PDCL2 protein (Sus scrofa) - STRING interaction network

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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

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second shell of interactors

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proteins of unknown 3D structure

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a 3D structure is known or predicted

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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.

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[Homology]

Score

PDCL2

Phosducin like 2. (241 aa)

Predicted Functional Partners:

SHCBP1L

0.873

PRMT8

0.765

SPATA3

0.765

CCT2

0.720

CCT4

0.714

TCP1

0.703

CCT3

0.696

CCT7

0.693

HSD17B4

0.685

CYP21A2

0.680

Your Current Organism:

Sus scrofa

NCBI taxonomy Id: 9823
Other names: S. scrofa, pig, pigs, swine, wild boar

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... functional annotations:

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
CCT2	CCT3	ENSSSCP00000000527	ENSSSCP00000045371	Chaperonin containing TCP1 subunit 2.	T-complex protein 1 subunit gamma; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin.	0.999
CCT2	CCT4	ENSSSCP00000000527	ENSSSCP00000008941	Chaperonin containing TCP1 subunit 2.	T-complex protein 1 subunit delta.	0.999
CCT2	CCT7	ENSSSCP00000000527	ENSSSCP00000074465	Chaperonin containing TCP1 subunit 2.	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.	0.999
CCT2	PDCL2	ENSSSCP00000000527	ENSSSCP00000009502	Chaperonin containing TCP1 subunit 2.	Phosducin like 2.	0.720
CCT2	TCP1	ENSSSCP00000000527	ENSSSCP00000004374	Chaperonin containing TCP1 subunit 2.	Uncharacterized protein.	0.999
CCT3	CCT2	ENSSSCP00000045371	ENSSSCP00000000527	T-complex protein 1 subunit gamma; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin.	Chaperonin containing TCP1 subunit 2.	0.999
CCT3	CCT4	ENSSSCP00000045371	ENSSSCP00000008941	T-complex protein 1 subunit gamma; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin.	T-complex protein 1 subunit delta.	0.999
CCT3	CCT7	ENSSSCP00000045371	ENSSSCP00000074465	T-complex protein 1 subunit gamma; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin.	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.	0.999
CCT3	PDCL2	ENSSSCP00000045371	ENSSSCP00000009502	T-complex protein 1 subunit gamma; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin.	Phosducin like 2.	0.696
CCT3	TCP1	ENSSSCP00000045371	ENSSSCP00000004374	T-complex protein 1 subunit gamma; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin.	Uncharacterized protein.	0.999
CCT4	CCT2	ENSSSCP00000008941	ENSSSCP00000000527	T-complex protein 1 subunit delta.	Chaperonin containing TCP1 subunit 2.	0.999
CCT4	CCT3	ENSSSCP00000008941	ENSSSCP00000045371	T-complex protein 1 subunit delta.	T-complex protein 1 subunit gamma; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin.	0.999
CCT4	CCT7	ENSSSCP00000008941	ENSSSCP00000074465	T-complex protein 1 subunit delta.	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.	0.999
CCT4	PDCL2	ENSSSCP00000008941	ENSSSCP00000009502	T-complex protein 1 subunit delta.	Phosducin like 2.	0.714
CCT4	TCP1	ENSSSCP00000008941	ENSSSCP00000004374	T-complex protein 1 subunit delta.	Uncharacterized protein.	0.999
CCT7	CCT2	ENSSSCP00000074465	ENSSSCP00000000527	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.	Chaperonin containing TCP1 subunit 2.	0.999
CCT7	CCT3	ENSSSCP00000074465	ENSSSCP00000045371	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.	T-complex protein 1 subunit gamma; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin.	0.999
CCT7	CCT4	ENSSSCP00000074465	ENSSSCP00000008941	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.	T-complex protein 1 subunit delta.	0.999
CCT7	PDCL2	ENSSSCP00000074465	ENSSSCP00000009502	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.	Phosducin like 2.	0.693
CCT7	TCP1	ENSSSCP00000074465	ENSSSCP00000004374	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.	Uncharacterized protein.	0.999