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Protein

Myristoylated alanine-rich C-kinase substrate

Gene

MARCKS

Organism
Homo sapiens (Human)
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

  • actin filament binding Source: ProtInc
  • calmodulin binding Source: ProtInc
  • phosphatidylserine binding Source: Ensembl

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Actin-binding, Calmodulin-binding

Enzyme and pathway databases

ReactomeiR-HSA-399997. Acetylcholine regulates insulin secretion.
SIGNORiP29966.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:6759. MARCKS.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: ProtInc
  • axon terminus Source: Ensembl
  • bleb Source: Ensembl
  • cell cortex Source: Ensembl
  • centrosome Source: Ensembl
  • chromatoid body Source: Ensembl
  • cytosol Source: Ensembl
  • dendritic branch Source: Ensembl
  • dendritic spine Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • germinal vesicle Source: Ensembl
  • growth cone Source: Ensembl
  • lysosome Source: Ensembl
  • microtubule Source: Ensembl
  • outer dense fiber Source: Ensembl
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30637.

Polymorphism and mutation databases

BioMutaiMARCKS.
DMDMi76803798.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 332331Myristoylated alanine-rich C-kinase substratePRO_0000157148Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine1 Publication
Modified residuei26 – 261PhosphoserineCombined sources
Modified residuei27 – 271PhosphoserineCombined sources
Modified residuei29 – 291PhosphoserineCombined sources
Modified residuei46 – 461PhosphoserineCombined sources
Modified residuei63 – 631PhosphoserineCombined sources
Modified residuei77 – 771PhosphoserineCombined sources
Modified residuei81 – 811PhosphoserineCombined sources
Modified residuei101 – 1011PhosphoserineCombined sources
Modified residuei118 – 1181PhosphoserineCombined sources
Modified residuei128 – 1281PhosphoserineBy similarity
Modified residuei135 – 1351PhosphoserineCombined sources
Modified residuei143 – 1431PhosphothreonineCombined sources
Modified residuei145 – 1451PhosphoserineCombined sources
Modified residuei147 – 1471PhosphoserineCombined sources
Modified residuei150 – 1501PhosphothreonineCombined sources
Modified residuei159 – 1591Phosphoserine; by PKC1 Publication
Modified residuei163 – 1631Phosphoserine; by PKCCombined sources1 Publication
Modified residuei167 – 1671Phosphoserine; by PKCCombined sources
Modified residuei170 – 1701Phosphoserine; by PKCCombined sources1 Publication
Modified residuei262 – 2621PhosphoserineBy similarity
Modified residuei314 – 3141PhosphoserineCombined sources

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

EPDiP29966.
MaxQBiP29966.
PaxDbiP29966.
PeptideAtlasiP29966.
PRIDEiP29966.
TopDownProteomicsiP29966.

PTM databases

iPTMnetiP29966.
PhosphoSiteiP29966.
SwissPalmiP29966.

Expressioni

Gene expression databases

BgeeiENSG00000155130.
CleanExiHS_MARCKS.
ExpressionAtlasiP29966. baseline and differential.
GenevisibleiP29966. HS.

Organism-specific databases

HPAiCAB022062.

Interactioni

GO - Molecular functioni

  • actin filament binding Source: ProtInc
  • calmodulin binding Source: ProtInc

Protein-protein interaction databases

BioGridi110257. 32 interactions.
IntActiP29966. 14 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

eggNOGiENOG410J04K. Eukaryota.
ENOG4111SZ0. LUCA.
GeneTreeiENSGT00730000111419.
HOGENOMiHOG000113482.
HOVERGENiHBG081955.
InParanoidiP29966.
KOiK12561.
OMAiMGTPLSK.
OrthoDBiEOG091G1B6O.
TreeFamiTF332815.

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.

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:
EMBLi
GenBanki
DDBJi
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_002356.6.
UniGeneiHs.519909.
Hs.712658.

Genome annotation databases

EnsembliENST00000612661; ENSP00000478061; ENSG00000277443.
GeneIDi4082.
KEGGihsa:4082.
UCSCiuc032xir.2. human.

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:
EMBLi
GenBanki
DDBJi
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_002356.6.
UniGeneiHs.519909.
Hs.712658.

3D structure databases

ProteinModelPortaliP29966.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110257. 32 interactions.
IntActiP29966. 14 interactions.
MINTiMINT-4999508.
STRINGi9606.ENSP00000357624.

PTM databases

iPTMnetiP29966.
PhosphoSiteiP29966.
SwissPalmiP29966.

Polymorphism and mutation databases

BioMutaiMARCKS.
DMDMi76803798.

Proteomic databases

EPDiP29966.
MaxQBiP29966.
PaxDbiP29966.
PeptideAtlasiP29966.
PRIDEiP29966.
TopDownProteomicsiP29966.

Protocols and materials databases

DNASUi4082.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000612661; ENSP00000478061; ENSG00000277443.
GeneIDi4082.
KEGGihsa:4082.
UCSCiuc032xir.2. human.

Organism-specific databases

CTDi4082.
GeneCardsiMARCKS.
H-InvDBHIX0006152.
HGNCiHGNC:6759. MARCKS.
HPAiCAB022062.
MIMi177061. gene.
neXtProtiNX_P29966.
PharmGKBiPA30637.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410J04K. Eukaryota.
ENOG4111SZ0. LUCA.
GeneTreeiENSGT00730000111419.
HOGENOMiHOG000113482.
HOVERGENiHBG081955.
InParanoidiP29966.
KOiK12561.
OMAiMGTPLSK.
OrthoDBiEOG091G1B6O.
TreeFamiTF332815.

Enzyme and pathway databases

ReactomeiR-HSA-399997. Acetylcholine regulates insulin secretion.
SIGNORiP29966.

Miscellaneous databases

ChiTaRSiMARCKS. human.
GeneWikiiMARCKS.
GenomeRNAii4082.
PROiP29966.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000155130.
CleanExiHS_MARCKS.
ExpressionAtlasiP29966. baseline and differential.
GenevisibleiP29966. HS.

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...

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: September 7, 2016
This is version 149 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

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.