YRC Logo
PROTEIN SEARCH:
Descriptions Names[Advanced Search]

Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules). Interacting selectively and non-covalently with any protein component of any cytoskeleton (actin, microtubule, or intermediate filament cytoskeleton). Interacting selectively and non-covalently with nebulette, a 107 kDa protein associated with the I-Z-I complex of cardiac myofibrils. It shows a high degree of homology with skeletal muscle nebulin. Interacting selectively and non-covalently with any protein involved in modulating the reorganization of the cytoskeleton. Interacting selectively and non-covalently with any part of a dynactin complex; dynactin is a large protein complex that activates dynein-based motor activity. Interacting selectively and non-covalently with actinin, any member of a family of proteins that crosslink F-actin. Interacting selectively and non-covalently with a family of FATZ proteins, filamin-, actinin-, and telethonin-binding proteins of the Z-disc of striated muscle. FATZ proteins are located in the Z-disc of the sarcomere and are involved in a complex network of interactions with other Z-band components. Interacting selectively and non-covalently with monomeric or multimeric forms of tubulin, including microtubules. Interacting selectively and non-covalently with a filamin, any member of a family of high molecular mass cytoskeletal proteins that crosslink actin filaments to form networks and stress fibers. Filamins contain an amino-terminal alpha-actinin-like actin binding domain, which is followed by a rod-domain composed of 4 to 24 100-residue repetitive segments including a carboxy-terminal dimerization domain. Interacting selectively and non-covalently with tropomyosin, a protein associated with actin filaments both in cytoplasm and, in association with troponin, in the thin filament of striated muscle. The binding activity of a molecule that brings together a cytoskeletal molecule and one or more other molecules, permitting them to function in a coordinated way. Interacting selectively and non-covalently wih ALP, actinin-associated LIM protein of the Z band. ALP is a PDZ/LIM domain protein found in the Z band. Interacting selectively and non-covalently with tau protein. tau is a microtubule-associated protein, implicated in Alzheimer's disease, Down Syndrome and ALS. Interacting selectively and non-covalently with telethonin, a protein found in the Z disc of striated muscle and which is a substrate of the titin kinase. Interacting selectively and non-covalently with ankyrin, a 200 kDa cytoskeletal protein that attaches other cytoskeletal proteins to integral membrane proteins. Interacting selectively and non-covalently with nebulin, a large protein (approximately 800kD) that is anchored at the Z-disc by its C-terminal region and spans the length of the thin filament, ending at the edge of the H-zone. Interacting selectively and non-covalently with spectrin, a protein that is the major constituent of the erythrocyte cytoskeletal network. It associates with band 4.1 (see band protein) and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane. It is composed of nonhomologous chains, alpha and beta, which aggregate side-to-side in an antiparallel fashion to form dimers, tetramers, and higher polymers. Interacting selectively and non-covalently with monomeric or multimeric forms of actin, including actin filaments. Interacting selectively and non-covalently with myotilin, a structural component of the Z-discs in human skeletal and cardiac muscle. Its C-terminus contains two immunoglobulin-like domains and the unique N-terminal half has a serine-rich region, with numerous potential phosphorylation sites, and a stretch of hydrophobic amino acids. Myotilin forms homodimers and binds to alpha-actinin, F-actin, and filamin C. Interacting selectively and non-covalently with titin, any of a family of giant proteins found in striated and smooth muscle. In striated muscle, single titin molecules span half the sarcomere, with their N- and C-termini in the Z-disc and M-line, respectively. Interacting selectively and non-covalently with Z-band alternatively spliced PDZ motif protein (ZASP). ZASP is a Z-band protein specifically expressed in heart and skeletal muscle. This protein contains N-terminal PDZ domain and C-terminal LIM domain. Interacting selectively and non-covalently with troponin C, the calcium-binding subunit of the troponin complex. Interacting selectively and non-covalently with troponin T, the tropomyosin-binding subunit of the troponin complex. Interacting selectively and non-covalently with troponin I, the inhibitory subunit of the troponin complex. The selective, non-covalent, often stoichiometric, interaction of a molecule with one or more specific sites on another molecule. Interacting selectively and non-covalently with vinculin, a protein found in muscle, fibroblasts, and epithelial cells that binds actin and appears to mediate attachment of actin filaments to integral proteins of the plasma membrane. Interacting selectively and non-covalently with any part of a myosin complex; myosins are any of a superfamily of molecular motor proteins that bind to actin and use the energy of ATP hydrolysis to generate force and movement along actin filaments. Interacting selectively and non-covalently and stoichiometrically with kinesin, a cytoplasmic protein responsible for moving vesicles and organelles towards the distal end of microtubules. Interacting selectively and non-covalently with myopalladin, a myofibrillar protein with titin-like Ig domains.

View Gene Ontology (GO) Term

GO TERM SUMMARY
Name: cytoskeletal protein binding
Acc: GO:0008092
Aspect: Molecular Function
Desc: Interacting selectively and non-covalently with any protein component of any cytoskeleton (actin, microtubule, or intermediate filament cytoskeleton).
Proteins in PDR annotated with:
   This term: 283 [Search]
   Term or descendants: 1925 [Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0008092 - cytoskeletal protein binding (interactive image map)
YRC Informatics Platform - Version 3.0
Created and Maintained by: Michael Riffle