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TCAP TCAP TMOD1 TMOD1 DES DES TMOD4 TMOD4 VIM VIM MYBPC2 MYBPC2 MYBPC1 MYBPC1 TTN TTN MYBPC3 MYBPC3 MYH1 MYH1 ACTC1 ACTC1 MYH8 MYH8 MYH7B MYH7B TPM1 TPM1 ITGA1 ITGA1 MYH2 MYH2 MYH4 MYH4 MYLK MYLK TLN1 TLN1 ITGB5 ITGB5 ACTA2 ACTA2 LMOD1 LMOD1 TMOD3 TMOD3 CALD1 CALD1 SORBS3 SORBS3 SORBS1 SORBS1
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)
ACTA2actin, alpha 2, smooth muscle, aorta; Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells (377 aa)
MYH1myosin, heavy chain 1, skeletal muscle, adult; Muscle contraction (1939 aa)
SORBS3sorbin and SH3 domain containing 3; Vinexin alpha isoform promotes up-regulation of actin stress fiber formation. Vinexin beta isoform plays a role in cell spreading and enhances the activation of JNK/SAPK in response to EGF stimulation by using its third SH3 domain (671 aa)
MYH2myosin, heavy chain 2, skeletal muscle, adult; Muscle contraction. Required for cytoskeleton organization (By similarity) (1941 aa)
MYH4myosin, heavy chain 4, skeletal muscle; Muscle contraction (1939 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)
MYH7Bmyosin, heavy chain 7B, cardiac muscle, beta; Involved in muscle contraction (1983 aa)
TPM1tropomyosin 1 (alpha) (284 aa)
ITGA1integrin, alpha 1; Integrin alpha-1/beta-1 is a receptor for laminin and collagen. It recognizes the proline-hydroxylated sequence G-F-P-G- E-R in collagen (1179 aa)
ACTC1actin, alpha, cardiac muscle 1; Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells (377 aa)
TMOD4tropomodulin 4 (muscle); 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 (345 aa)
ITGB5integrin, beta 5; Integrin alpha-V/beta-5 is a receptor for fibronectin. It recognizes the sequence R-G-D in its ligand (799 aa)
TMOD3tropomodulin 3 (ubiquitous); 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 (By similarity) (352 aa)
TCAPtitin-cap; Muscle assembly regulating factor. Mediates the antiparallel assembly of titin (TTN) molecules at the sarcomeric Z-disk (167 aa)
TLN1talin 1; Probably involved in connections of major cytoskeletal structures to the plasma membrane. High molecular weight cytoskeletal protein concentrated at regions of cell-substratum contact and, in lymphocytes, at cell-cell contacts (By similarity) (2541 aa)
TTNtitin (33423 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)
MYLKmyosin light chain kinase (1914 aa)
CALD1caldesmon 1; Actin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). Stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, inhibits the actomyosin ATPase by binding to F-actin. This inhibition is attenuated by calcium-calmodulin and is potentiated by tropomyosin. Interacts with actin, myosin, two molecules of tropomyosin and with calmodulin. Also play an essential role during cellular mitos [...] (793 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)
SORBS1sorbin and SH3 domain containing 1 (1292 aa)
LMOD1leiomodin 1 (smooth muscle) (600 aa)
DESdesmin (470 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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