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UniProtKB/Swiss-Prot entry P29966


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MARCS_HUMAN
Primary accession number P29966
Secondary accession numbers Q2LA83 Q5TDB7
Integrated into Swiss-Prot on April 1, 1993
Sequence was last modified on January 23, 2007 (Sequence version 4)
Annotations were last modified on    June 16, 2009 (Entry version 81)
Name and origin of the protein
Protein name Myristoylated alanine-rich C-kinase substrate
Synonyms MARCKS
Protein kinase C substrate, 80 kDa protein, light chain
PKCSL
80K-L protein
Gene name
Name: MARCKS
Synonyms: MACS, PRKCSL
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
PubMed=1860846 [NCBI, ExPASy, EBI, Israel, Japan]
Harlan D.M., Graff J.M., Stumpo D.J., Eddy R.L. Jr., Shows T.B., Boyle J.M., Blackshear P.J.;
"The human myristoylated alanine-rich C kinase substrate (MARCKS) gene (MACS). Analysis of its gene product, promoter, and chromosomal localization.";
J. Biol. Chem. 266:14399-14405(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/S0888-7543(05)80301-5; PubMed=1427823 [NCBI, ExPASy, EBI, Israel, Japan]
Sakai K., Hirai M., Kudoh J., Minoshima S., Shimizu N.;
"Molecular cloning and chromosomal mapping of a cDNA encoding human 80K-L protein: major substrate for protein kinase C.";
Genomics 14:175-178(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-250 AND VAL-274.
NIEHS SNPs program;
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02055; PubMed=14574404 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 189-322.
DOI=10.1111/j.1432-1033.1992.tb17255.x; PubMed=1396720 [NCBI, ExPASy, EBI, Israel, Japan]
Herget T., Brooks S.F., Broad S., Rozengurt E.;
"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.";
Eur. J. Biochem. 209:7-14(1992).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46; SER-77; SER-81; SER-101; THR-143; SER-145; SER-159; SER-163; SER-167 AND SER-170, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND SER-167, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan]
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"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.";
J. Proteome Res. 6:4150-4162(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-27; SER-29; SER-145; THR-150; SER-163; SER-167 AND SER-170, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan]
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-159 AND SER-170, AND MASS SPECTROMETRY.
DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan]
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Anal. Sci. 24:161-166(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-46; SER-77; SER-81; SER-101; SER-118; THR-143; SER-145; SER-147; THR-150; SER-163; SER-167 AND SER-170, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M68956; AAA59555.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M68955; AAA59554.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D10522; BAA01392.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ341274; ABC67467.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL132660; CAI19942.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC089040; AAH89040.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00219301; -.
PIR A38873; A38873.
RefSeq NP_002347.5; -.
UniGene Hs.519909
3D structure databases
ModBase P29966.
Protein-protein interaction databases
IntAct P29966; 3.
PTM databases
PhosphoSite P29966; -.
Organism-specific databases
GeneCards GC06P114285; -.
HGNC HGNC:6759; MARCKS.
GenAtlas MARCKS.
MIM 177061; gene. [NCBI / EBI]
PharmGKB PA30637; -.
Gene expression databases
ArrayExpress P29966; -.
Bgee P29966; -.
CleanEx HS_MARCKS; -.
GermOnline ENSG00000155130; Homo sapiens.
