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P26645

- MARCS_MOUSE

UniProt

P26645 - MARCS_MOUSE

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Protein
Myristoylated alanine-rich C-kinase substrate
Gene
Marcks, Macs
Organism
Mus musculus (Mouse)
Status
Reviewed - 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

  1. protein binding Source: IntAct
  2. protein kinase C binding Source: BHF-UCL
Complete GO annotation...

Keywords - Ligandi

Actin-binding, Calmodulin-binding

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: Chromosome 10

Organism-specific databases

MGIiMGI:96907. Marcks.

Subcellular locationi

Cytoplasmcytoskeleton Inferred. Membrane; Lipid-anchor By similarity

GO - Cellular componenti

  1. cell cortex Source: MGI
  2. centrosome Source: MGI
  3. cytoplasm Source: MGI
  4. germinal vesicle Source: MGI
  5. 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 – 11Removed By similarity
Chaini2 – 309308Myristoylated alanine-rich C-kinase substrate
PRO_0000157149Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine By similarity
Modified residuei27 – 271Phosphoserine By similarity
Modified residuei46 – 461Phosphoserine1 Publication
Modified residuei63 – 631Phosphoserine By similarity
Modified residuei113 – 1131Phosphoserine; by MAPK1 Publication
Modified residuei128 – 1281Phosphoserine By similarity
Modified residuei138 – 1381Phosphoserine By similarity
Modified residuei143 – 1431Phosphothreonine By similarity
Modified residuei152 – 1521Phosphoserine; by PKC1 Publication
Modified residuei156 – 1561Phosphoserine; by PKC1 Publication
Modified residuei160 – 1601Phosphoserine By similarity
Modified residuei163 – 1631Phosphoserine; by PKC2 Publications
Modified residuei246 – 2461Phosphoserine1 Publication

Post-translational modificationi

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

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

ArrayExpressiP26645.
BgeeiP26645.
GenevestigatoriP26645.

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

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IWQX-ray2.00B148-166[»]
DisProtiDP00253.
ProteinModelPortaliP26645.

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.

Phylogenomic databases

eggNOGiNOG44640.
GeneTreeiENSGT00730000111419.
HOGENOMiHOG000113482.
InParanoidiP26645.
KOiK12561.
OMAiQLTIISK.
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

MGAQFSKTAA KGEATAERPG EAAVASSPSK ANGQENGHVK VNGDASPAAA    50
EPGAKEELQA NGSAPAADKE EPASGSAATP AAAEKDEAAA ATEPGAGAAD 100
KEAAEAEPAE PSSPAAEAEG ASASSTSSPK AEDGAAPSPS SETPKKKKKR 150
FSFKKSFKLS GFSFKKSKKE SGEGAEAEGA TAEGAKDEAA AAAGGEGAAA 200
PGEQAGGAGA EGAAGGEPRE AEAAEPEQPE QPEQPAAEEP QAEEQSEAAG 250
EKAEEPAPGA TAGDASSAAG PEQEAPAATD EAAASAAPAA SPEPQPECSP 300
EAPPAPTAE 309
Length:309
Mass (Da):29,661
Last modified:January 23, 2007 - v2
Checksum:i3BB1E392D74B5A98
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti96 – 983AGA → TGT AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
M60474 mRNA. Translation: AAA39491.1 .
BC046601 mRNA. Translation: AAH46601.1 .
CCDSi CCDS23784.1.
PIRi A39169.
RefSeqi NP_032564.1. NM_008538.2.
UniGenei Mm.30059.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1IWQ X-ray 2.00 B 148-166 [» ]
DisProti DP00253.
ProteinModelPortali P26645.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201268. 8 interactions.
IntActi P26645. 2 interactions.
MINTi MINT-4101028.
STRINGi 10090.ENSMUSP00000090245.

PTM databases

PhosphoSitei P26645.

Proteomic databases

MaxQBi P26645.
PaxDbi P26645.
PRIDEi P26645.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000092584 ; ENSMUSP00000090245 ; ENSMUSG00000069662 .
GeneIDi 17118.
KEGGi mmu:17118.
UCSCi uc007evg.1. mouse.

Organism-specific databases

CTDi 4082.
MGIi MGI:96907. Marcks.

Phylogenomic databases

eggNOGi NOG44640.
GeneTreei ENSGT00730000111419.
HOGENOMi HOG000113482.
InParanoidi P26645.
KOi K12561.
OMAi QLTIISK.
OrthoDBi EOG7P2XW3.
TreeFami TF332815.

Miscellaneous databases

ChiTaRSi MARCKS. mouse.
EvolutionaryTracei P26645.
NextBioi 291280.
PROi P26645.
SOURCEi Search...

Gene expression databases

ArrayExpressi P26645.
Bgeei P26645.
Genevestigatori P26645.

Family and domain databases

InterProi IPR002101. MARCKS.
[Graphical view ]
PANTHERi PTHR14353. PTHR14353. 1 hit.
Pfami PF02063. MARCKS. 1 hit.
[Graphical view ]
PRINTSi PR00963. MARCKS.
PROSITEi PS00826. MARCKS_1. 1 hit.
PS00827. MARCKS_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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 9, 2014
This is version 130 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

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