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MYH4 MYH4 MYH10 MYH10 CGN CGN MYH13 MYH13 HSP90AA1 HSP90AA1 MYH9 MYH9 MYH2 MYH2 MYOM1 MYOM1 MYH1 MYH1 MYH15 MYH15 MYBPH MYBPH HSP90AB1 HSP90AB1 MYH7 MYH7 MYH11 MYH11 MYH6 MYH6 MYBPC2 MYBPC2 MYH3 MYH3 MYH14 MYH14 MYBPC3 MYBPC3 MYH8 MYH8 MYBPC1 MYBPC1 TMOD1 TMOD1 DES DES TCAP TCAP VIM VIM NEB NEB
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:
MYH9myosin, 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)
VIMvimentin (466 aa)
MYH1myosin, heavy chain 1, skeletal muscle, adult; Muscle contraction (1939 aa)
MYH3myosin, heavy chain 3, skeletal muscle, embryonic; Muscle contraction (1940 aa)
MYH2myosin, heavy chain 2, skeletal muscle, adult; Muscle contraction. Required for cytoskeleton organization (By similarity) (1941 aa)
MYH13myosin, heavy chain 13, skeletal muscle; Muscle contraction (1938 aa)
MYH4myosin, heavy chain 4, skeletal muscle; Muscle contraction (1939 aa)
MYBPHmyosin binding protein H; Binds to myosin; probably involved in interaction with thick myofilaments in the A-band (477 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)
MYH14myosin, heavy chain 14, non-muscle (2036 aa)
MYH10myosin, 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)
CGNcingulin; Probably plays a role in the formation and regulation of the tight junction (TJ) paracellular permeability barrier (1203 aa)
MYH15myosin, heavy chain 15; Muscle contraction (By similarity) (1946 aa)
TCAPtitin-cap; Muscle assembly regulating factor. Mediates the antiparallel assembly of titin (TTN) molecules at the sarcomeric Z-disk (167 aa)
HSP90AB1heat shock protein 90kDa alpha (cytosolic), class B member 1; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (724 aa)
HSP90AA1heat shock protein 90kDa alpha (cytosolic), class A member 1; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (854 aa)
MYH7myosin, heavy chain 7, cardiac muscle, beta (1935 aa)
MYH6myosin, heavy chain 6, cardiac muscle, alpha; Muscle contraction (1939 aa)
MYOM1myomesin 1; Major component of the vertebrate myofibrillar M band. Binds myosin, titin, and light meromyosin. This binding is dose dependent (1685 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)
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)
DESdesmin (470 aa)
MYH11myosin, heavy chain 11, smooth muscle; Muscle contraction (1979 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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