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Protein

MARCKS-related protein

Gene

MARCKSL1

Organism
Homo sapiens (Human)
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 (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Actin-binding, Calmodulin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
MARCKS-related protein
Alternative name(s):
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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:7142. MARCKSL1.

Subcellular locationi

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

  • 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 (By similarity). In prostate cancers, detected in the cytoplasm and associated with apical or basal membranes (By similarity).By similarity

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • plasma membrane Source: LIFEdb
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30857.

Polymorphism and mutation databases

BioMutaiMARCKSL1.
DMDMi1346576.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 195194MARCKS-related proteinPRO_0000157152Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine1 Publication
Modified residuei14 – 141PhosphothreonineBy similarity
Modified residuei22 – 221PhosphoserineCombined sources
Modified residuei36 – 361PhosphoserineCombined sources
Modified residuei41 – 411PhosphoserineCombined sources
Modified residuei48 – 481PhosphoserineBy similarity
Modified residuei71 – 711PhosphoserineCombined sources
Modified residuei85 – 851PhosphothreonineBy similarity
Modified residuei93 – 931PhosphoserineCombined sources
Modified residuei101 – 1011PhosphoserineCombined sources
Modified residuei104 – 1041PhosphoserineCombined sources
Modified residuei119 – 1191PhosphoserineBy similarity
Modified residuei120 – 1201PhosphoserineCombined sources
Modified residuei135 – 1351PhosphoserineBy similarity
Modified residuei148 – 1481PhosphothreonineCombined sources
Modified residuei151 – 1511PhosphoserineCombined sources
Modified residuei162 – 1621PhosphoserineBy similarity
Modified residuei165 – 1651PhosphoserineBy similarity
Modified residuei178 – 1781PhosphothreonineCombined sources
Modified residuei187 – 1871PhosphothreonineBy similarity

Post-translational modificationi

Phosphorylation at Ser-120 and Thr-178 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 (By similarity).By similarity

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

EPDiP49006.
MaxQBiP49006.
PaxDbiP49006.
PeptideAtlasiP49006.
PRIDEiP49006.
TopDownProteomicsiP49006.

PTM databases

iPTMnetiP49006.
PhosphoSiteiP49006.
SwissPalmiP49006.

Miscellaneous databases

PMAP-CutDBP49006.

Expressioni

Gene expression databases

BgeeiP49006.
CleanExiHS_MARCKSL1.
GenevisibleiP49006. HS.

Organism-specific databases

HPAiCAB020787.
HPA030528.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
LOXL2Q9Y4K04EBI-4289961,EBI-7172227

Protein-protein interaction databases

BioGridi122395. 41 interactions.
IntActiP49006. 6 interactions.
MINTiMINT-5001034.
STRINGi9606.ENSP00000362638.

Structurei

3D structure databases

ProteinModelPortaliP49006.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi87 – 915Poly-Lys

Sequence similaritiesi

Belongs to the MARCKS family.Curated

Phylogenomic databases

eggNOGiENOG410IDYZ. Eukaryota.
ENOG410Z8K4. LUCA.
GeneTreeiENSGT00730000111349.
HOGENOMiHOG000059262.
HOVERGENiHBG003515.
InParanoidiP49006.
KOiK13536.
OMAiEIGACGE.
OrthoDBiEOG7W41DW.
PhylomeDBiP49006.
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.

P49006-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSQSSKAPR GDVTAEEAAG ASPAKANGQE NGHVKSNGDL SPKGEGESPP
60 70 80 90 100
VNGTDEAAGA TGDAIEPAPP SQGAEAKGEV PPKETPKKKK KFSFKKPFKL
110 120 130 140 150
SGLSFKRNRK EGGGDSSASS PTEEEQEQGE IGACSDEGTA QEGKAAATPE
160 170 180 190
SQEPQAKGAE ASAASEEEAG PQATEPSTPS GPESGPTPAS AEQNE
Length:195
Mass (Da):19,529
Last modified:January 23, 2007 - v2
Checksum:i8B997FAA8D20E34B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti70 – 701P → T in AAH66915 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70326 mRNA. Translation: CAA49793.1.
AL109945 Genomic DNA. Translation: CAI22887.1.
AY293577 Genomic DNA. Translation: AAP37955.1.
AL713653 mRNA. Translation: CAD28462.1.
CH471059 Genomic DNA. Translation: EAX07538.1.
CH471059 Genomic DNA. Translation: EAX07539.1.
BC007904 mRNA. Translation: AAH07904.1.
BC066915 mRNA. Translation: AAH66915.1.
CCDSiCCDS361.1.
PIRiS31861.
RefSeqiNP_075385.1. NM_023009.6.
UniGeneiHs.75061.

Genome annotation databases

EnsembliENST00000329421; ENSP00000362638; ENSG00000175130.
GeneIDi65108.
KEGGihsa:65108.
UCSCiuc001bvd.5. human.

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70326 mRNA. Translation: CAA49793.1.
AL109945 Genomic DNA. Translation: CAI22887.1.
AY293577 Genomic DNA. Translation: AAP37955.1.
AL713653 mRNA. Translation: CAD28462.1.
CH471059 Genomic DNA. Translation: EAX07538.1.
CH471059 Genomic DNA. Translation: EAX07539.1.
BC007904 mRNA. Translation: AAH07904.1.
BC066915 mRNA. Translation: AAH66915.1.
CCDSiCCDS361.1.
PIRiS31861.
RefSeqiNP_075385.1. NM_023009.6.
UniGeneiHs.75061.

3D structure databases

ProteinModelPortaliP49006.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122395. 41 interactions.
IntActiP49006. 6 interactions.
MINTiMINT-5001034.
STRINGi9606.ENSP00000362638.

PTM databases

iPTMnetiP49006.
PhosphoSiteiP49006.
SwissPalmiP49006.

Polymorphism and mutation databases

BioMutaiMARCKSL1.
DMDMi1346576.

Proteomic databases

EPDiP49006.
MaxQBiP49006.
PaxDbiP49006.
PeptideAtlasiP49006.
PRIDEiP49006.
TopDownProteomicsiP49006.

Protocols and materials databases

DNASUi65108.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000329421; ENSP00000362638; ENSG00000175130.
GeneIDi65108.
KEGGihsa:65108.
UCSCiuc001bvd.5. human.

Organism-specific databases

CTDi65108.
GeneCardsiMARCKSL1.
HGNCiHGNC:7142. MARCKSL1.
HPAiCAB020787.
HPA030528.
MIMi602940. gene.
neXtProtiNX_P49006.
PharmGKBiPA30857.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IDYZ. Eukaryota.
ENOG410Z8K4. LUCA.
GeneTreeiENSGT00730000111349.
HOGENOMiHOG000059262.
HOVERGENiHBG003515.
InParanoidiP49006.
KOiK13536.
OMAiEIGACGE.
OrthoDBiEOG7W41DW.
PhylomeDBiP49006.
TreeFamiTF332815.

Miscellaneous databases

ChiTaRSiMARCKSL1. human.
GeneWikiiMARCKSL1.
GenomeRNAii65108.
NextBioi67298.
PMAP-CutDBP49006.
PROiP49006.
SOURCEiSearch...

Gene expression databases

BgeeiP49006.
CleanExiHS_MARCKSL1.
GenevisibleiP49006. HS.

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. "cDNA and derived amino acid sequence of human maeMARCKS an LPS-inducible macrophage PKC substrate."
    Blockx H., Maertebs C., Fransen L.M.L.
    Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  3. NIEHS SNPs program
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [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 and Muscle.
  7. "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-22, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; THR-148 AND THR-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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].
  11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-41 AND SER-71, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "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-22; SER-101 AND SER-104, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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-22; SER-36; SER-41; SER-93; SER-101; SER-104; THR-148 AND SER-151, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104; SER-120; THR-148 AND THR-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  16. "Global profiling of co- and post-translationally N-myristoylated proteomes in human cells."
    Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H., Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.
    Nat. Commun. 5:4919-4919(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiMRP_HUMAN
AccessioniPrimary (citable) accession number: P49006
Secondary accession number(s): D3DPQ0, Q5TEE6, Q6NXS5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: April 13, 2016
This is version 145 of the entry and version 2 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 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.