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P26645

- MARCS_MOUSE

UniProt

P26645 - MARCS_MOUSE

Protein

Myristoylated alanine-rich C-kinase substrate

Gene

Marcks

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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

    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 Curated. Membrane By similarity; 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

    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 residuei27 – 271PhosphoserineBy similarity
    Modified residuei46 – 461Phosphoserine1 Publication
    Modified residuei63 – 631PhosphoserineBy similarity
    Modified residuei113 – 1131Phosphoserine; by MAPK1 Publication
    Modified residuei128 – 1281PhosphoserineBy similarity
    Modified residuei138 – 1381PhosphoserineBy 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

    Post-translational modificationi

    Phosphorylation by PKC displaces MARCKS from the membrane. It also inhibits the F-actin cross-linking activity.4 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

    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

    1
    309
    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.
    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.
    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

    Experimental Info

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

    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

    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: October 1, 2014
    This is version 131 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