Ontologies
GO
GO:0015629; Cellular component: actin cytoskeleton (traceable author statement from ProtInc).
GO:0016020; Cellular component: membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0051015; Molecular function: actin filament binding (traceable author statement from ProtInc).
GO:0005516; Molecular function: calmodulin binding (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR002101; MARCKS.
Graphical view of domain structure.
PANTHER PTHR14353; MARCKS; 1.
Pfam PF02063; MARCKS; 1.
Pfam graphical view of domain structure.
PRINTS PR00963; MARCKS.
PROSITE PS00826; MARCKS_1; 1.
PS00827; MARCKS_2; 1.
Proteomic databases
PeptideAtlas P29966; -.
PRIDE P29966; -.
Genome annotation databases
Ensembl ENSG00000155130; Homo sapiens. [Contig view]
GeneID 4082; -.
KEGG hsa:4082; -.
Phylogenomic databases
HOGENOM P29966; -.
HOVERGEN P29966; -.
OMA P29966; MGTPLSK.
Other
NextBio 16000; -.
SOURCE MARCKS; Homo sapiens.
ProtoNet P29966.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Actin-binding; Calmodulin-binding; Cytoplasm; Cytoskeleton; Lipoprotein; Membrane; Myristate; Phosphoprotein; Polymorphism.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   332  331     Myristoylated alanine-rich C-kinase substrate. PRO_0000157148
REGION   152   176  25     Calmodulin-binding (PSD). 
MOD_RES   26    26        Phosphoserine. 
MOD_RES   27    27        Phosphoserine. 
MOD_RES   29    29        Phosphoserine. 
MOD_RES   46    46        Phosphoserine. 
MOD_RES   77    77        Phosphoserine. 
MOD_RES   81    81        Phosphoserine. 
MOD_RES   101   101        Phosphoserine. 
MOD_RES   118   118        Phosphoserine. 
MOD_RES   135   135        Phosphoserine (By similarity). 
MOD_RES   143   143        Phosphothreonine. 
MOD_RES   145   145        Phosphoserine. 
MOD_RES   147   147        Phosphoserine. 
MOD_RES   150   150        Phosphothreonine. 
MOD_RES   159   159        Phosphoserine; by PKC. 
MOD_RES   163   163        Phosphoserine; by PKC. 
MOD_RES   167   167        Phosphoserine; by PKC. 
MOD_RES   170   170        Phosphoserine; by PKC. 
MOD_RES   262   262        Phosphoserine (By similarity). 
LIPID   2     2        N-myristoyl glycine (By similarity). 
VARIANT   250   250  1     P -> L. VAR_025825 
VARIANT   274   274  1     A -> V. VAR_025826 
CONFLICT   84    84        A -> S (in Ref. 2; BAA01392). 
CONFLICT   119   119        P -> A (in Ref. 2; BAA01392). 
CONFLICT   225   225        G -> R (in Ref. 6). 
CONFLICT   234   234        P -> S (in Ref. 1; AAA59555). 
CONFLICT   235   235        Q -> E (in Ref. 6). 
CONFLICT   287   308        PGAPPEQEAAPAEEPAAAAASS -> LVCPRRGGSPRGGARGRRSLNQ (in Ref. 1; AAA59555). 
Sequence information
Length: 332 AA [This is the length of the unprocessed precursor] Molecular weight: 31555 Da [This is the MW of the unprocessed precursor] CRC64: 0AB247801EF8FCBF [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGAQFSKTAA KGEAAAERPG EAAVASSPSK ANGQENGHVK VNGDASPAAA ESGAKEELQA 

        70         80         90        100        110        120 
NGSAPAADKE EPAAAGSGAA SPSAAEKGEP AAAAAPEAGA SPVEKEAPAE GEAAEPGSPT 

       130        140        150        160        170        180 
AAEGEAASAA SSTSSPKAED GATPSPSNET PKKKKKRFSF KKSFKLSGFS FKKNKKEAGE 

       190        200        210        220        230        240 
GGEAEAPAAE GGKDEAAGGA AAAAAEAGAA SGEQAAAPGE EAAAGEEGAA GGDPQEAKPQ 

       250        260        270        280        290        300 
EAAVAPEKPP ASDETKAAEE PSKVEEKKAE EAGASAAACE APSAAGPGAP PEQEAAPAEE 

       310        320        330 
PAAAAASSAC AAPSQEAQPE CSPEAPPAEA AE 

P29966 in FASTA format

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