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Protein

MARCKS-related protein

Gene

Marcksl1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Controls cell movement by regulating actin cytoskeleton homeostasis and filopodium and lamellipodium formation. When unphosphorylated, induces cell migration. When phosphorylated by MAPK8, induces actin bundles formation and stabilization, thereby reducing actin plasticity, hence restricting cell movement, including neuronal migration. May also affect cancer cell migration. May be involved in coupling the protein kinase C and calmodulin signal transduction systems.1 Publication

GO - Biological processi

  • positive regulation of cell proliferation Source: MGI
Complete GO annotation...

Keywords - Ligandi

Actin-binding, Calmodulin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
MARCKS-related protein
Alternative name(s):
Brain protein F52
MARCKS-like protein 1
Macrophage myristoylated alanine-rich C kinase substrate
Short name:
Mac-MARCKS
Short name:
MacMARCKS
Gene namesi
Name:Marcksl1
Synonyms:Mlp, Mrp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:97143. Marcksl1.

Subcellular locationi

  • Cytoplasm
  • Cell membrane By similarity; Lipid-anchor By similarity

  • Note: Associates with the membrane via the insertion of the N-terminal N-myristoyl chain and the partial insertion of the effector domain. Association of the effector domain with membranes may be regulated by Ca2+/calmodulin.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi120 – 1201S → A: Complete loss of MAPK-mediated phosphorylation; when associated with A-148 and A-183. In neurons, induces the generation of large, flat lamellipodial protrusions; when associated with A-148 and A-183. 1 Publication
Mutagenesisi120 – 1201S → D: Induction of F-actin-bundling; when associated with D-148 and D-183. In neurons, induces the generation of long and prominent filopodia; when associated with D-148 and D-183. 1 Publication
Mutagenesisi148 – 1481T → A: Complete loss of MAPK-mediated phosphorylation; when associated with A-120 and A-183. In neurons, induces the generation of large, flat lamellipodial protrusions; when associated with A-120 and A-183. 1 Publication
Mutagenesisi148 – 1481T → D: Induction of F-actin-bundling; when associated with D-120 and D-183. In neurons, induces the generation of long and prominent filopodia; when associated with D-120 and D-183. 1 Publication
Mutagenesisi183 – 1831T → A: Complete loss of MAPK-mediated phosphorylation; when associated with A-120 and A-148. In neurons, induces the generation of large, flat lamellipodial protrusions; when associated with A-120 and A-148. 1 Publication
Mutagenesisi183 – 1831T → D: Induction of F-actin-bundling; when associated with D-120 and D-148. In neurons, induces the generation of long and prominent filopodia; when associated with D-120 and D-148. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 200199MARCKS-related proteinPRO_0000157153Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine1 Publication
Modified residuei14 – 141PhosphothreonineCombined sources
Modified residuei22 – 221PhosphoserineCombined sources
Modified residuei36 – 361PhosphoserineBy similarity
Modified residuei48 – 481PhosphoserineCombined sources
Modified residuei71 – 711PhosphoserineCombined sources
Modified residuei85 – 851PhosphothreonineCombined sources
Modified residuei93 – 931Phosphoserine; by PKCBy similarity
Modified residuei101 – 1011Phosphoserine; by PKCBy similarity
Modified residuei104 – 1041Phosphoserine; by PKCBy similarity
Modified residuei119 – 1191PhosphoserineCombined sources
Modified residuei120 – 1201Phosphoserine; by MAPK8Combined sources1 Publication
Modified residuei132 – 1321PhosphoserineCombined sources
Modified residuei135 – 1351PhosphoserineCombined sources
Modified residuei148 – 1481Phosphothreonine; by MAPK8Combined sources1 Publication
Modified residuei151 – 1511PhosphoserineBy similarity
Modified residuei162 – 1621PhosphoserineCombined sources
Modified residuei165 – 1651PhosphoserineCombined sources
Modified residuei170 – 1701PhosphothreonineCombined sources
Modified residuei183 – 1831Phosphothreonine; by MAPK8Combined sources1 Publication
Modified residuei192 – 1921PhosphothreonineCombined sources

Post-translational modificationi

Phosphorylation at Ser-120 and Thr-183 are non-redundantly catalyzed by MAPK8 in vivo. Phosphorylation at Thr-148 is preferentially catalyzed by MAPK8 in vivo, but this modification can also be catalyzed by other kinases in the absence of MAPK8.1 Publication

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

EPDiP28667.
MaxQBiP28667.
PaxDbiP28667.
PeptideAtlasiP28667.
PRIDEiP28667.

