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P29966 (MARCS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:MARCKS
Synonyms:MACS, PRKCSL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length332 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subcellular location

Cytoplasmcytoskeleton Probable. Membrane; Lipid-anchor By similarity.

Post-translational modification

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

Sequence similarities

Belongs to the MARCKS family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 332331Myristoylated alanine-rich C-kinase substrate
PRO_0000157148

Regions

Region152 – 17625Calmodulin-binding (PSD)

Amino acid modifications

Modified residue271Phosphoserine Ref.11 Ref.13
Modified residue461Phosphoserine Ref.9 Ref.11 Ref.13 Ref.15
Modified residue631Phosphoserine Ref.15
Modified residue771Phosphoserine Ref.9 Ref.11 Ref.15
Modified residue811Phosphoserine Ref.11 Ref.15
Modified residue1011Phosphoserine Ref.9 Ref.13 Ref.15
Modified residue1181Phosphoserine Ref.11
Modified residue1351Phosphoserine By similarity
Modified residue1431Phosphothreonine Ref.11
Modified residue1451Phosphoserine Ref.11
Modified residue1501Phosphothreonine Ref.11 Ref.13 Ref.15
Modified residue1591Phosphoserine; by PKC Ref.8
Modified residue1631Phosphoserine; by PKC Ref.8 Ref.13 Ref.15
Modified residue1671Phosphoserine; by PKC Ref.10 Ref.13
Modified residue1701Phosphoserine; by PKC Ref.8 Ref.9 Ref.13 Ref.15
Modified residue2621Phosphoserine By similarity
Lipidation21N-myristoyl glycine By similarity

Natural variations

Natural variant2501P → L. Ref.3
Corresponds to variant rs45593337 [ dbSNP | Ensembl ].
VAR_025825
Natural variant2741A → V. Ref.3
Corresponds to variant rs3734458 [ dbSNP | Ensembl ].
VAR_025826

Experimental info

Sequence conflict841A → S in BAA01392. Ref.2
Sequence conflict1191P → A in BAA01392. Ref.2
Sequence conflict2251G → R Ref.7
Sequence conflict2341P → S in AAA59555. Ref.1
Sequence conflict2351Q → E Ref.7
Sequence conflict287 – 30822PGAPP…AAASS → LVCPRRGGSPRGGARGRRSL NQ in AAA59555. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P29966 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 0AB247801EF8FCBF

FASTA33231,555
        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 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS5101.1.
PIRA38873.
RefSeqNP_002347.5. NM_002356.5.
UniGeneHs.519909.
Hs.712658.

3D structure databases

ProteinModelPortalP29966.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110257. 25 interactions.
IntActP29966. 6 interactions.
MINTMINT-4999508.
STRING9606.ENSP00000357624.

PTM databases

PhosphoSiteP29966.

Polymorphism databases

DMDM76803798.

Proteomic databases

MaxQBP29966.
PaxDbP29966.
PeptideAtlasP29966.
PRIDEP29966.

Protocols and materials databases

DNASU4082.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368635; ENSP00000357624; ENSG00000155130.
GeneID4082.
KEGGhsa:4082.
UCSCuc003pvy.4. human.

Organism-specific databases

CTD4082.
GeneCardsGC06P114189.
H-InvDBHIX0006152.
HGNCHGNC:6759. MARCKS.
HPACAB022062.
HPA051913.
HPA054820.
MIM177061. gene.
neXtProtNX_P29966.
PharmGKBPA30637.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG44640.
HOGENOMHOG000113482.
HOVERGENHBG081955.
InParanoidP29966.
KOK12561.
OMAMGTPLSK.
OrthoDBEOG7P2XW3.
TreeFamTF332815.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressP29966.
BgeeP29966.
CleanExHS_MARCKS.
GenevestigatorP29966.

Family and domain databases

InterProIPR002101. MARCKS.
[Graphical view]
PANTHERPTHR14353. PTHR14353. 1 hit.
PfamPF02063. MARCKS. 1 hit.
[Graphical view]
PRINTSPR00963. MARCKS.
PROSITEPS00826. MARCKS_1. 1 hit.
PS00827. MARCKS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiMARCKS.
GenomeRNAi4082.
NextBio16000.
PROP29966.
SOURCESearch...

Entry information

Entry nameMARCS_HUMAN
AccessionPrimary (citable) accession number: P29966
Secondary accession number(s): E1P560, Q2LA83, Q5TDB7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 127 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM