S4RIG8_PETMA protein (Petromyzon marinus) - STRING interaction network

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Score

S4RIG8_PETMA

CAP-ZIP_m domain-containing protein. (1050 aa)

Predicted Functional Partners:

S4RCJ6_PETMA

0.977

S4RGL3_PETMA

0.972

S4RDB4_PETMA

0.971

S4RWC9_PETMA

0.969

S4R4P9_PETMA

0.958

S4RE17_PETMA

0.876

S4RW17_PETMA

0.858

S4RJQ7_PETMA

0.841

S4R8G2_PETMA

0.779

S4RKW0_PETMA

0.766

Your Current Organism:

Petromyzon marinus

NCBI taxonomy Id: 7757
Other names: P. marinus, marine lamprey, sea lamprey, sea lampreys

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
S4R4P9_PETMA	S4RCJ6_PETMA	ENSPMAP00000000178	ENSPMAP00000002928	Vacuolar protein sorting-associated protein 35; Plays a role in vesicular protein sorting.	Vacuolar protein sorting-associated protein 29; Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway.	0.999
S4R4P9_PETMA	S4RDB4_PETMA	ENSPMAP00000000178	ENSPMAP00000003196	Vacuolar protein sorting-associated protein 35; Plays a role in vesicular protein sorting.	WASH complex subunit 4.	0.705
S4R4P9_PETMA	S4RGL3_PETMA	ENSPMAP00000000178	ENSPMAP00000004345	Vacuolar protein sorting-associated protein 35; Plays a role in vesicular protein sorting.	WASH complex subunit 3.	0.622
S4R4P9_PETMA	S4RIG8_PETMA	ENSPMAP00000000178	ENSPMAP00000005000	Vacuolar protein sorting-associated protein 35; Plays a role in vesicular protein sorting.	CAP-ZIP_m domain-containing protein.	0.958
S4R4P9_PETMA	S4RKW0_PETMA	ENSPMAP00000000178	ENSPMAP00000005843	Vacuolar protein sorting-associated protein 35; Plays a role in vesicular protein sorting.	VPS26, retromer complex component A.	0.999
S4R4P9_PETMA	S4RWC9_PETMA	ENSPMAP00000000178	ENSPMAP00000009519	Vacuolar protein sorting-associated protein 35; Plays a role in vesicular protein sorting.	WASH complex subunit 5.	0.854
S4R8G2_PETMA	S4RE17_PETMA	ENSPMAP00000001493	ENSPMAP00000003449	DNA topoisomerase II binding protein 1.	Si:dkey-119f1.1.	0.609
S4R8G2_PETMA	S4RIG8_PETMA	ENSPMAP00000001493	ENSPMAP00000005000	DNA topoisomerase II binding protein 1.	CAP-ZIP_m domain-containing protein.	0.779
S4R8G2_PETMA	S4RW17_PETMA	ENSPMAP00000001493	ENSPMAP00000009407	DNA topoisomerase II binding protein 1.	NSE1 homolog, SMC5-SMC6 complex component.	0.446
S4RCJ6_PETMA	S4R4P9_PETMA	ENSPMAP00000002928	ENSPMAP00000000178	Vacuolar protein sorting-associated protein 29; Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway.	Vacuolar protein sorting-associated protein 35; Plays a role in vesicular protein sorting.	0.999
S4RCJ6_PETMA	S4RDB4_PETMA	ENSPMAP00000002928	ENSPMAP00000003196	Vacuolar protein sorting-associated protein 29; Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway.	WASH complex subunit 4.	0.525
S4RCJ6_PETMA	S4RGL3_PETMA	ENSPMAP00000002928	ENSPMAP00000004345	Vacuolar protein sorting-associated protein 29; Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway.	WASH complex subunit 3.	0.642
S4RCJ6_PETMA	S4RIG8_PETMA	ENSPMAP00000002928	ENSPMAP00000005000	Vacuolar protein sorting-associated protein 29; Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway.	CAP-ZIP_m domain-containing protein.	0.977
S4RCJ6_PETMA	S4RKW0_PETMA	ENSPMAP00000002928	ENSPMAP00000005843	Vacuolar protein sorting-associated protein 29; Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway.	VPS26, retromer complex component A.	0.999
S4RCJ6_PETMA	S4RWC9_PETMA	ENSPMAP00000002928	ENSPMAP00000009519	Vacuolar protein sorting-associated protein 29; Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway.	WASH complex subunit 5.	0.918
S4RDB4_PETMA	S4R4P9_PETMA	ENSPMAP00000003196	ENSPMAP00000000178	WASH complex subunit 4.	Vacuolar protein sorting-associated protein 35; Plays a role in vesicular protein sorting.	0.705
S4RDB4_PETMA	S4RCJ6_PETMA	ENSPMAP00000003196	ENSPMAP00000002928	WASH complex subunit 4.	Vacuolar protein sorting-associated protein 29; Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway.	0.525
S4RDB4_PETMA	S4RGL3_PETMA	ENSPMAP00000003196	ENSPMAP00000004345	WASH complex subunit 4.	WASH complex subunit 3.	0.996
S4RDB4_PETMA	S4RIG8_PETMA	ENSPMAP00000003196	ENSPMAP00000005000	WASH complex subunit 4.	CAP-ZIP_m domain-containing protein.	0.971
S4RDB4_PETMA	S4RJQ7_PETMA	ENSPMAP00000003196	ENSPMAP00000005440	WASH complex subunit 4.	F-actin-capping protein subunit alpha; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.	0.857