Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P29966

- MARCS_HUMAN

UniProt

P29966 - MARCS_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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
Complete GO annotation...

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. focal adhesion Source: UniProtKB
  6. germinal vesicle Source: Ensembl
  7. plasma membrane Source: Reactome
Complete GO annotation...

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

BgeeiP29966.
CleanExiHS_MARCKS.
ExpressionAtlasiP29966. differential.
GenevestigatoriP29966.

Organism-specific databases

HPAiCAB022062.
HPA051913.
HPA054820.

Interactioni

Protein-protein interaction databases

BioGridi110257. 26 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.
GeneTreeiENSGT00730000111419.
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

        10         20         30         40         50
MGAQFSKTAA KGEAAAERPG EAAVASSPSK ANGQENGHVK VNGDASPAAA
60 70 80 90 100
ESGAKEELQA NGSAPAADKE EPAAAGSGAA SPSAAEKGEP AAAAAPEAGA
110 120 130 140 150
SPVEKEAPAE GEAAEPGSPT AAEGEAASAA SSTSSPKAED GATPSPSNET
160 170 180 190 200
PKKKKKRFSF KKSFKLSGFS FKKNKKEAGE GGEAEAPAAE GGKDEAAGGA
210 220 230 240 250
AAAAAEAGAA SGEQAAAPGE EAAAGEEGAA GGDPQEAKPQ EAAVAPEKPP
260 270 280 290 300
ASDETKAAEE PSKVEEKKAE EAGASAAACE APSAAGPGAP PEQEAAPAEE
310 320 330
PAAAAASSAC AAPSQEAQPE CSPEAPPAEA AE
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

EnsembliENST00000612661; ENSP00000478061; ENSG00000277443.
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. 26 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

Ensembli ENST00000612661 ; ENSP00000478061 ; ENSG00000277443 .
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.
GeneTreei ENSGT00730000111419.
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

Bgeei P29966.
CleanExi HS_MARCKS.
ExpressionAtlasi P29966. differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 130 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