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P29966

- MARCS_HUMAN

UniProt

P29966 - MARCS_HUMAN

Protein

Myristoylated alanine-rich C-kinase substrate

Gene

MARCKS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 4 (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. actin filament binding Source: ProtInc
    2. calmodulin binding Source: ProtInc

    GO - Biological processi

    1. energy reserve metabolic process Source: Reactome
    2. regulation of insulin secretion Source: Reactome
    3. small molecule metabolic process Source: Reactome

    Keywords - Ligandi

    Actin-binding, Calmodulin-binding

    Enzyme and pathway databases

    ReactomeiREACT_18405. Acetylcholine regulates insulin secretion.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Myristoylated alanine-rich C-kinase substrate
    Short name:
    MARCKS
    Alternative name(s):
    Protein kinase C substrate, 80 kDa protein, light chain
    Short name:
    80K-L protein
    Short name:
    PKCSL
    Gene namesi
    Name:MARCKS
    Synonyms:MACS, PRKCSL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:6759. MARCKS.

    Subcellular locationi

    Cytoplasmcytoskeleton Curated. Membrane By similarity; Lipid-anchor By similarity

    GO - Cellular componenti

    1. actin cytoskeleton Source: ProtInc
    2. cell cortex Source: Ensembl
    3. centrosome Source: Ensembl
    4. extracellular vesicular exosome Source: UniProt
    5. germinal vesicle Source: Ensembl
    6. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30637.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 332331Myristoylated alanine-rich C-kinase substratePRO_0000157148Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycineBy similarity
    Modified residuei27 – 271Phosphoserine2 Publications
    Modified residuei46 – 461Phosphoserine4 Publications
    Modified residuei63 – 631Phosphoserine1 Publication
    Modified residuei77 – 771Phosphoserine3 Publications
    Modified residuei81 – 811Phosphoserine2 Publications
    Modified residuei101 – 1011Phosphoserine3 Publications
    Modified residuei118 – 1181Phosphoserine1 Publication
    Modified residuei135 – 1351PhosphoserineBy similarity
    Modified residuei143 – 1431Phosphothreonine1 Publication
    Modified residuei145 – 1451Phosphoserine1 Publication
    Modified residuei150 – 1501Phosphothreonine3 Publications
    Modified residuei159 – 1591Phosphoserine; by PKC1 Publication
    Modified residuei163 – 1631Phosphoserine; by PKC3 Publications
    Modified residuei167 – 1671Phosphoserine; by PKC2 Publications
    Modified residuei170 – 1701Phosphoserine; by PKC4 Publications
    Modified residuei262 – 2621PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylation by PKC displaces MARCKS from the membrane. It also inhibits the F-actin cross-linking activity.6 Publications

    Keywords - PTMi

    Lipoprotein, Myristate, Phosphoprotein

    Proteomic databases

    MaxQBiP29966.
    PaxDbiP29966.
    PeptideAtlasiP29966.
    PRIDEiP29966.

    PTM databases

    PhosphoSiteiP29966.

    Expressioni

    Gene expression databases

    ArrayExpressiP29966.
    BgeeiP29966.
    CleanExiHS_MARCKS.
    GenevestigatoriP29966.

    Organism-specific databases

    HPAiCAB022062.
    HPA051913.
    HPA054820.

    Interactioni

    Protein-protein interaction databases

    BioGridi110257. 25 interactions.
    IntActiP29966. 6 interactions.
    MINTiMINT-4999508.
    STRINGi9606.ENSP00000357624.

    Structurei

    3D structure databases

    ProteinModelPortaliP29966.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni152 – 17625Calmodulin-binding (PSD)Add
    BLAST

    Sequence similaritiesi

    Belongs to the MARCKS family.Curated

    Phylogenomic databases

    eggNOGiNOG44640.
    HOGENOMiHOG000113482.
    HOVERGENiHBG081955.
    InParanoidiP29966.
    KOiK12561.
    OMAiMGTPLSK.
    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.

    P29966-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGAQFSKTAA KGEAAAERPG EAAVASSPSK ANGQENGHVK VNGDASPAAA    50
    ESGAKEELQA NGSAPAADKE EPAAAGSGAA SPSAAEKGEP AAAAAPEAGA 100
    SPVEKEAPAE GEAAEPGSPT AAEGEAASAA SSTSSPKAED GATPSPSNET 150
    PKKKKKRFSF KKSFKLSGFS FKKNKKEAGE GGEAEAPAAE GGKDEAAGGA 200
    AAAAAEAGAA SGEQAAAPGE EAAAGEEGAA GGDPQEAKPQ EAAVAPEKPP 250
    ASDETKAAEE PSKVEEKKAE EAGASAAACE APSAAGPGAP PEQEAAPAEE 300
    PAAAAASSAC AAPSQEAQPE CSPEAPPAEA AE 332
    Length:332
    Mass (Da):31,555
    Last modified:January 23, 2007 - v4
    Checksum:i0AB247801EF8FCBF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti84 – 841A → S in BAA01392. (PubMed:1427823)Curated
    Sequence conflicti119 – 1191P → A in BAA01392. (PubMed:1427823)Curated
    Sequence conflicti225 – 2251G → R(PubMed:1396720)Curated
    Sequence conflicti234 – 2341P → S in AAA59555. (PubMed:1860846)Curated
    Sequence conflicti235 – 2351Q → E(PubMed:1396720)Curated
    Sequence conflicti287 – 30822PGAPP…AAASS → LVCPRRGGSPRGGARGRRSL NQ in AAA59555. (PubMed:1860846)CuratedAdd
    BLAST

