Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-00816
Entry Name
UniProt Accession
Theoretical PI
4.6
Molecular Weight
20165.43
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
MARCKS-related protein
Protein Synonyms/Alias
Brain protein F52; MARCKS-like protein 1; Macrophage myristoylated alanine-rich C kinase substrate; Mac-MARCKS; MacMARCKS;
Gene Name
Marcksl1
Gene Synonyms/Alias
Mlp; Mrp;
Created Date
01-DEC-1992
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGSQSSKAP
[1]
N-Myristoylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] Bähr G, Diederich A, Vergères G, Winterhalter M. Interaction of the effectordomain of MARCKS and MARCKS-related protein with lipid membranes revealed byelectric potential measurements. Biochemistry. 1998 Nov 17;37(46):16252-61.[PMID:9819217]
Functional Description
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 also affect cancer cell migration. May be involved in coupling the protein kinase C and calmodulin signal transduction systems.
Sequence Annotation
Region: 87 110 Effector domain involved in lipid-binding.
Region: 87 100 Calmodulin-binding (PSD).
Modified residue: 22 22 Phosphoserine.
Modified residue: 36 36 Phosphoserine.
Modified residue: 48 48 Phosphoserine.
Modified residue: 71 71 Phosphoserine.
Modified residue: 85 85 Phosphothreonine.
Modified residue: 93 93 Phosphoserine; by PKC.
Modified residue: 101 101 Phosphoserine; by PKC.
Modified residue: 104 104 Phosphoserine; by PKC.
Modified residue: 120 120 Phosphoserine; by MAPK8.
Modified residue: 135 135 Phosphoserine.
Modified residue: 148 148 Phosphothreonine; by MAPK8.
Modified residue: 151 151 Phosphoserine.
Modified residue: 162 162 Phosphoserine.
Modified residue: 165 165 Phosphoserine.
Modified residue: 170 170 Phosphothreonine.
Modified residue: 183 183 Phosphothreonine; by MAPK8.
Modified residue: 192 192 Phosphothreonine.
Protein Length
200 AA.
Protein Sequence
(Canonical)
MGSQSSKAPR GDVTAEEAAG ASPAKANGQE NGHVRSNGDL TPKGEGESPP VNGTDEAAGA  60
TGDAIEPAPP SQEAEAKGEV APKETPKKKK KFSFKKPFKL SGLSFKRNRK EGGGDSSASS  120
PTEEEQEQGE MSACSDEGTA QEGKAAATPE SQEPQAKGAE ASAASKEGDT EEEAGPQAAE  180
PSTPSGPESG PTPASAEQNE                                              200
FASTA
(Canonical)
>LipidDB-10090-00816|P28667
MGSQSSKAPRGDVTAEEAAGASPAKANGQENGHVRSNGDLTPKGEGESPPVNGTDEAAGA
TGDAIEPAPPSQEAEAKGEVAPKETPKKKKKFSFKKPFKLSGLSFKRNRKEGGGDSSASS
PTEEEQEQGEMSACSDEGTAQEGKAAATPESQEPQAKGAEASAASKEGDTEEEAGPQAAE
PSTPSGPESGPTPASAEQNE
Gene Ontology
GO:0005737; C:cytoplasm; IEA:UniProtKB-KW
GO:0070062; C:extracellular vesicular exosome; IEA:Ensembl
GO:0005886; C:plasma membrane; IEA:UniProtKB-KW
GO:0008284; P:positive regulation of cell proliferation; IDA:MGI
Interpro
InterPro; IPR002101; MARCKS
Pfam
Pfam; PF02063; MARCKS;
SMART
PROSITE
PROSITE; PS00826; MARCKS_1;
PROSITE; PS00827; MARCKS_2;
PRINTS
PRINTS; PR00963; MARCKS;