A0A182RM18 protein (Anopheles funestus) - STRING interaction network

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Score

A0A182RM18

ADF-H domain-containing protein. (163 aa)

Predicted Functional Partners:

A0A182R7S4

0.845

A0A182RRQ2

0.761

A0A182R8E2

0.732

A0A182RM36

0.697

A0A182RBT4

0.687

A0A182R3P8

0.566

A0A4Y0ALL7

0.566

A0A182RTN0

0.544

A0A182RGZ6

0.542

A0A182RHP0

0.537

Your Current Organism:

Anopheles funestus

NCBI taxonomy Id: 62324
Other names: A. funestus

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Browse interactions in tabular form:

node1	node2	node1 annotation	node2 annotation	score
A0A182R3P8	A0A182R7S4	Uncharacterized protein.	Adenylyl cyclase-associated protein; Belongs to the CAP family.	0.743
A0A182R3P8	A0A182R8E2	Uncharacterized protein.	Uncharacterized protein.	0.438
A0A182R3P8	A0A182RBT4	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.	0.923
A0A182R3P8	A0A182RM18	Uncharacterized protein.	ADF-H domain-containing protein.	0.566
A0A182R3P8	A0A182RM36	Uncharacterized protein.	Actin-related protein 2; ATP-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility. Seems to contact the pointed end of the daughter actin filament.	0.792
A0A182R3P8	A0A182RRQ2	Uncharacterized protein.	Uncharacterized protein.	0.449
A0A182R3P8	A0A182RTN0	Uncharacterized protein.	Uncharacterized protein; Belongs to the actin family.	0.796
A0A182R7S4	A0A182R3P8	Adenylyl cyclase-associated protein; Belongs to the CAP family.	Uncharacterized protein.	0.743
A0A182R7S4	A0A182RBT4	Adenylyl cyclase-associated protein; Belongs to the CAP family.	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.	0.727
A0A182R7S4	A0A182RM18	Adenylyl cyclase-associated protein; Belongs to the CAP family.	ADF-H domain-containing protein.	0.845
A0A182R7S4	A0A182RM36	Adenylyl cyclase-associated protein; Belongs to the CAP family.	Actin-related protein 2; ATP-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility. Seems to contact the pointed end of the daughter actin filament.	0.857
A0A182R7S4	A0A182RTN0	Adenylyl cyclase-associated protein; Belongs to the CAP family.	Uncharacterized protein; Belongs to the actin family.	0.851
A0A182R7S4	A0A4Y0ALL7	Adenylyl cyclase-associated protein; Belongs to the CAP family.	Uncharacterized protein.	0.743
A0A182R8E2	A0A182R3P8	Uncharacterized protein.	Uncharacterized protein.	0.438
A0A182R8E2	A0A182RM18	Uncharacterized protein.	ADF-H domain-containing protein.	0.732
A0A182R8E2	A0A182RM36	Uncharacterized protein.	Actin-related protein 2; ATP-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility. Seems to contact the pointed end of the daughter actin filament.	0.493
A0A182R8E2	A0A182RRQ2	Uncharacterized protein.	Uncharacterized protein.	0.620
A0A182R8E2	A0A182RTN0	Uncharacterized protein.	Uncharacterized protein; Belongs to the actin family.	0.479
A0A182R8E2	A0A4Y0ALL7	Uncharacterized protein.	Uncharacterized protein.	0.438
A0A182RBT4	A0A182R3P8	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.	0.923