Marcksl1
entrez
17357
canonical
uniprot
P28667
canonical
ensembl
ENSMUSG00000047945
resolver
ensp
ENSMUSP00000055637
resolver
enst
ENSMUST00000062356
resolver
genesymbol
Marcksl1
resolver
genesymbol_syn
Mlp
resolver
genesymbol_syn
Mrp
resolver
uniprot
Q3TEZ4
resolver
uniprot
Q91W07
resolver
uniprot_entry
MRP_MOUSE
resolver
uniprot_sec
Q3TEZ4
resolver
uniprot_sec
Q91W07
resolver
amino_acid_sequence
MGSQSSKAPRGDVTAEEAAGASPAKANGQENGHVRSNGDLTPKGEGESPPVNGTDEAAGATGDAIEPAPPSQEAEAKGEVAPKETPKKKKKFSFKKPFKLSGLSFKRNRKEGGGDSSASSPTEEEQEQGEMSACSDEGTAQEGKAAATPESQEPQAKGAEASAASKEGDTEEEAGPQAAEPSTPSGPESGPTPASAEQNE
uniprot
proteins
function
FUNCTION: Involved in the control of cell movement by regulating actin cytoskeleton homeostasis and filopodium and lamellipodium formation (PubMed:22751924). When unphosphorylated, induces cell migration (PubMed:22751924). When phosphorylated by MAPK8, induces actin bundles formation and stabilization, thereby reducing actin plasticity, hence restricting cell movement, including neuronal migration (PubMed:22751924). May be involved in coupling the protein kinase C and calmodulin signal transduction systems (Probable). {ECO:0000269|PubMed:22751924, ECO:0000305|PubMed:1618855}.
uniprot
proteins
mass_dalton
20165
uniprot
proteins
mutagenesis
MUTAGEN 120; /note="S->A: Complete loss of MAPK-mediated phosphorylation; when associated with A-148 and A-183. In neurons, induces the generation of large, flat lamellipodial protrusions; when associated with A-148 and A-183."; /evidence="ECO:0000269|PubMed:22751924"; MUTAGEN 120; /note="S->D: Induction of F-actin-bundling; when associated with D-148 and D-183. In neurons, induces the generation of long and prominent filopodia; when associated with D-148 and D-183."; /evidence="ECO:0000269|PubMed:22751924"; MUTAGEN 148; /note="T->A: Complete loss of MAPK-mediated phosphorylation; when associated with A-120 and A-183. In neurons, induces the generation of large, flat lamellipodial protrusions; when associated with A-120 and A-183."; /evidence="ECO:0000269|PubMed:22751924"; MUTAGEN 148; /note="T->D: Induction of F-actin-bundling; when associated with D-120 and D-183. In neurons, induces the generation of long and prominent filopodia; when associated with D-120 and D-183."; /evidence="ECO:0000269|PubMed:22751924"; MUTAGEN 183; /note="T->A: Complete loss of MAPK-mediated phosphorylation; when associated with A-120 and A-148. In neurons, induces the generation of large, flat lamellipodial protrusions; when associated with A-120 and A-148."; /evidence="ECO:0000269|PubMed:22751924"; MUTAGEN 183; /note="T->D: Induction of F-actin-bundling; when associated with D-120 and D-148. In neurons, induces the generation of long and prominent filopodia; when associated with D-120 and D-148."; /evidence="ECO:0000269|PubMed:22751924
uniprot
proteins
post_translational_modification
PTM: Phosphorylated (PubMed:1618855, PubMed:22751924). Phosphorylation at Ser-120 and Thr-183 is non-redundantly catalyzed by MAPK8 in vivo (PubMed:22751924). 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 (PubMed:22751924). May be phosphorylated by protein kinase C, which disrupts the interaction with calmodulin (PubMed:1618855). {ECO:0000269|PubMed:1618855, ECO:0000269|PubMed:22751924}.
uniprot
proteins
protein_family
MARCKS family
uniprot
proteins
pubmed
1516135
uniprot
proteins
pubmed
15345747
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
1618855
uniprot
proteins
pubmed
1864362
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22751924
uniprot
proteins
pubmed
8406449
uniprot
proteins
pubmed
9598313
uniprot
proteins
pubmed
9819217
uniprot
proteins
sequence_length
200
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:22751924}. Cell membrane {ECO:0000305|PubMed:1618855, ECO:0000305|PubMed:9819217}; Lipid-anchor {ECO:0000305|PubMed:1618855}. Note=Associates with the membrane via the insertion of the N-terminal N-myristoyl chain and the partial insertion of the effector domain (Probable). Association of the effector domain with membranes may be regulated by Ca(2+)/calmodulin (By similarity). Colocalizes with F-actin at the leading edge of migrating cells (PubMed:22751924). {ECO:0000250|UniProtKB:P49006, ECO:0000269|PubMed:22751924, ECO:0000305|PubMed:1618855, ECO:0000305|PubMed:9819217}.
uniprot
proteins