MARCKSL1
entrez
65108
canonical
uniprot
P49006
canonical
ensembl
ENSG00000175130
resolver
ensp
ENSP00000362638
resolver
enst
ENST00000329421
resolver
genesymbol
MARCKSL1
resolver
genesymbol_syn
MLP
resolver
genesymbol_syn
MRP
resolver
hgnc
HGNC:7142
resolver
uniprot
D3DPQ0
resolver
uniprot
Q5TEE6
resolver
uniprot
Q6NXS5
resolver
uniprot_entry
MRP_HUMAN
resolver
uniprot_sec
D3DPQ0
resolver
uniprot_sec
Q5TEE6
resolver
uniprot_sec
Q6NXS5
resolver
amino_acid_sequence
MGSQSSKAPRGDVTAEEAAGASPAKANGQENGHVKSNGDLSPKGEGESPPVNGTDEAAGATGDAIEPAPPSQGAEAKGEVPPKETPKKKKKFSFKKPFKLSGLSFKRNRKEGGGDSSASSPTEEEQEQGEIGACSDEGTAQEGKAAATPESQEPQAKGAEASAASEEEAGPQATEPSTPSGPESGPTPASAEQNE
uniprot
proteins
function
FUNCTION: Controls cell movement by regulating actin cytoskeleton homeostasis and filopodium and lamellipodium formation (PubMed:22751924). When unphosphorylated, induces cell migration (By similarity). When phosphorylated by MAPK8, induces actin bundles formation and stabilization, thereby reducing actin plasticity, hence restricting cell movement, including neuronal migration (By similarity). May be involved in coupling the protein kinase C and calmodulin signal transduction systems (By similarity). {ECO:0000250|UniProtKB:P28667, ECO:0000269|PubMed:22751924}.
uniprot
proteins
mass_dalton
19529
uniprot
proteins
post_translational_modification
PTM: Phosphorylated. Phosphorylation at Ser-120 and Thr-178 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
pubmed
16710414
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17525332
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22751924
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25255805
uniprot
proteins
sequence_length
195
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P28667}. Cell membrane {ECO:0000305|PubMed:22751924, ECO:0000305|PubMed:25255805}; Lipid-anchor {ECO:0000305|PubMed:25255805}. 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 (By similarity). In prostate cancers, shows strong expression at apical and/or basal regions of the cell and also has weak cytoplasmic expression (PubMed:22751924). {ECO:0000250|UniProtKB:P28667, ECO:0000269|PubMed:22751924}.
uniprot
proteins