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STRINGSTRING
TNNI2 TNNI2 MYBPC3 MYBPC3 TNNI1 TNNI1 TCAP TCAP MYL3 MYL3 MYBPC1 MYBPC1 TNNI3 TNNI3 MYL1 MYL1 TPM2 TPM2 TNNC1 TNNC1 TNNC2 TNNC2 VIM VIM TPM3 TPM3 TPM4 TPM4 TNNT3 TNNT3 MYL4 MYL4 TPM1 TPM1 ACTN2 ACTN2 MYH6 MYH6 TNNT2 TNNT2 DES DES DMD DMD NEB NEB TMOD1 TMOD1 MYBPC2 MYBPC2 MYH8 MYH8
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 Size
small protein node
small nodes:
protein of unknown 3D structure
large protein node
large nodes:
some 3D structure is known or predicted
Node Color
colored protein node
colored nodes:
query proteins and first shell of interactors
non-colored protein node
white nodes:
second shell of interactors
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 each other.
Known Interactions
database edge
from curated databases
experiment edge
experimentally determined
Predicted Interactions
neighborhood edge
gene neighborhood
fusion edge
gene fusions
cooccurrence edge
gene co-occurrence
Others
textmining edge
textmining
coexpression edge
co-expression
homology edge
protein homology
Your Input:
VIMvimentin (466 aa)
TNNC1troponin C type 1 (slow); Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components- Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments (161 aa)
TNNI2troponin I type 2 (skeletal, fast); Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity (182 aa)
TMOD1tropomodulin 1; Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton. May play an important role in regulating the organization of actin filaments by preferentially binding to a specific tropomyosin isoform at its N-terminus (359 aa)
TPM1tropomyosin 1 (alpha) (284 aa)
TNNT3troponin T type 3 (skeletal, fast) (258 aa)
MYL3myosin, light chain 3, alkali; ventricular, skeletal, slow; Regulatory light chain of myosin. Does not bind calcium (195 aa)
MYL1myosin, light chain 1, alkali; skeletal, fast; Regulatory light chain of myosin. Does not bind calcium (194 aa)
TCAPtitin-cap; Muscle assembly regulating factor. Mediates the antiparallel assembly of titin (TTN) molecules at the sarcomeric Z-disk (167 aa)
TNNI1troponin I type 1 (skeletal, slow) (187 aa)
TNNI3troponin I type 3 (cardiac); Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity (210 aa)
TPM4tropomyosin 4 (284 aa)
MYL4myosin, light chain 4, alkali; atrial, embryonic; Regulatory light chain of myosin. Does not bind calcium (197 aa)
MYH6myosin, heavy chain 6, cardiac muscle, alpha; Muscle contraction (1939 aa)
MYBPC2myosin binding protein C, fast type; Thick filament-associated protein located in the crossbridge region of vertebrate striated muscle a bands. In vitro it binds MHC, F-actin and native thin filaments, and modifies the activity of actin-activated myosin ATPase. It may modulate muscle contraction or may play a more structural role (1141 aa)
TPM2tropomyosin 2 (beta); Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments. The non-muscle isoform may have a role in agonist-mediated receptor internalization (By similarity) (284 aa)
MYBPC1myosin binding protein C, slow type; Thick filament-associated protein located in the crossbridge region of vertebrate striated muscle a bands. In vitro it binds MHC, F-actin and native thin filaments, and modifies the activity of actin-activated myosin ATPase. It may modulate muscle contraction or may play a more structural role (1171 aa)
DMDdystrophin (3685 aa)
ACTN2actinin, alpha 2; F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein (894 aa)
TNNT2troponin T type 2 (cardiac); Troponin T is the tropomyosin-binding subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity (288 aa)
TPM3tropomyosin 3; Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments (285 aa)
TNNC2troponin C type 2 (fast); Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components- Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments (160 aa)
DESdesmin (470 aa)
NEBnebulin (8525 aa)
MYH8myosin, heavy chain 8, skeletal muscle, perinatal; Muscle contraction (1937 aa)
MYBPC3myosin binding protein C, cardiac; Thick filament-associated protein located in the crossbridge region of vertebrate striated muscle a bands. In vitro it binds MHC, F-actin and native thin filaments, and modifies the activity of actin-activated myosin ATPase. It may modulate muscle contraction or may play a more structural role (1274 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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