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 nodes:
protein of unknown 3D structure
protein of unknown 3D structure
large nodes:
some 3D structure is known or predicted
some 3D structure is known or predicted
Node Color
colored nodes:
query proteins and first shell of interactors
query proteins and first shell of interactors
white nodes:
second shell of interactors
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
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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Your Input:
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 | MYL6B | myosin, light chain 6B, alkali, smooth muscle and non-muscle; Regulatory light chain of myosin. Does not bind calcium (208 aa) | ||
 | MYL12A | myosin, light chain 12A, regulatory, non-sarcomeric; Myosin regulatory subunit that plays an important role in regulation of both smooth muscle and nonmuscle cell contractile activity via its phosphorylation. Implicated in cytokinesis, receptor capping, and cell locomotion (By similarity) (171 aa) | ||
 | VIM | vimentin (466 aa) | ||
 | MYL2 | myosin, light chain 2, regulatory, cardiac, slow (166 aa) | ||
 | TNNC1 | troponin 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) | ||
 | TMOD1 | tropomodulin 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) | ||
 | MYL9 | myosin, light chain 9, regulatory; Myosin regulatory subunit that plays an important role in regulation of both smooth muscle and nonmuscle cell contractile activity via its phosphorylation. Implicated in cytokinesis, receptor capping, and cell locomotion (172 aa) | ||
 | MYL3 | myosin, light chain 3, alkali; ventricular, skeletal, slow; Regulatory light chain of myosin. Does not bind calcium (195 aa) | ||
 | MYL1 | myosin, light chain 1, alkali; skeletal, fast; Regulatory light chain of myosin. Does not bind calcium (194 aa) | ||
 | CASP3 | caspase 3, apoptosis-related cysteine peptidase; Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a ’216-Asp-|-Gly-217’ bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop- helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage (277 aa) | ||
 | TCAP | titin-cap; Muscle assembly regulating factor. Mediates the antiparallel assembly of titin (TTN) molecules at the sarcomeric Z-disk (167 aa) | ||
 | MYLPF | myosin light chain, phosphorylatable, fast skeletal muscle (169 aa) | ||
 | TTN | titin (33423 aa) | ||
 | FIBP | fibroblast growth factor (acidic) intracellular binding protein; May be involved in mitogenic function of FGF1 (364 aa) | ||
 | UBC | ubiquitin C (685 aa) | ||
 | MYL4 | myosin, light chain 4, alkali; atrial, embryonic; Regulatory light chain of myosin. Does not bind calcium (197 aa) | ||
 | MYOM1 | myomesin 1; Major component of the vertebrate myofibrillar M band. Binds myosin, titin, and light meromyosin. This binding is dose dependent (1685 aa) | ||
 | MYBPC2 | myosin 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) | ||
 | MYBPC1 | myosin 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) | ||
 | DMD | dystrophin (3685 aa) | ||
 | ACTN2 | actinin, 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) | ||
 | TNNC2 | troponin 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) | ||
 | DES | desmin (470 aa) | ||
 | NEB | nebulin (8525 aa) | ||
 | MYL5 | myosin, light chain 5, regulatory (173 aa) | ||
 | MYBPC3 | myosin 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
Other names: H. sapiens, Homo, Homo sapiens, human, man
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