.	0.854
C05D12.2	pfd-4	C05D12.2.1	B0035.4.2	Uncharacterized protein.	Probable prefoldin subunit 4; Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins (By similarity); Belongs to the prefoldin subunit beta family.	0.856
C05D12.2	pfd-5	C05D12.2.1	R151.9.1	Uncharacterized protein.	Probable prefoldin subunit 5; Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins (By similarity); Belongs to the prefoldin subunit alpha family.	0.897
C05D12.2	pfd-6	C05D12.2.1	F21C3.5.1	Uncharacterized protein.	Probable prefoldin subunit 6; Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins (By similarity). Required for positioning of the mitotic spindle.	0.943
C05D12.3	T11G6.5	C05D12.3a.2	T11G6.5a.1	Uncharacterized protein.	Uncharacterized protein.	0.436
C05D12.3	cct-1	C05D12.3a.2	T05C12.7.1	Uncharacterized protein.	T-complex protein 1 subunit alpha; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.	0.559
C05D12.3	cct-2	C05D12.3a.2	T21B10.7.2	Uncharacterized protein.	T-complex protein 1 subunit beta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin; Belongs to the TCP-1 chaperonin family.	0.566
C05D12.3	cct-3	C05D12.3a.2	F54A3.3.1	Uncharacterized protein.	T-complex protein 1 subunit gamma; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis (By similarity). Known to play a role, in vitro, in the folding of actin and tubulin (By similarity). Plays a role in microtubule polymerization.	0.568
C05D12.3	cct-4	C05D12.3a.2	K01C8.10.1	Uncharacterized protein.	T-complex protein 1 subunit delta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.	0.599
C05D12.3	cct-5	C05D12.3a.2	C07G2.3a.1	Uncharacterized protein.	T-complex protein 1 subunit epsilon; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.	0.479