MARCKS Related Protein (MARCKSL1)

MLP1; MRP; MLP; F52; MACMARCKS; MARCKS-like protein 1; Macrophage myristoylated alanine-rich C kinase substrate

SPN	M682
HGNC	7142
MGI	97143
PubMed	22751924
RGD	621197
UniProt	P49006
Wiki	MARCKSL1

The myristoylated, alanine-rich protein MARCKS is a widely expressed, prominent substrate for protein kinase C, a key enzyme of intracellular signal transduction. The predicted 200-amino acid protein, which they called F52, shares 52% amino acid identity with bovine MARCKS. The similarity between the 2 proteins is found in the consensus myristoylation sequence near the N-terminus and in the 25-amino acid protein kinase C phosphorylation site domain. F52 has a similar amino acid composition to MARCKS, although its alanine content is not as high. It is distributed throughout the mouse brain in a pattern that is distinct from that of MARCKS.A transgene containing this 433-bp fragment from mouse linked to a reporter Mrp beta-galactosidase gene produced normal patterns of Mrp expression in the developing mouse embryo.

Reference

"The full-ORF clone resource of the German cDNA consortium."
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]

"The DNA sequence and biological annotation of human chromosome 1."
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]

"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]

"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]

"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]

"A quantitative atlas of mitotic phosphorylation."
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]

"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]

"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]

"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]

"Initial characterization of the human central proteome."
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]

"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]

"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]