PTM databases

iPTMnetiP28667.
PhosphoSiteiP28667.
SwissPalmiP28667.

Miscellaneous databases

PMAP-CutDBP28667.

Expressioni

Tissue specificityi

Expressed at high levels in brain cortex and hippocampus (at protein level), including dentate gyrus, anterior olfactory nucleus, primary olfactory cortex, entorhinal cortex, medial preoptic area and dorsomedial hypothalamic nucleus. Expressed in neuronal cells (at protein level). Also detected in the retina. Up-regulated in a wide variety of cancers.2 Publications

Developmental stagei

Expressed in the developing neural tube as early as 8.5 dpc. Remains most highly expressed in the developing brain and spinal cord during later development at least until 14.5 dpc. Also detected in the lung, adrenal gland, gut and kidney, particularly the kidney cortex. Undetectable in the liver.1 Publication

Gene expression databases

BgeeiP28667.
CleanExiMM_MARCKSL1.
GenevisibleiP28667. MM.

Interactioni

Subunit structurei

Binds to filamentous actin (F-actin), but not to monomeric G-actin, independently of its phosphorylation status.

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000055637.

Structurei

3D structure databases

ProteinModelPortaliP28667.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni87 – 11024Effector domain involved in lipid-bindingAdd
BLAST
Regioni87 – 10014Calmodulin-binding (PSD)Add
BLAST

Sequence similaritiesi

Belongs to the MARCKS family.Curated

Phylogenomic databases

eggNOGiENOG410IDYZ. Eukaryota.
ENOG410Z8K4. LUCA.
GeneTreeiENSGT00730000111349.
HOGENOMiHOG000059262.
HOVERGENiHBG003515.
InParanoidiP28667.
KOiK13536.
OMAiEIGACGE.
OrthoDBiEOG7W41DW.
PhylomeDBiP28667.
TreeFamiTF332815.

Family and domain databases

InterProiIPR002101. MARCKS.
[Graphical view]
PANTHERiPTHR14353. PTHR14353. 1 hit.
PfamiPF02063. MARCKS. 2 hits.
[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.

P28667-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSQSSKAPR GDVTAEEAAG ASPAKANGQE NGHVRSNGDL TPKGEGESPP
60 70 80 90 100
VNGTDEAAGA TGDAIEPAPP SQEAEAKGEV APKETPKKKK KFSFKKPFKL
110 120 130 140 150
SGLSFKRNRK EGGGDSSASS PTEEEQEQGE MSACSDEGTA QEGKAAATPE
160 170 180 190 200
SQEPQAKGAE ASAASKEGDT EEEAGPQAAE PSTPSGPESG PTPASAEQNE
Length:200
Mass (Da):20,165
Last modified:January 23, 2007 - v2
Checksum:iAA50A0E2029921AF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti134 – 1341C → S in AAH06757 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61399 mRNA. Translation: CAA43671.1.
S65597 Genomic DNA. Translation: AAP13962.1.
AK079390 mRNA. Translation: BAC37630.1.
AK083913 mRNA. Translation: BAC39058.1.
AK152990 mRNA. Translation: BAE31636.1.
AK169355 mRNA. Translation: BAE41104.1.
BC006757 mRNA. Translation: AAH06757.1.
CCDSiCCDS18695.1.
PIRiS17185.
RefSeqiNP_034937.1. NM_010807.4.
UniGeneiMm.424974.

Genome annotation databases

EnsembliENSMUST00000062356; ENSMUSP00000055637; ENSMUSG00000047945.
GeneIDi17357.
KEGGimmu:17357.
UCSCiuc008uxf.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61399 mRNA. Translation: CAA43671.1.
S65597 Genomic DNA. Translation: AAP13962.1.
AK079390 mRNA. Translation: BAC37630.1.
AK083913 mRNA. Translation: BAC39058.1.
AK152990 mRNA. Translation: BAE31636.1.
AK169355 mRNA. Translation: BAE41104.1.
BC006757 mRNA. Translation: AAH06757.1.
CCDSiCCDS18695.1.
PIRiS17185.
RefSeqiNP_034937.1. NM_010807.4.
UniGeneiMm.424974.

3D structure databases

ProteinModelPortaliP28667.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000055637.

PTM databases

iPTMnetiP28667.
PhosphoSiteiP28667.
SwissPalmiP28667.

Proteomic databases

EPDiP28667.
MaxQBiP28667.
PaxDbiP28667.
PeptideAtlasiP28667.
PRIDEiP28667.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000062356; ENSMUSP00000055637; ENSMUSG00000047945.
GeneIDi17357.
KEGGimmu:17357.
UCSCiuc008uxf.2. mouse.

Organism-specific databases

CTDi65108.
MGIiMGI:97143. Marcksl1.

Phylogenomic databases

eggNOGiENOG410IDYZ. Eukaryota.
ENOG410Z8K4. LUCA.
GeneTreeiENSGT00730000111349.
HOGENOMiHOG000059262.
HOVERGENiHBG003515.
InParanoidiP28667.
KOiK13536.
OMAiEIGACGE.
OrthoDBiEOG7W41DW.
PhylomeDBiP28667.
TreeFamiTF332815.

Miscellaneous databases

PMAP-CutDBP28667.
PROiP28667.
SOURCEiSearch...

Gene expression databases

BgeeiP28667.
CleanExiMM_MARCKSL1.
GenevisibleiP28667. MM.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "A mouse brain cDNA encodes a novel protein with the protein kinase C phosphorylation site domain common to MARCKS."
    Umekage T., Kato K.
    FEBS Lett. 286:147-151(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/cJ.
    Tissue: Brain.
  2. "MacMARCKS, a novel member of the MARCKS family of protein kinase C substrates."
    Li J., Aderem A.
    Cell 70:791-801(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Nucleotide sequence, expression, and chromosomal mapping of Mrp and mapping of five related sequences."
    Lobach D.F., Rochelle J.M., Watson M.L., Seldin M.F., Blackshear P.J.
    Genomics 17:194-204(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone marrow, Cerebellum, Kidney and Spinal ganglion.
  5. "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].
    Strain: NMRI.
    Tissue: Mammary gland.
  6. "Characteristics of the F52 protein, a MARCKS homologue."
    Blackshear P.J., Verghese G.M., Johnson J.D., Haupt D.M., Stumpo D.J.
    J. Biol. Chem. 267:13540-13546(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  7. "Interaction of the effector domain of MARCKS and MARCKS-related protein with lipid membranes revealed by electric potential measurements."
    Bahr G., Diederich A., Vergeres G., Winterhalter M.
    Biochemistry 37:16252-16261(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, MYRISTOYLATION AT GLY-2.
  8. "Promoter sequence, expression, and fine chromosomal mapping of the human gene (MLP) encoding the MARCKS-like protein: identification of neighboring and linked polymorphic loci for MLP and MACS and use in the evaluation of human neural tube defects."
    Stumpo D.J., Eddy R.L. Jr., Haley L.L., Sait S., Shows T.B., Lai W.S., Young W.S. III, Speer M.C., Dehejia A., Polymeropoulos M., Blackshear P.J.
    Genomics 49:253-264(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-48; SER-71; SER-135; THR-148; SER-162; SER-165; THR-170 AND THR-192, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  10. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; THR-85 AND THR-148, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14; SER-22; THR-85; SER-119; SER-120; SER-132; SER-135; THR-148; THR-170 AND THR-183, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  12. "c-Jun N-terminal kinase phosphorylation of MARCKSL1 determines actin stability and migration in neurons and in cancer cells."
    Bjorkblom B., Padzik A., Mohammad H., Westerlund N., Komulainen E., Hollos P., Parviainen L., Papageorgiou A.C., Iljin K., Kallioniemi O., Kallajoki M., Courtney M.J., Magard M., James P., Coffey E.T.
    Mol. Cell. Biol. 32:3513-3526(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH F-ACTIN, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-120; THR-148 AND THR-183, TISSUE SPECIFICITY, MUTAGENESIS OF SER-120; THR-148 AND THR-183.

Entry informationi

Entry nameiMRP_MOUSE
AccessioniPrimary (citable) accession number: P28667
Secondary accession number(s): Q3TEZ4, Q91W07
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 133 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, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.