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Protein

Myristoylated alanine-rich C-kinase substrate

Gene

Marcks

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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

  • phosphatidylserine binding Source: RGD
  • phospholipid binding Source: RGD

GO - Biological processi

  • actin filament organization Source: RGD
  • activation of phospholipase D activity Source: RGD
  • brain development Source: RGD
  • cell-substrate adhesion Source: RGD
  • intracellular protein transport Source: RGD
  • positive regulation of dendritic spine morphogenesis Source: RGD
  • positive regulation of glucose import in response to insulin stimulus Source: RGD
  • positive regulation of neuron projection development Source: RGD
  • positive regulation of protein kinase C activity Source: RGD
  • ventricular cardiac muscle tissue development Source: RGD
Complete GO annotation...

Keywords - Ligandi

Actin-binding, Calmodulin-binding

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
Gene namesi
Name:Marcks
Synonyms:Macs
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3028. Marcks.

Subcellular locationi

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

GO - Cellular componenti

  • axon terminus Source: RGD
  • bleb Source: RGD
  • chromatoid body Source: RGD
  • cytoplasm Source: UniProtKB
  • cytoskeleton Source: UniProtKB-SubCell
  • cytosol Source: RGD
  • dendritic branch Source: RGD
  • dendritic spine Source: RGD
  • growth cone Source: RGD
  • lysosome Source: RGD
  • membrane Source: RGD
  • outer dense fiber Source: RGD
  • plasma membrane Source: RGD
  • synapse Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 309308Myristoylated alanine-rich C-kinase substratePRO_0000157150Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineBy similarity
Modified residuei26 – 261PhosphoserineCombined sources
Modified residuei27 – 271PhosphoserineCombined sources
Modified residuei29 – 291PhosphoserineCombined sources
Modified residuei46 – 461PhosphoserineCombined sources
Modified residuei63 – 631PhosphoserineCombined sources
Modified residuei74 – 741PhosphoserineCombined sources
Modified residuei79 – 791PhosphothreonineCombined sources
Modified residuei113 – 1131PhosphoserineCombined sources
Modified residuei122 – 1221PhosphoserineCombined sources
Modified residuei128 – 1281PhosphoserineBy similarity
Modified residuei138 – 1381PhosphoserineCombined sources
Modified residuei140 – 1401PhosphoserineBy similarity
Modified residuei141 – 1411PhosphoserineBy similarity
Modified residuei143 – 1431PhosphothreonineCombined sources
Modified residuei152 – 1521Phosphoserine; by PKC1 Publication
Modified residuei156 – 1561Phosphoserine; by PKCCombined sources1 Publication
Modified residuei160 – 1601PhosphoserineCombined sources
Modified residuei163 – 1631Phosphoserine; by PKCCombined sources1 Publication
Modified residuei218 – 2181PhosphoserineCombined sources
Modified residuei246 – 2461PhosphoserineBy similarity
Modified residuei291 – 2911PhosphoserineBy similarity

Post-translational modificationi

Phosphorylation by PKC displaces MARCKS from the membrane. It also inhibits the F-actin cross-linking activity.1 Publication

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

PaxDbiP30009.
PRIDEiP30009.

PTM databases

iPTMnetiP30009.
PhosphoSiteiP30009.

Expressioni

Tissue specificityi

Highest levels found in spleen and brain. Intermediate levels seen in thymus, ovary, lung and heart. Very low levels seen in kidney, skeletal muscle and liver.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000000707.

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

eggNOGiENOG410J04K. Eukaryota.
ENOG4111SZ0. LUCA.
HOGENOMiHOG000113482.
InParanoidiP30009.

Family and domain databases

InterProiIPR002101. MARCKS.
[Graphical view]
PANTHERiPTHR14353. PTHR14353. 2 hits.
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.

P30009-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGAQFSKTAA KGEAAAERPG EAAVASSPSK ANGQENGHVK VNGDASPAAA
60 70 80 90 100
EPGAKEELQA NGSAPAADKE EPASGGAATP AAADKDEAAA APEPGAATAD
110 120 130 140 150
KEAAEAEPAE PGSPSAETEG ASASSTSSPK AEDGAAPSPS SETPKKKKKR
160 170 180 190 200
FSFKKSFKLS GFSFKKSKKE AGEGAEAEGA TADGAKDEAA AAAGGDAAAA
210 220 230 240 250
PGEQAGGAGA EGAEGGESRE AEAAEPEQPE QPEQPAAEEP RAEEPSEAVG
260 270 280 290 300
EKAEEPAPGA TADDAPSAAG PEQEAPAATD EPAASAAPSA SPEPQPECSP

EAPPAPVAE
Length:309
Mass (Da):29,795
Last modified:January 23, 2007 - v2
Checksum:i9957F2037F203316
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti29 – 291S → G AA sequence (PubMed:2676596).Curated
Sequence conflicti183 – 1831D → E (PubMed:1396720).Curated
Sequence conflicti216 – 2161G → E AA sequence (PubMed:2676596).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59859 mRNA. No translation available.
PIRiA39773.
UniGeneiRn.9560.

Genome annotation databases

UCSCiRGD:3028. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59859 mRNA. No translation available.
PIRiA39773.
UniGeneiRn.9560.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000000707.

PTM databases

iPTMnetiP30009.
PhosphoSiteiP30009.

Proteomic databases

PaxDbiP30009.
PRIDEiP30009.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:3028. rat.

Organism-specific databases

RGDi3028. Marcks.

Phylogenomic databases

eggNOGiENOG410J04K. Eukaryota.
ENOG4111SZ0. LUCA.
HOGENOMiHOG000113482.
InParanoidiP30009.

Miscellaneous databases

PROiP30009.

Family and domain databases

InterProiIPR002101. MARCKS.
[Graphical view]
PANTHERiPTHR14353. PTHR14353. 2 hits.
PfamiPF02063. MARCKS. 1 hit.
[Graphical view]
PRINTSiPR00963. MARCKS.
PROSITEiPS00826. MARCKS_1. 1 hit.
PS00827. MARCKS_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and characterization of the acidic 80-kDa protein kinase C substrate from rat brain. Identification as a glycoprotein."
    Erusalimsky J.D., Brooks S.F., Herget T., Morris C., Rozengurt E.
    J. Biol. Chem. 266:7073-7080(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Internal amino acid sequence analysis of the 80 kDa protein kinase C substrate from rat brain: relationship to the 87 kDa substrate from bovine brain."
    Erusalimsky J.D., Morris C., Perks K., Brown R., Brooks S., Rozengurt E.
    FEBS Lett. 255:149-153(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 12-31; 189-217; 252-275 AND 300-309.
    Tissue: Brain.
  3. "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, TISSUE SPECIFICITY.
  4. "Protein kinase C phosphorylates Ser-152, Ser-156 and Ser-163 but not Ser-160 of MARCKS in rat brain."
    Heemskerk F.M., Chen H.C., Huang F.L.
    Biochem. Biophys. Res. Commun. 190:236-241(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-152; SER-156 AND SER-163.
    Tissue: Brain.
  5. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-27; SER-29; SER-46; SER-63; SER-74; THR-79; SER-113; SER-122; SER-138; THR-143; SER-156; SER-160; SER-163 AND SER-218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMARCS_RAT
AccessioniPrimary (citable) accession number: P30009
Secondary accession number(s): P20468
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: February 17, 2016
This is version 107 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.