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P26645 (MARCS_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myristoylated alanine-rich C-kinase substrate

Short name=MARCKS
Gene names
Name:Marcks
Synonyms:Macs
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length309 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

MARCKS is the most prominent cellular substrate for protein kinase C. This protein binds calmodulin, actin, and synapsin. MARCKS is a filamentous (F) actin cross-linking protein.

Subcellular location

Cytoplasmcytoskeleton Probable. Membrane; Lipid-anchor By similarity.

Tissue specificity

Brain, spleen, less in kidney and heart, and very low levels in liver.

Induction

By lipopolysaccharides (LPS).

Post-translational modification

Phosphorylation by PKC displaces MARCKS from the membrane. It also inhibits the F-actin cross-linking activity.

Sequence similarities

Belongs to the MARCKS family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CALM3P621582EBI-911805,EBI-397435From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 309308Myristoylated alanine-rich C-kinase substrate
PRO_0000157149

Regions

Region145 – 16925Calmodulin-binding (PSD)

Amino acid modifications

Modified residue271Phosphoserine By similarity
Modified residue461Phosphoserine Ref.9
Modified residue631Phosphoserine By similarity
Modified residue1131Phosphoserine; by MAPK Ref.6
Modified residue1281Phosphoserine By similarity
Modified residue1381Phosphoserine By similarity
Modified residue1431Phosphothreonine By similarity
Modified residue1521Phosphoserine; by PKC Ref.8
Modified residue1561Phosphoserine; by PKC Ref.8
Modified residue1601Phosphoserine By similarity
Modified residue1631Phosphoserine; by PKC Ref.8 Ref.11
Modified residue2461Phosphoserine Ref.9
Lipidation21N-myristoyl glycine By similarity

Experimental info

Mutagenesis1131S → A: Poorly phosphorylated. Ref.6
Sequence conflict96 – 983AGA → TGT AA sequence Ref.2

Secondary structure

... 309
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P26645 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 3BB1E392D74B5A98

FASTA30929,661
        10         20         30         40         50         60 
MGAQFSKTAA KGEATAERPG EAAVASSPSK ANGQENGHVK VNGDASPAAA EPGAKEELQA 

        70         80         90        100        110        120 
NGSAPAADKE EPASGSAATP AAAEKDEAAA ATEPGAGAAD KEAAEAEPAE PSSPAAEAEG 

       130        140        150        160        170        180 
ASASSTSSPK AEDGAAPSPS SETPKKKKKR FSFKKSFKLS GFSFKKSKKE SGEGAEAEGA 

       190        200        210        220        230        240 
TAEGAKDEAA AAAGGEGAAA PGEQAGGAGA EGAAGGEPRE AEAAEPEQPE QPEQPAAEEP 

       250        260        270        280        290        300 
QAEEQSEAAG EKAEEPAPGA TAGDASSAAG PEQEAPAATD EAAASAAPAA SPEPQPECSP 


EAPPAPTAE 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and molecular characterization of the murine macrophage '68-kDa' protein kinase C substrate and its regulation by bacterial lipopolysaccharide."
Seykora J.T., Ravetch J.V., Aderem A.
Proc. Natl. Acad. Sci. U.S.A. 88:2505-2509(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Macrophage.
[2]"Protein kinase C activation potently down-regulates the expression of its major substrate, 80K, in Swiss 3T3 cells."
Brooks S.F., Herget T., Erusalimsky J.D., Rozengurt E.
EMBO J. 10:2497-2505(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Fibroblast.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Olfactory epithelium.
[4]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 131-145 AND 170-186, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[5]"Purification and internal amino acid sequence of the 80 kDa protein kinase C substrate from Swiss 3T3 fibroblasts. Homology with substrates from brain."
Brooks S.F., Erusalimsky J.D., Totty N.F., Rozengurt E.
FEBS Lett. 268:291-295(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
Strain: Swiss.
Tissue: Fibroblast.
[6]"p42 MAPK phosphorylates 80 kDa MARCKS at Ser-113."
Schoenwasser D.C., Palmer R.H., Herget T., Parker P.J.
FEBS Lett. 395:1-5(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 102-130, PHOSPHORYLATION AT SER-113, MUTAGENESIS OF SER-113.
[7]"Relationship between the major protein kinase C substrates acidic 80-kDa protein-kinase-C substrate (80K) and myristoylated alanine-rich C-kinase substrate (MARCKS). Members of a gene family or equivalent genes in different species."
Herget T., Brooks S.F., Broad S., Rozengurt E.
Eur. J. Biochem. 209:7-14(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 182-301.
[8]"The myristoylated alanine-rich C-kinase substrate (MARCKS) is sequentially phosphorylated by conventional, novel and atypical isotypes of protein kinase C."
Herget T., Oehrlein S.A., Pappin D.J.C., Rozengurt E., Parker P.J.
Eur. J. Biochem. 233:448-457(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-152; SER-156 AND SER-163.
[9]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46 AND SER-246, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic brain.
[10]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[11]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[12]"Crystal structure of a MARCKS peptide containing the calmodulin-binding domain in complex with Ca2+-calmodulin."
Yamauchi E., Nakatsu T., Matsubara M., Kato H., Taniguchi H.
Nat. Struct. Biol. 10:226-231(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 148-166 IN COMPLEX WITH CALMODULIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M60474 mRNA. Translation: AAA39491.1.
BC046601 mRNA. Translation: AAH46601.1.
PIRA39169.
RefSeqNP_032564.1. NM_008538.2.
UniGeneMm.30059.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IWQX-ray2.00B148-166[»]
DisProtDP00253.
ProteinModelPortalP26645.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201268. 7 interactions.
IntActP26645. 2 interactions.
MINTMINT-4101028.
STRING10090.ENSMUSP00000090245.

PTM databases

PhosphoSiteP26645.

Proteomic databases

PaxDbP26645.
PRIDEP26645.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000092584; ENSMUSP00000090245; ENSMUSG00000069662.
GeneID17118.
KEGGmmu:17118.
UCSCuc007evg.1. mouse.

Organism-specific databases

CTD4082.
MGIMGI:96907. Marcks.

Phylogenomic databases

eggNOGNOG44640.
GeneTreeENSGT00730000111419.
HOGENOMHOG000113482.
InParanoidP26645.
KOK12561.
OMAADICMSA.
OrthoDBEOG7P2XW3.
TreeFamTF332815.

Gene expression databases

ArrayExpressP26645.
BgeeP26645.
GenevestigatorP26645.

Family and domain databases

InterProIPR002101. MARCKS.
[Graphical view]
PANTHERPTHR14353. PTHR14353. 1 hit.
PfamPF02063. MARCKS. 1 hit.
[Graphical view]
PRINTSPR00963. MARCKS.
PROSITEPS00826. MARCKS_1. 1 hit.
PS00827. MARCKS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMARCKS. mouse.
EvolutionaryTraceP26645.
NextBio291280.
PROP26645.
SOURCESearch...

Entry information

Entry nameMARCS_MOUSE
AccessionPrimary (citable) accession number: P26645
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot