Marcksl1
entrez
81520
canonical
uniprot
Q9EPH2
canonical
ensembl
ENSRNOG00000009113
resolver
ensembl
ENSRNOG00055027689
resolver
ensembl
ENSRNOG00060023201
resolver
ensembl
ENSRNOG00065023930
resolver
ensp
ENSRNOP00000012663
resolver
ensp
ENSRNOP00055039495
resolver
ensp
ENSRNOP00060033094
resolver
ensp
ENSRNOP00065033533
resolver
enst
ENSRNOT00000012663
resolver
enst
ENSRNOT00055047967
resolver
enst
ENSRNOT00060040103
resolver
enst
ENSRNOT00065041063
resolver
genesymbol
Marcksl1
resolver
genesymbol_syn
Mlp
resolver
uniprot_entry
MRP_RAT
resolver
amino_acid_sequence
MGSQSSKAPRGDVTAEEAAGASPAKANGQENGHVKSNGDLTPKGEGESPPVNGADEAAGATGDAIEPAPPSQEAEAKGEVAPKETPKKKKKFSFKKPFKLSGLSFKRNRKEGGGDSSASSPTEEEQEQGEISACSDEGTAQEGKAAATPESQEPQAKGAEASAVSKGGDAEEEAGPQAAEPSTPSGPESGPASASAENE
uniprot
proteins
function
FUNCTION: Controls cell movement by regulating actin cytoskeleton homeostasis and filopodium and lamellipodium formation. When unphosphorylated, induces cell migration. When phosphorylated by MAPK8, induces actin bundles formation and stabilization, thereby reducing actin plasticity, hence restricting cell movement, including neuronal migration. May be involved in coupling the protein kinase C and calmodulin signal transduction systems. {ECO:0000250|UniProtKB:P28667, ECO:0000250|UniProtKB:P49006}.
uniprot
proteins
mass_dalton
19847
uniprot
proteins
post_translational_modification
PTM: Phosphorylated. Phosphorylation at Ser-120 and Thr-183 is non-redundantly catalyzed by MAPK8 in vivo. Phosphorylation at Thr-148 is preferentially catalyzed by MAPK8 in vivo, but this modification can also be catalyzed by other kinases in the absence of MAPK8. May be phosphorylated by protein kinase C, which disrupts the interaction with calmodulin. {ECO:0000250|UniProtKB:P28667}.
uniprot
proteins
protein_family
MARCKS family
uniprot
proteins
pubmed
15489334
uniprot
proteins
sequence_length
199
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P28667}. Cell membrane {ECO:0000250|UniProtKB:P28667}; Lipid-anchor {ECO:0000250|UniProtKB:P28667}. Note=Associates with the membrane via the insertion of the N-terminal N-myristoyl chain and the partial insertion of the effector domain. Association of the effector domain with membranes may be regulated by Ca(2+)/calmodulin. Colocalizes with F-actin at the leading edge of migrating cells. {ECO:0000250|UniProtKB:P28667, ECO:0000250|UniProtKB:P49006}.
uniprot
proteins