PLS3 protein (Anas platyrhynchos) - STRING interaction network

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Predicted Interactions

gene neighborhood

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textmining

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Score

PLS3

Plastin 3. (637 aa)

Predicted Functional Partners:

CAPZB

0.715

CORO1B

0.639

CORO1C

0.639

CNN3

0.628

MBTPS2

0.611

TMEM38B

0.610

P3H1

0.603

SEC24D

0.592

ENSAPLP00000018815

0.592

CAPZA1

0.588

Your Current Organism:

Anas platyrhynchos

NCBI taxonomy Id: 8840
Other names: A. platyrhynchos platyrhynchos, Anas platyrhynchos platyrhynchos, common mallard, northern mallard

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
CAPZA1	CAPZB	ENSAPLP00000024395	ENSAPLP00000024655	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.	F-actin-capping protein subunit beta; 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.	0.999
CAPZA1	CNN3	ENSAPLP00000024395	ENSAPLP00000028315	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.	Calponin; Thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin, troponin C and tropomyosin. The interaction of calponin with actin inhibits the actomyosin Mg-ATPase activity.	0.472
CAPZA1	PLS3	ENSAPLP00000024395	ENSAPLP00000010885	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.	Plastin 3.	0.588
CAPZB	CAPZA1	ENSAPLP00000024655	ENSAPLP00000024395	F-actin-capping protein subunit beta; 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.	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.	0.999
CAPZB	PLS3	ENSAPLP00000024655	ENSAPLP00000010885	F-actin-capping protein subunit beta; 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.	Plastin 3.	0.715
CNN3	CAPZA1	ENSAPLP00000028315	ENSAPLP00000024395	Calponin; Thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin, troponin C and tropomyosin. The interaction of calponin with actin inhibits the actomyosin Mg-ATPase activity.	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.	0.472
CNN3	PLS3	ENSAPLP00000028315	ENSAPLP00000010885	Calponin; Thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin, troponin C and tropomyosin. The interaction of calponin with actin inhibits the actomyosin Mg-ATPase activity.	Plastin 3.	0.628
CORO1B	PLS3	ENSAPLP00000026656	ENSAPLP00000010885	Coronin; Belongs to the WD repeat coronin family.	Plastin 3.	0.639
CORO1C	PLS3	ENSAPLP00000029629	ENSAPLP00000010885	Coronin 1C.	Plastin 3.	0.639
ENSAPLP00000018815	MBTPS2	ENSAPLP00000018815	ENSAPLP00000013220	Uncharacterized protein.	Membrane bound transcription factor peptidase, site 2.	0.619
ENSAPLP00000018815	P3H1	ENSAPLP00000018815	ENSAPLP00000003799	Uncharacterized protein.	Prolyl 3-hydroxylase 1.	0.615
ENSAPLP00000018815	PLS3	ENSAPLP00000018815	ENSAPLP00000010885	Uncharacterized protein.	Plastin 3.	0.592
ENSAPLP00000018815	TMEM38B	ENSAPLP00000018815	ENSAPLP00000028543	Uncharacterized protein.	Transmembrane protein 38B.	0.619
MBTPS2	ENSAPLP00000018815	ENSAPLP00000013220	ENSAPLP00000018815	Membrane bound transcription factor peptidase, site 2.	Uncharacterized protein.	0.619
MBTPS2	P3H1	ENSAPLP00000013220	ENSAPLP00000003799	Membrane bound transcription factor peptidase, site 2.	Prolyl 3-hydroxylase 1.	0.747
MBTPS2	PLS3	ENSAPLP00000013220	ENSAPLP00000010885	Membrane bound transcription factor peptidase, site 2.	Plastin 3.	0.611
MBTPS2	SEC24D	ENSAPLP00000013220	ENSAPLP00000001915	Membrane bound transcription factor peptidase, site 2.	SEC24 homolog D, COPII coat complex component.	0.619
MBTPS2	TMEM38B	ENSAPLP00000013220	ENSAPLP00000028543	Membrane bound transcription factor peptidase, site 2.	Transmembrane protein 38B.	0.749
P3H1	ENSAPLP00000018815	ENSAPLP00000003799	ENSAPLP00000018815	Prolyl 3-hydroxylase 1.	Uncharacterized protein.	0.615
P3H1	MBTPS2	ENSAPLP00000003799	ENSAPLP00000013220	Prolyl 3-hydroxylase 1.	Membrane bound transcription factor peptidase, site 2.	0.747