LCP1 protein (Callithrix jacchus) - 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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second shell of interactors

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Known Interactions

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experimentally determined

Predicted Interactions

gene neighborhood

gene fusions

gene co-occurrence

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textmining

co-expression

protein homology

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[Homology]

Score

LCP1

Plastin-2. (627 aa)

Predicted Functional Partners:

CAPZB

0.778

ENSCJAP00000075757

0.658

CTSF

0.656

ACTA2

0.656

ACTC1

0.656

ACTA1

0.656

CXADR

0.651

TACSTD2

0.645

LAPTM5

0.645

HCLS1

0.637

Your Current Organism:

Callithrix jacchus

NCBI taxonomy Id: 9483
Other names: C. jacchus, Callithrix jacchus jacchus, common marmoset, white ear-tufted marmoset, white-tufted-ear marmoset

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
ACTA1	CAPZB	ENSCJAP00000075679	ENSCJAP00000059185	Actin alpha 1, skeletal muscle.	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.	0.678
ACTA1	LCP1	ENSCJAP00000075679	ENSCJAP00000031005	Actin alpha 1, skeletal muscle.	Plastin-2.	0.656
ACTA2	CAPZB	ENSCJAP00000010246	ENSCJAP00000059185	Actin alpha 2, smooth muscle.	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.	0.678
ACTA2	LCP1	ENSCJAP00000010246	ENSCJAP00000031005	Actin alpha 2, smooth muscle.	Plastin-2.	0.656
ACTC1	CAPZB	ENSCJAP00000020535	ENSCJAP00000059185	Uncharacterized protein.	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.	0.678
ACTC1	LCP1	ENSCJAP00000020535	ENSCJAP00000031005	Uncharacterized protein.	Plastin-2.	0.656
CAPZB	ACTA1	ENSCJAP00000059185	ENSCJAP00000075679	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.	Actin alpha 1, skeletal muscle.	0.678
CAPZB	ACTA2	ENSCJAP00000059185	ENSCJAP00000010246	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.	Actin alpha 2, smooth muscle.	0.678
CAPZB	ACTC1	ENSCJAP00000059185	ENSCJAP00000020535	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.	Uncharacterized protein.	0.678
CAPZB	HCLS1	ENSCJAP00000059185	ENSCJAP00000015637	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.	Hematopoietic cell-specific Lyn substrate 1.	0.433
CAPZB	LCP1	ENSCJAP00000059185	ENSCJAP00000031005	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-2.	0.778
CTSF	CXADR	ENSCJAP00000002331	ENSCJAP00000062535	Cathepsin F; Belongs to the peptidase C1 family.	CXADR Ig-like cell adhesion molecule.	0.582
CTSF	ENSCJAP00000075757	ENSCJAP00000002331	ENSCJAP00000075757	Cathepsin F; Belongs to the peptidase C1 family.	Uncharacterized protein.	0.605
CTSF	LCP1	ENSCJAP00000002331	ENSCJAP00000031005	Cathepsin F; Belongs to the peptidase C1 family.	Plastin-2.	0.656
CTSF	TACSTD2	ENSCJAP00000002331	ENSCJAP00000062065	Cathepsin F; Belongs to the peptidase C1 family.	Tumor associated calcium signal transducer 2.	0.600
CXADR	CTSF	ENSCJAP00000062535	ENSCJAP00000002331	CXADR Ig-like cell adhesion molecule.	Cathepsin F; Belongs to the peptidase C1 family.	0.582
CXADR	ENSCJAP00000075757	ENSCJAP00000062535	ENSCJAP00000075757	CXADR Ig-like cell adhesion molecule.	Uncharacterized protein.	0.624
CXADR	LCP1	ENSCJAP00000062535	ENSCJAP00000031005	CXADR Ig-like cell adhesion molecule.	Plastin-2.	0.651
CXADR	TACSTD2	ENSCJAP00000062535	ENSCJAP00000062065	CXADR Ig-like cell adhesion molecule.	Tumor associated calcium signal transducer 2.	0.599
ENSCJAP00000075757	CTSF	ENSCJAP00000075757	ENSCJAP00000002331	Uncharacterized protein.	Cathepsin F; Belongs to the peptidase C1 family.	0.605