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MYBPC3 MYBPC3 TNNI1 TNNI1 TNNI2 TNNI2 MYBPC1 MYBPC1 NEB NEB TNNC1 TNNC1 MYBPC2 MYBPC2 TCAP TCAP DES DES TNNT2 TNNT2 VIM VIM PRKX PRKX TTN TTN DMD DMD TMOD1 TMOD1 EFHA2 EFHA2 TNNI3 TNNI3 PPP2R5E PPP2R5E PPP2R2C PPP2R2C PPP2R3B PPP2R3B PPP2R5C PPP2R5C PPP2R3C PPP2R3C PPP2R5A PPP2R5A PPP2CA PPP2CA PPP2R5D PPP2R5D PPP2R5B PPP2R5B
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:
PPP2R5Bprotein phosphatase 2, regulatory subunit B’, beta; The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. The phosphorylated form mediates the interaction between AKT1 and PP2A phosphatase leading to dephosphorylation of AKT1 on the ’Thr-308’ and ’Ser-373’ residues (497 aa)
VIMvimentin (466 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)
TNNI2troponin 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)
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)
PPP2R5Aprotein phosphatase 2, regulatory subunit B’, alpha; The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment (486 aa)
PPP2R3Cprotein phosphatase 2, regulatory subunit B’’, gamma (453 aa)
PRKXprotein kinase, X-linked; Serine/threonine protein kinase regulated by and mediating cAMP signaling in cells. Acts through phosphorylation of downstream targets that may include CREB, SMAD6 and PKD1 and has multiple functions in cellular differentiation and epithelial morphogenesis. Regulates myeloid cell differentiation through SMAD6 phosphorylation. Involved in nephrogenesis by stimulating renal epithelial cell migration and tubulogenesis. Also involved in angiogenesis through stimulation of endothelial cell proliferation, migration and vascular-like structure formation (358 aa)
TCAPtitin-cap; Muscle assembly regulating factor. Mediates the antiparallel assembly of titin (TTN) molecules at the sarcomeric Z-disk (167 aa)
EFHA2EF-hand domain family, member A2; May play a role in mitochondrial calcium uptake (By similarity) (530 aa)
PPP2R2Cprotein phosphatase 2, regulatory subunit B, gamma; The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment (447 aa)
TNNI1troponin I type 1 (skeletal, slow) (187 aa)
PPP2R5Eprotein phosphatase 2, regulatory subunit B’, epsilon isoform; The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment (467 aa)
TNNI3troponin 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)
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)
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)
TNNT2troponin 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)
DESdesmin (470 aa)
PPP2R3Bprotein phosphatase 2, regulatory subunit B’’, beta; The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment (575 aa)
NEBnebulin (8525 aa)
PPP2R5Cprotein phosphatase 2, regulatory subunit B’, gamma; The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. The PP2A-PPP2R5C holoenzyme may specifically dephosphorylate and activate TP53 and play a role in DNA damage- induced inhibition of cell proliferation. PP2A-PPP2R5C may also regulate the ERK signaling pathway through ERK dephosphorylation (555 aa)
PPP2R5Dprotein phosphatase 2, regulatory subunit B’, delta; The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment (602 aa)
PPP2CAprotein phosphatase 2, catalytic subunit, alpha isozyme; PP2A is the major phosphatase for microtubule-associated proteins (MAPs). PP2A can modulate the activity of phosphorylase B kinase casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase. Cooperates with SGOL2 to protect centromeric cohesin from separase-mediated cleavage in oocytes specifically during meiosis I (By similarity). Can dephosphorylate SV40 large T antigen and p53/TP53. Activates RAF1 by dephosphorylating it at ’Ser-259’ (309 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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