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti250 – 2501P → L.1 Publication
    Corresponds to variant rs45593337 [ dbSNP | Ensembl ].
    VAR_025825
    Natural varianti274 – 2741A → V.1 Publication
    Corresponds to variant rs3734458 [ dbSNP | Ensembl ].
    VAR_025826

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M68956 mRNA. Translation: AAA59555.1.
    M68955 Genomic DNA. Translation: AAA59554.1.
    D10522 mRNA. Translation: BAA01392.1.
    DQ341274 Genomic DNA. Translation: ABC67467.1.
    AL132660 Genomic DNA. Translation: CAI19942.1.
    CH471051 Genomic DNA. Translation: EAW48258.1.
    CH471051 Genomic DNA. Translation: EAW48259.1.
    BC089040 mRNA. Translation: AAH89040.1.
    CCDSiCCDS5101.1.
    PIRiA38873.
    RefSeqiNP_002347.5. NM_002356.5.
    UniGeneiHs.519909.
    Hs.712658.

    Genome annotation databases

    GeneIDi4082.
    KEGGihsa:4082.
    UCSCiuc003pvy.4. human.

    Polymorphism databases

    DMDMi76803798.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M68956 mRNA. Translation: AAA59555.1 .
    M68955 Genomic DNA. Translation: AAA59554.1 .
    D10522 mRNA. Translation: BAA01392.1 .
    DQ341274 Genomic DNA. Translation: ABC67467.1 .
    AL132660 Genomic DNA. Translation: CAI19942.1 .
    CH471051 Genomic DNA. Translation: EAW48258.1 .
    CH471051 Genomic DNA. Translation: EAW48259.1 .
    BC089040 mRNA. Translation: AAH89040.1 .
    CCDSi CCDS5101.1.
    PIRi A38873.
    RefSeqi NP_002347.5. NM_002356.5.
    UniGenei Hs.519909.
    Hs.712658.

    3D structure databases

    ProteinModelPortali P29966.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110257. 25 interactions.
    IntActi P29966. 6 interactions.
    MINTi MINT-4999508.
    STRINGi 9606.ENSP00000357624.

    PTM databases

    PhosphoSitei P29966.

    Polymorphism databases

    DMDMi 76803798.

    Proteomic databases

    MaxQBi P29966.
    PaxDbi P29966.
    PeptideAtlasi P29966.
    PRIDEi P29966.

    Protocols and materials databases

    DNASUi 4082.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 4082.
    KEGGi hsa:4082.
    UCSCi uc003pvy.4. human.

    Organism-specific databases

    CTDi 4082.
    GeneCardsi GC06P114189.
    H-InvDB HIX0006152.
    HGNCi HGNC:6759. MARCKS.
    HPAi CAB022062.
    HPA051913.
    HPA054820.
    MIMi 177061. gene.
    neXtProti NX_P29966.
    PharmGKBi PA30637.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG44640.
    HOGENOMi HOG000113482.
    HOVERGENi HBG081955.
    InParanoidi P29966.
    KOi K12561.
    OMAi MGTPLSK.
    OrthoDBi EOG7P2XW3.
    TreeFami TF332815.

    Enzyme and pathway databases

    Reactomei REACT_18405. Acetylcholine regulates insulin secretion.

    Miscellaneous databases

    GeneWikii MARCKS.
    GenomeRNAii 4082.
    NextBioi 16000.
    PROi P29966.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P29966.
    Bgeei P29966.
    CleanExi HS_MARCKS.
    Genevestigatori P29966.

    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. "The human myristoylated alanine-rich C kinase substrate (MARCKS) gene (MACS). Analysis of its gene product, promoter, and chromosomal localization."
      Harlan D.M., Graff J.M., Stumpo D.J., Eddy R.L. Jr., Shows T.B., Boyle J.M., Blackshear P.J.
      J. Biol. Chem. 266:14399-14405(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
    2. "Molecular cloning and chromosomal mapping of a cDNA encoding human 80K-L protein: major substrate for protein kinase C."
      Sakai K., Hirai M., Kudoh J., Minoshima S., Shimizu N.
      Genomics 14:175-178(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. NIEHS SNPs program
      Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-250 AND VAL-274.
    4. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Brain.
    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 189-322.
    8. "PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163."
      Palmer R.H., Schonwasser D.C., Rahman D., Pappin D.J., Herget T., Parker P.J.
      FEBS Lett. 378:281-285(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-159; SER-163 AND SER-170.
    9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46; SER-77; SER-101 AND SER-170, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-46; SER-77; SER-81; SER-118; THR-143; SER-145 AND THR-150, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-46; SER-101; THR-150; SER-163; SER-167 AND SER-170, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46; SER-63; SER-77; SER-81; SER-101; THR-150; SER-163 AND SER-170, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMARCS_HUMAN
    AccessioniPrimary (citable) accession number: P29966
    Secondary accession number(s): E1P560, Q2LA83, Q5TDB7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 129 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3