MARCKS
entrez
4082
canonical
uniprot
P29966
canonical
ensembl
ENSG00000277443
resolver
ensp
ENSP00000478061
resolver
enst
ENST00000612661
resolver
genesymbol
MARCKS
resolver
genesymbol_syn
MACS
resolver
genesymbol_syn
PRKCSL
resolver
hgnc
HGNC:6759
resolver
uniprot
E1P560
resolver
uniprot
Q2LA83
resolver
uniprot
Q5TDB7
resolver
uniprot
Q6NVI1
resolver
uniprot_entry
MARCS_HUMAN
resolver
uniprot_entry
Q6NVI1_HUMAN
resolver
uniprot_sec
E1P560
resolver
uniprot_sec
Q2LA83
resolver
uniprot_sec
Q5TDB7
resolver
amino_acid_sequence
MGAQFSKTAAKGEAAAERPGEAAVASSPSKANGQENGHVKVNGDASPAAAESGAKEELQANGSAPAADKEEPAAAGSGAASPSAAEKGEPAAAAAPEAGASPVEKEAPAEGEAAEPGSPTAAEGEAASAASSTSSPKAEDGATPSPSNETPKKKKKRFSFKKSFKLSGFSFKKNKKEAGEGGEAEAPAAEGGKDEAAGGAAAAAAEAGAASGEQAAAPGEEAAAGEEGAAGGDPQEAKPQEAAVAPEKPPASDETKAAEEPSKVEEKKAEEAGASAAACEAPSAAGPGAPPEQEAAPAEEPAAAAASSACAAPSQEAQPECSPEAPPAEAAE
uniprot
proteins
function
FUNCTION: Membrane-associated protein that plays a role in the structural modulation of the actin cytoskeleton, chemotaxis, motility, cell adhesion, phagocytosis, and exocytosis through lipid sequestering and/or protein docking to membranes (PubMed:23704996, PubMed:36009319). Thus, exerts an influence on a plethora of physiological processes, such as embryonic development, tissue regeneration, neuronal plasticity, and inflammation. Sequesters phosphatidylinositol 4,5-bisphosphate (PIP2) at lipid rafts in the plasma membrane of quiescent cells, an action reversed by protein kinase C, ultimately inhibiting exocytosis (PubMed:23704996). During inflammation, promotes the migration and adhesion of inflammatory cells and the secretion of cytokines such as tumor necrosis factor (TNF), particularly in macrophages (PubMed:37949888). Plays an essential role in bacteria-induced intracellular reactive oxygen species (ROS) formation in the monocytic cell type. Participates in the regulation of neurite initiation and outgrowth by interacting with components of cellular machinery including CDC42 that regulates cell shape and process extension through modulation of the cytoskeleton (By similarity). Plays also a role in axon development by mediating docking and fusion of RAB10-positive vesicles with the plasma membrane (By similarity). {ECO:0000250|UniProtKB:P26645, ECO:0000250|UniProtKB:P30009, ECO:0000269|PubMed:23704996, ECO:0000269|PubMed:36009319, ECO:0000269|PubMed:37949888}.
uniprot
proteins
mass_dalton
31555
uniprot
proteins
post_translational_modification
PTM: Phosphorylation by PKC displaces MARCKS from the membrane. It also inhibits the F-actin cross-linking activity. PKC-mediated phosphorylation increases 4 to 5-fold upon TNF or LPS induction. {ECO:0000269|PubMed:2034276, ECO:0000269|PubMed:2116001, ECO:0000269|PubMed:8557118}.; PTM: Myristoylated. A proper myristoylation is essential for the proper distribution to the plasma membrane. {ECO:0000269|PubMed:2034276, ECO:0000269|PubMed:2116001}.; PTM: Acetylated at Lys-172 by KAT5; acetylation is required for its subsequent phosphorylation. Deacetylated by SIRT2. {ECO:0000250|UniProtKB:P26645}.
uniprot
proteins
protein_family
MARCKS family
uniprot
proteins
pubmed
1396720
uniprot
proteins
pubmed
1427823
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17924679
uniprot
proteins
pubmed
1860846
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
2034276
uniprot
proteins
pubmed
2116001
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23704996
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25255805
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
36009319
uniprot
proteins
pubmed
37949888
uniprot
proteins
pubmed
8557118
uniprot
proteins
sequence_length
332
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2034276}; Lipid-anchor {ECO:0000305}. Cytoplasm, cytoskeleton {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:2034276}. Note=PKC-dependent phosphorylation displaces MARCKS from the cell membrane and subsequent dephosphorylation is accompanied by its reassociation with the membrane. {ECO:0000269|PubMed:2034276}.
uniprot
proteins