KLHL41

This gene is a member of the kelch-like family. The encoded protein contains a BACK domain, a BTB/POZ domain, and 5 Kelch repeats. This protein is thought to function in skeletal muscle development and maintenance. Mutations in this gene have been associated with nemaline myopathy (NM), a rare congenital muscle disorder.

KLHL41

Involved in skeletal muscle development and differentiation. Regulates proliferation and differentiation of myoblasts and plays a role in myofibril assembly by promoting lateral fusion of adjacent thin fibrils into mature, wide myofibrils. Required for pseudopod elongation in transformed cells.

Myofibril assemblyISS:UniProtKB
Protein ubiquitinationManual Assertion Based On ExperimentIDA:UniProtKB
Regulation of myoblast differentiationISS:UniProtKB
Regulation of myoblast proliferationISS:UniProtKB
Regulation of skeletal muscle cell differentiationManual Assertion Based On ExperimentIBA:GO_Central
Sarcomere organizationIEA:InterPro
Skeletal muscle cell differentiationISS:UniProtKB
Skeletal muscle fiber developmentIEA:InterPro
Striated muscle contractionManual Assertion Based On ExperimentTAS:ProtInc

Cytoplasm; Cytoplasm, cytoskeleton; Cell projection, pseudopodium; Cell projection, ruffle; Cytoplasm, myofibril, sarcomere, M line; Sarcoplasmic reticulum membrane; Endoplasmic reticulum membrane. Predominantly cytoplasmic but can colocalize with F-actin at the membrane ruffle-like structures at the tips of transformation-specific pseudopodia.

Nemaline myopathy 9 (NEM9):
An autosomal recessive form of nemaline myopathy. Nemaline myopathies are muscular disorders characterized by muscle weakness of varying severity and onset, and abnormal thread-like or rod-shaped structures in muscle fibers on histologic examination. NEM9 phenotype is highly variable, ranging from death in infancy due to lack of antigravity movements, to slowly progressive distal muscle weakness with preserved ambulation later in childhood.

Ubiquitinated by E3 ubiquitin ligase complex formed by CUL3 and RBX1 and probably targeted for proteasome-independent degradation. Quinone-induced oxidative stress increases its ubiquitination.