• Version:
  • 11.0 [archived version]
STRINGSTRING
ITGB5 ITGB5 ITGA1 ITGA1 SORBS1 SORBS1 PXN PXN LMOD1 LMOD1 CALD1 CALD1 TLN1 TLN1 SORBS3 SORBS3 MYL6 MYL6 VCL VCL MYL7 MYL7 CDKN1B CDKN1B MYL10 MYL10 MYL12B MYL12B MYLK MYLK MYLPF MYLPF MYL5 MYL5 MYL6B MYL6B MYL9 MYL9 CBFB CBFB MYL1 MYL1 MYL3 MYL3 RUNX1 RUNX1 MYBPC3 MYBPC3 MYOM2 MYOM2 MYBPH MYBPH
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 Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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
Your Input:
VCLVinculin; Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell- surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion; Belongs to the vinculin/alpha-catenin family (1134 aa)
MYL10Myosin regulatory light chain 10; EF-hand domain containing (226 aa)
MYL7Myosin regulatory light chain 2, atrial isoform; EF-hand domain containing (175 aa)
CDKN1BCyclin-dependent kinase inhibitor 1B; Important regulator of cell cycle progression. Inhibits the kinase activity of CDK2 bound to cyclin A, but has little inhibitory activity on CDK2 bound to SPDYA. Involved in G1 arrest. Potent inhibitor of cyclin E- and cyclin A- CDK2 complexes. Forms a complex with cyclin type D-CDK4 complexes and is involved in the assembly, stability, and modulation of CCND1-CDK4 complex activation. Acts either as an inhibitor or an activator of cyclin type D-CDK4 complexes depending on its phosphorylation state and/or stoichometry; Belongs to the CDI family (198 aa)
SORBS3Vinexin; 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)
MYBPHMyosin-binding protein H; Binds to myosin; probably involved in interaction with thick myofilaments in the A-band; Fibronectin type III domain containing (477 aa)
MYOM2Myomesin-2; Major component of the vertebrate myofibrillar M band. Binds myosin, titin, and light meromyosin. This binding is dose dependent; Fibronectin type III domain containing (1465 aa)
PXNPaxillin; Cytoskeletal protein involved in actin-membrane attachment at sites of cell adhesion to the extracellular matrix (focal adhesion); Belongs to the paxillin family (605 aa)
MYL9Myosin regulatory light polypeptide 9; 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; EF-hand domain containing (172 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. Involved in anchorage-dependent, negative regulation of EGF-stimulated cell growth; CD molecules (1179 aa)
ITGB5Integrin beta-5; Integrin alpha-V/beta-5 (ITGAV-ITGB5) is a receptor for fibronectin. It recognizes the sequence R-G-D in its ligand (799 aa)
RUNX1Runt-related transcription factor 1; CBF binds to the core site, 5’-PYGPYGGT-3’, of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, LCK, IL-3 and GM-CSF promoters. The alpha subunit binds DNA and appears to have a role in the development of normal hematopoiesis. Isoform AML-1L interferes with the transactivation activity of RUNX1. Acts synergistically with ELF4 to transactivate the IL-3 promoter and with ELF2 to transactivate the mouse BLK promoter. Inhibits KAT6B- dependent transcriptional activation. Controls the [...] (480 aa)
MYL1Myosin light chain 1/3, skeletal muscle isoform; Regulatory light chain of myosin. Does not bind calcium; EF-hand domain containing (194 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); FERM domain containing (2541 aa)
MYLPFMyosin light chain, phosphorylatable, fast skeletal muscle; EF-hand domain containing (169 aa)
MYLKMyosin light chain kinase, smooth muscle; Calcium/calmodulin-dependent myosin light chain kinase implicated in smooth muscle contraction via phosphorylation of myosin light chains (MLC). Also regulates actin-myosin interaction through a non-kinase activity. Phosphorylates PTK2B/PYK2 and myosin light-chains. Involved in the inflammatory response (e.g. apoptosis, vascular permeability, leukocyte diapedesis), cell motility and morphology, airway hyperreactivity and other activities relevant to asthma. Required for tonic airway smooth muscle contraction that is necessary for physiological [...] (1914 aa)
CALD1Caldesmon; 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 mitosis [...] (793 aa)
LMOD1Leiomodin-1; Mediates nucleation of actin filaments; Belongs to the tropomodulin family (600 aa)
SORBS1Sorbin and SH3 domain-containing protein 1; Plays a role in tyrosine phosphorylation of CBL by linking CBL to the insulin receptor. Required for insulin- stimulated glucose transport. Involved in formation of actin stress fibers and focal adhesions (By similarity) (1292 aa)
MYL3Myosin light chain 3; Regulatory light chain of myosin. Does not bind calcium; EF-hand domain containing (195 aa)
MYL5Myosin light chain 5; EF-hand domain containing (173 aa)
CBFBCore-binding factor subunit beta; CBF binds to the core site, 5’-PYGPYGGT-3’, of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, LCK, IL3 and GM- CSF promoters. CBFB enhances DNA binding by RUNX1; Belongs to the CBF-beta family (187 aa)
MYBPC3Myosin-binding protein C, cardiac-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; Fibronectin type III domain containing (1274 aa)
MYL6Myosin light polypeptide 6; Regulatory light chain of myosin. Does not bind calcium; EF-hand domain containing (151 aa)
MYL6BMyosin light chain 6B; Regulatory light chain of myosin. Does not bind calcium; EF-hand domain containing (208 aa)
MYL12BMyosin regulatory light chain 12B; Myosin regulatory subunit that plays an important role in regulation of both smooth muscle and nonmuscle cell contractile activity via its phosphorylation. Phosphorylation triggers actin polymerization in vascular smooth muscle. Implicated in cytokinesis, receptor capping, and cell locomotion; EF-hand domain containing (172 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
Server load: low (2%) [HD]