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Protein

Myristoylated alanine-rich C-kinase substrate

Gene

Marcks

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  • protein kinase C binding Source: BHF-UCL
Complete GO annotation...

Keywords - Ligandi

Actin-binding, Calmodulin-binding

Enzyme and pathway databases

ReactomeiREACT_306601. Acetylcholine regulates insulin secretion.

Names & Taxonomyi

Protein namesi
Recommended name:
Myristoylated alanine-rich C-kinase substrate
Short name:
MARCKS
Gene namesi
Name:Marcks
Synonyms:Macs
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:96907. Marcks.

Subcellular locationi

GO - Cellular componenti

  • cell cortex Source: MGI
  • centrosome Source: MGI
  • cytoplasm Source: MGI
  • extracellular exosome Source: Ensembl
  • focal adhesion Source: Ensembl
  • germinal vesicle Source: MGI
  • membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi113 – 1131S → A: Poorly phosphorylated. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 309308Myristoylated alanine-rich C-kinase substratePRO_0000157149Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineBy similarity
Modified residuei26 – 261PhosphoserineBy similarity
Modified residuei27 – 271PhosphoserineBy similarity
Modified residuei29 – 291PhosphoserineBy similarity
Modified residuei46 – 461Phosphoserine1 Publication
Modified residuei63 – 631PhosphoserineBy similarity
Modified residuei113 – 1131Phosphoserine; by MAPK1 Publication
Modified residuei128 – 1281PhosphoserineBy similarity
Modified residuei138 – 1381PhosphoserineBy similarity
Modified residuei140 – 1401PhosphoserineBy similarity
Modified residuei143 – 1431PhosphothreonineBy similarity
Modified residuei152 – 1521Phosphoserine; by PKC1 Publication
Modified residuei156 – 1561Phosphoserine; by PKC1 Publication
Modified residuei160 – 1601PhosphoserineBy similarity
Modified residuei163 – 1631Phosphoserine; by PKC2 Publications
Modified residuei246 – 2461Phosphoserine1 Publication
Modified residuei291 – 2911PhosphoserineBy similarity

Post-translational modificationi

Phosphorylation by PKC displaces MARCKS from the membrane. It also inhibits the F-actin cross-linking activity.2 Publications

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

MaxQBiP26645.
PaxDbiP26645.
PRIDEiP26645.

PTM databases

PhosphoSiteiP26645.

Expressioni

Tissue specificityi

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

Inductioni

By lipopolysaccharides (LPS).

Gene expression databases

BgeeiP26645.
ExpressionAtlasiP26645. baseline and differential.
GenevisibleiP26645. MM.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CALM3P621582EBI-911805,EBI-397435From a different organism.

Protein-protein interaction databases

BioGridi201268. 8 interactions.
IntActiP26645. 2 interactions.
MINTiMINT-4101028.
STRINGi10090.ENSMUSP00000090245.

Structurei

Secondary structure

1
309
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi157 – 1626Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IWQX-ray2.00B148-166[»]
DisProtiDP00253.
ProteinModelPortaliP26645.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26645.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni145 – 16925Calmodulin-binding (PSD)Add
BLAST

Sequence similaritiesi

Belongs to the MARCKS family.Curated

Phylogenomic databases

eggNOGiNOG44640.
GeneTreeiENSGT00730000111419.
HOGENOMiHOG000113482.
InParanoidiP26645.
KOiK12561.
OMAiDSAAFRI.
OrthoDBiEOG7P2XW3.
TreeFamiTF332815.

Family and domain databases

InterProiIPR002101. MARCKS.
[Graphical view]
PANTHERiPTHR14353. PTHR14353. 1 hit.
PfamiPF02063. MARCKS. 1 hit.
[Graphical view]
PRINTSiPR00963. MARCKS.
PROSITEiPS00826. MARCKS_1. 1 hit.
PS00827. MARCKS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P26645-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGAQFSKTAA KGEATAERPG EAAVASSPSK ANGQENGHVK VNGDASPAAA
60 70 80 90 100
EPGAKEELQA NGSAPAADKE EPASGSAATP AAAEKDEAAA ATEPGAGAAD
110 120 130 140 150
KEAAEAEPAE PSSPAAEAEG ASASSTSSPK AEDGAAPSPS SETPKKKKKR
160 170 180 190 200
FSFKKSFKLS GFSFKKSKKE SGEGAEAEGA TAEGAKDEAA AAAGGEGAAA
210 220 230 240 250
PGEQAGGAGA EGAAGGEPRE AEAAEPEQPE QPEQPAAEEP QAEEQSEAAG
260 270 280 290 300
EKAEEPAPGA TAGDASSAAG PEQEAPAATD EAAASAAPAA SPEPQPECSP

EAPPAPTAE
Length:309
Mass (Da):29,661
Last modified:January 23, 2007 - v2
Checksum:i3BB1E392D74B5A98
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti96 – 983AGA → TGT AA sequence (PubMed:1868832).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60474 mRNA. Translation: AAA39491.1.
BC046601 mRNA. Translation: AAH46601.1.
CCDSiCCDS23784.1.
PIRiA39169.
RefSeqiNP_032564.1. NM_008538.2.
UniGeneiMm.30059.

Genome annotation databases

EnsembliENSMUST00000092584; ENSMUSP00000090245; ENSMUSG00000069662.
GeneIDi17118.
KEGGimmu:17118.
UCSCiuc007evg.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60474 mRNA. Translation: AAA39491.1.
BC046601 mRNA. Translation: AAH46601.1.
CCDSiCCDS23784.1.
PIRiA39169.
RefSeqiNP_032564.1. NM_008538.2.
UniGeneiMm.30059.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IWQX-ray2.00B148-166[»]
DisProtiDP00253.
ProteinModelPortaliP26645.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201268. 8 interactions.
IntActiP26645. 2 interactions.
MINTiMINT-4101028.
STRINGi10090.ENSMUSP00000090245.

PTM databases

PhosphoSiteiP26645.

Proteomic databases

MaxQBiP26645.
PaxDbiP26645.
PRIDEiP26645.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000092584; ENSMUSP00000090245; ENSMUSG00000069662.
GeneIDi17118.
KEGGimmu:17118.
UCSCiuc007evg.1. mouse.

Organism-specific databases

CTDi4082.
MGIiMGI:96907. Marcks.

Phylogenomic databases

eggNOGiNOG44640.
GeneTreeiENSGT00730000111419.
HOGENOMiHOG000113482.
InParanoidiP26645.
KOiK12561.
OMAiDSAAFRI.
OrthoDBiEOG7P2XW3.
TreeFamiTF332815.

Enzyme and pathway databases

ReactomeiREACT_306601. Acetylcholine regulates insulin secretion.

Miscellaneous databases

ChiTaRSiMarcks. mouse.
EvolutionaryTraceiP26645.
NextBioi291280.
PROiP26645.
SOURCEiSearch...

Gene expression databases

BgeeiP26645.
ExpressionAtlasiP26645. baseline and differential.
GenevisibleiP26645. MM.

Family and domain databases

InterProiIPR002101. MARCKS.
[Graphical view]
PANTHERiPTHR14353. PTHR14353. 1 hit.
PfamiPF02063. MARCKS. 1 hit.
[Graphical view]
PRINTSiPR00963. MARCKS.
PROSITEiPS00826. MARCKS_1. 1 hit.
PS00827. MARCKS_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46 AND SER-246, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  10. 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.

Entry informationi

Entry nameiMARCS_MOUSE
AccessioniPrimary (citable) accession number: P26645
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.