BP

GO:0032233

positive regulation of actin filament bundle assembly

Any process that activates or increases the frequency, rate or extent of the assembly of actin filament bundles.

IBA

CC

GO:0005634

nucleus

A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

IBA|ISS

CC

GO:0005925

focal adhesion

Small region on the surface of a cell that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments.

IDA

CC

GO:0015629

actin cytoskeleton

The part of the cytoskeleton (the internal framework of a cell) composed of actin and associated proteins. Includes actin cytoskeleton-associated complexes.

IBA|IDA

CC

GO:0030018

Z disc

Platelike region of a muscle sarcomere to which the plus ends of actin filaments are attached.

IBA|ISS

MF

GO:0003779

actin binding

Interacting selectively and non-covalently with monomeric or multimeric forms of actin, including actin filaments.

IBA

MF

GO:0005515

protein binding

Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).

IPI

MF

GO:0051371

muscle alpha-actinin binding

Interacting selectively and non-covalently with muscle isoforms of actinin. Muscle alpha-actinin isoforms are found in skeletal and cardiac muscle and are localized to the Z-disc.

ISS

MF

GO:0071889

14-3-3 protein binding

Interacting selectively and non-covalently with a 14-3-3 protein. A 14-3-3 protein is any of a large family of approximately 30kDa acidic proteins which exist primarily as homo- and heterodimers within all eukaryotic cells, and have been implicated in the modulation of distinct biological processes by binding to specific phosphorylated sites on diverse target proteins, thereby forcing conformational changes or influencing interactions between their targets and other molecules. Each 14-3-3 protein sequence can be roughly divided into three sections: a divergent amino terminus, the conserved core region and a divergent carboxyl terminus. The conserved middle core region of the 14-3-3s encodes an amphipathic groove that forms the main functional domain, a cradle for interacting with client proteins.

ISS