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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 | VIM | vimentin (466 aa) | ||
 | MYH3 | myosin, heavy chain 3, skeletal muscle, embryonic; Muscle contraction (1940 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) | ||
 | 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) | ||
 | 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) | ||
 | THOC3 | THO complex 3; Component of the THO subcomplex of the TREX complex. The TREX complex specifically associates with spliced mRNA and not with unspliced pre-mRNA. It is recruited to spliced mRNAs by a transcription-independent mechanism. Binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5’ end of the mRNA where it functions in mRNA export. The recruitment occurs via an interaction between ALYREF/THOC4 and the cap-binding protein NCBP1. DDX39B functions as a bridge between ALYREF/THOC4 and the THO complex [...] (351 aa) | ||
 | TPM1 | tropomyosin 1 (alpha) (284 aa) | ||
 | TNNT3 | troponin T type 3 (skeletal, fast) (258 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) | ||
 | TCAP | titin-cap; Muscle assembly regulating factor. Mediates the antiparallel assembly of titin (TTN) molecules at the sarcomeric Z-disk (167 aa) | ||
 | TNNI1 | troponin I type 1 (skeletal, slow) (187 aa) | ||
 | TNNI3 | troponin I type 3 (cardiac); Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity (210 aa) | ||
 | TTN | titin (33423 aa) | ||
 | UBC | ubiquitin C (685 aa) | ||
 | TPM4 | tropomyosin 4 (284 aa) | ||
 | MYL4 | myosin, light chain 4, alkali; atrial, embryonic; Regulatory light chain of myosin. Does not bind calcium (197 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) | ||
 | TPM2 | tropomyosin 2 (beta); Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments. The non-muscle isoform may have a role in agonist-mediated receptor internalization (By similarity) (284 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) | ||
 | MAGOH | mago-nashi homolog, proliferation-associated (Drosophila); Component of a splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of a few core proteins and several more peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Core components of the EJC, that remains bound to spliced mRNAs throughout all stages of mRNA metabolism, functions to mark the position of the exon-exon junction in the mature mR [...] (146 aa) | ||
 | THOC5 | THO complex 5; Component the THO subcomplex of the TREX complex. The TREX complex specifically associates with spliced mRNA and not with unspliced pre-mRNA. It is recruited to spliced mRNAs by a transcription-independent mechanism. Binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5’ end of the mRNA where it functions in mRNA export. The recruitment occurs via an interaction between ALYREF/THOC4 and the cap-binding protein NCBP1. The TREX complex is essential for the export of Kaposi’s sarcoma-associa [...] (683 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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