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NUP107 NUP107 VIM VIM TNNC1 TNNC1 DES DES MYBPC2 MYBPC2 MYL2 MYL2 MYBPC1 MYBPC1 TNNC2 TNNC2 MYOM1 MYOM1 MYBPC3 MYBPC3 TMOD1 TMOD1 TCAP TCAP MYL9 MYL9 MYL3 MYL3 MYL4 MYL4 ACTN2 ACTN2 MYL6B MYL6B MYL1 MYL1 TTN TTN DMD DMD NEB NEB MYLPF MYLPF MYL5 MYL5 MYOD1 MYOD1 RB1 RB1 PAX3 PAX3
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:
MYL6Bmyosin, light chain 6B, alkali, smooth muscle and non-muscle; Regulatory light chain of myosin. Does not bind calcium (208 aa)
VIMvimentin (466 aa)
MYL2myosin, light chain 2, regulatory, cardiac, slow (166 aa)
NUP107nucleoporin 107kDa; Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. Required for the assembly of peripheral proteins into the NPC. May anchor NUP62 to the NPC (925 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)
MYOD1myogenic differentiation 1; Involved in muscle differentiation (myogenic factor). Induces fibroblasts to differentiate into myoblasts. Activates muscle-specific promoters. Interacts with and is inhibited by the twist protein. This interaction probably involves the basic domains of both proteins (By similarity) (320 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)
RB1retinoblastoma 1; Key regulator of entry into cell division that acts as a tumor suppressor. Promotes G0-G1 transition when phosphorylated by CDK3/cyclin-C. Acts as a transcription repressor of E2F1 target genes. The underphosphorylated, active form of RB1 interacts with E2F1 and represses its transcription activity, leading to cell cycle arrest. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases SUV39H1, SUV [...] (928 aa)
MYL9myosin, 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)
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)
MYLPFmyosin light chain, phosphorylatable, fast skeletal muscle (169 aa)
TTNtitin (33423 aa)
MYL4myosin, light chain 4, alkali; atrial, embryonic; Regulatory light chain of myosin. Does not bind calcium (197 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)
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)
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)
PAX3paired box 3 (505 aa)
NEBnebulin (8525 aa)
MYL5myosin, light chain 5, regulatory (173 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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