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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 | MYH9 | myosin, heavy chain 9, non-muscle; Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping (1960 aa) | ||
 | VIM | vimentin (466 aa) | ||
 | MYH1 | myosin, heavy chain 1, skeletal muscle, adult; Muscle contraction (1939 aa) | ||
 | MYH3 | myosin, heavy chain 3, skeletal muscle, embryonic; Muscle contraction (1940 aa) | ||
 | MYH2 | myosin, heavy chain 2, skeletal muscle, adult; Muscle contraction. Required for cytoskeleton organization (By similarity) (1941 aa) | ||
 | TNNI2 | troponin 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) | ||
 | MYH4 | myosin, heavy chain 4, skeletal muscle; Muscle contraction (1939 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) | ||
 | MYH7B | myosin, heavy chain 7B, cardiac muscle, beta; Involved in muscle contraction (1983 aa) | ||
 | MYH10 | myosin, heavy chain 10, non-muscle; Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2 (1976 aa) | ||
 | TNNT3 | troponin T type 3 (skeletal, fast) (258 aa) | ||
 | TCAP | titin-cap; Muscle assembly regulating factor. Mediates the antiparallel assembly of titin (TTN) molecules at the sarcomeric Z-disk (167 aa) | ||
 | TTN | titin (33423 aa) | ||
 | MYH7 | myosin, heavy chain 7, cardiac muscle, beta (1935 aa) | ||
 | MYH6 | myosin, heavy chain 6, cardiac muscle, alpha; Muscle contraction (1939 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) | ||
 | TNNT2 | troponin 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) | ||
 | 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) | ||
 | TRIM63 | tripartite motif containing 63, E3 ubiquitin protein ligase; E3 ubiquitin ligase. Mediates the ubiquitination and subsequent proteasomal degradation of CKM, GMEB1 and HIBADH. Regulates the proteasomal degradation of muscle proteins under amino acid starvation, where muscle protein is catabolized to provide other organs with amino acids. Inhibits de novo skeletal muscle protein synthesis under amino acid starvation. Regulates proteasomal degradation of cardiac troponin I/TNNI3 and probably of other sarcomeric-associated proteins. May play a role in striated muscle atrophy and hypertroph [...] (353 aa) | ||
 | MYH11 | myosin, heavy chain 11, smooth muscle; Muscle contraction (1979 aa) | ||
 | NEB | nebulin (8525 aa) | ||
 | MYH8 | myosin, heavy chain 8, skeletal muscle, perinatal; Muscle contraction (1937 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) | ||
 | TNNT1 | troponin T type 1 (skeletal, slow); Troponin T is the tropomyosin-binding subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity (278 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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