(6 nodes) Mixed, incl. Class II Aldolase and Adducin N-terminal domain, and FERM domain network (Canis lupus familiaris)

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.

Node Color

colored nodes:
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

Others

textmining

co-expression

protein homology

Your Input:
	TMOD1	Tropomodulin 1. (359 aa)
	ADD2	Adducin 2. (722 aa)
	DMTN	Dematin actin binding protein. (399 aa)
	GYPC	Glycophorin C. (76 aa)
	EPB41	Protein 4.1; Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes. Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase. (1039 aa)
	ADD1	Adducin 1. (825 aa)

Your Current Organism:

Canis lupus familiaris

NCBI taxonomy Id: 9615
Other names: C. lupus familiaris, Canis canis, Canis domesticus, Canis familiaris, beagle dog, beagle dogs, dog, dogs

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
ADD1	ADD2	ENSCAFP00000065621	ENSCAFP00000005087	Adducin 1.	Adducin 2.	0.963
ADD1	DMTN	ENSCAFP00000065621	ENSCAFP00000014298	Adducin 1.	Dematin actin binding protein.	0.857
ADD1	EPB41	ENSCAFP00000065621	ENSCAFP00000048815	Adducin 1.	Protein 4.1; Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes. Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase.	0.844
ADD1	GYPC	ENSCAFP00000065621	ENSCAFP00000036216	Adducin 1.	Glycophorin C.	0.681
ADD1	TMOD1	ENSCAFP00000065621	ENSCAFP00000003547	Adducin 1.	Tropomodulin 1.	0.856
ADD2	ADD1	ENSCAFP00000005087	ENSCAFP00000065621	Adducin 2.	Adducin 1.	0.963
ADD2	DMTN	ENSCAFP00000005087	ENSCAFP00000014298	Adducin 2.	Dematin actin binding protein.	0.891
ADD2	EPB41	ENSCAFP00000005087	ENSCAFP00000048815	Adducin 2.	Protein 4.1; Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes. Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase.	0.869
ADD2	GYPC	ENSCAFP00000005087	ENSCAFP00000036216	Adducin 2.	Glycophorin C.	0.586
ADD2	TMOD1	ENSCAFP00000005087	ENSCAFP00000003547	Adducin 2.	Tropomodulin 1.	0.765
DMTN	ADD1	ENSCAFP00000014298	ENSCAFP00000065621	Dematin actin binding protein.	Adducin 1.	0.857
DMTN	ADD2	ENSCAFP00000014298	ENSCAFP00000005087	Dematin actin binding protein.	Adducin 2.	0.891
DMTN	EPB41	ENSCAFP00000014298	ENSCAFP00000048815	Dematin actin binding protein.	Protein 4.1; Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes. Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase.	0.838
DMTN	GYPC	ENSCAFP00000014298	ENSCAFP00000036216	Dematin actin binding protein.	Glycophorin C.	0.440
DMTN	TMOD1	ENSCAFP00000014298	ENSCAFP00000003547	Dematin actin binding protein.	Tropomodulin 1.	0.708
EPB41	ADD1	ENSCAFP00000048815	ENSCAFP00000065621	Protein 4.1; Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes. Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase.	Adducin 1.	0.844
EPB41	ADD2	ENSCAFP00000048815	ENSCAFP00000005087	Protein 4.1; Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes. Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase.	Adducin 2.	0.869
EPB41	DMTN	ENSCAFP00000048815	ENSCAFP00000014298	Protein 4.1; Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes. Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase.	Dematin actin binding protein.	0.838
EPB41	GYPC	ENSCAFP00000048815	ENSCAFP00000036216	Protein 4.1; Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes. Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase.	Glycophorin C.	0.884
EPB41	TMOD1	ENSCAFP00000048815	ENSCAFP00000003547	Protein 4.1; Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes. Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase.	Tropomodulin 1.	0.582