(31 nodes) Cortical actin cytoskeleton organization network (Rhinocladiella mackenziei)

Nodes:

Network nodes represent proteins

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

white nodes:
second shell of interactors

Node Content

empty nodes:
proteins of unknown 3D structure

filled nodes:
a 3D structure is known or predicted

Edges:

Edges represent protein-protein associations

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.

Known Interactions

from curated databases

experimentally determined

Predicted Interactions

gene neighborhood

gene fusions

gene co-occurrence

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textmining

co-expression

protein homology

Your Input:
	Z518_01319	annotation not available (967 aa)
	Z518_00889	Actin-related protein 2/3 complex subunit 3; Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. (188 aa)
	Z518_11045	annotation not available (751 aa)
	Z518_01676	annotation not available (375 aa)
	Z518_01318	annotation not available (457 aa)
	Z518_02903	annotation not available (429 aa)
	Z518_06384	annotation not available (448 aa)
	Z518_09574	Arp2/3 complex 34 kDa subunit; Functions as actin-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. (319 aa)
	Z518_09363	Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family. (1252 aa)
	Z518_10284	annotation not available (196 aa)
	Z518_04552	Clathrin heavy chain; Clathrin is the major protein of the polyhedral coat of coated pits and vesicles; Belongs to the clathrin heavy chain family. (1679 aa)
	Z518_01215	Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family. (1335 aa)
	Z518_01622	annotation not available (1791 aa)
	Z518_03017	Belongs to the actin family. (457 aa)
	Z518_06023	annotation not available (1058 aa)
	Z518_04432	Actin-related protein 2/3 complex subunit 5; Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Arp2/3 complex plays a critical role in the control of cell morphogenesis via the modulation of cell polarity development. (192 aa)
	Z518_06536	annotation not available (1001 aa)
	Z518_06316	annotation not available (653 aa)
	Z518_07930	annotation not available (271 aa)
	Z518_08981	annotation not available (1195 aa)
	Z518_08802	annotation not available (1128 aa)
	Z518_07963	annotation not available (991 aa)
	Z518_09804	annotation not available (822 aa)
	Z518_01522	annotation not available (275 aa)
	Z518_00515	annotation not available (667 aa)
	Z518_02213	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. (388 aa)
	Z518_01531	annotation not available (749 aa)
	Z518_05067	Actin-related protein 2/3 complex subunit; Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks; Belongs to the WD repeat ARPC1 family. (363 aa)
	Z518_07739	annotation not available (870 aa)
	Z518_00079	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. (273 aa)
	Z518_08104	annotation not available (147 aa)

Your Current Organism:

Rhinocladiella mackenziei

NCBI taxonomy Id: 1442369
Other names: R. mackenziei CBS 650.93, Rhinocladiella mackenziei CBS 650.93

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
Z518_00079	Z518_00515	A0A0D2J069	A0A0D2JJ48	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.	annotation not available	0.769
Z518_00079	Z518_00889	A0A0D2J069	A0A0D2HGJ8	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-related protein 2/3 complex subunit 3; Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks.	0.848
Z518_00079	Z518_01318	A0A0D2J069	A0A0D2G5Q1	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.	annotation not available	0.608
Z518_00079	Z518_01319	A0A0D2J069	A0A0D2HHS2	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.	annotation not available	0.608
Z518_00079	Z518_01522	A0A0D2J069	A0A0D2JLU3	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.	annotation not available	0.676
Z518_00079	Z518_01531	A0A0D2J069	A0A0D2HIF2	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.	annotation not available	0.769
Z518_00079	Z518_01676	A0A0D2J069	A0A0D2G6K8	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.	annotation not available	0.966
Z518_00079	Z518_02213	A0A0D2J069	A0A0D2JEG9	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-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.	0.855
Z518_00079	Z518_03017	A0A0D2J069	A0A0D2IY84	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.	Belongs to the actin family.	0.919
Z518_00079	Z518_04432	A0A0D2J069	A0A0D2ITH2	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-related protein 2/3 complex subunit 5; Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Arp2/3 complex plays a critical role in the control of cell morphogenesis via the modulation of cell polarity development.	0.502
Z518_00079	Z518_05067	A0A0D2J069	A0A0D2JD59	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-related protein 2/3 complex subunit; Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks; Belongs to the WD repeat ARPC1 family.	0.635
Z518_00079	Z518_08981	A0A0D2J069	A0A0D2IDE4	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.	annotation not available	0.866
Z518_00079	Z518_09574	A0A0D2J069	A0A0D2FIJ1	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.	Arp2/3 complex 34 kDa subunit; Functions as actin-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks.	0.840
Z518_00515	Z518_00079	A0A0D2JJ48	A0A0D2J069	annotation not available	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.	0.769
Z518_00515	Z518_01215	A0A0D2JJ48	A0A0D2IVR7	annotation not available	Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family.	0.863
Z518_00515	Z518_01522	A0A0D2JJ48	A0A0D2JLU3	annotation not available	annotation not available	0.636
Z518_00515	Z518_01676	A0A0D2JJ48	A0A0D2G6K8	annotation not available	annotation not available	0.908
Z518_00515	Z518_02213	A0A0D2JJ48	A0A0D2JEG9	annotation not available	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.	0.670
Z518_00515	Z518_03017	A0A0D2JJ48	A0A0D2IY84	annotation not available	Belongs to the actin family.	0.637
Z518_00515	Z518_06536	A0A0D2JJ48	A0A0D2II96	annotation not available	annotation not available	0.497