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Entry version 150 (16 Oct 2019)
Sequence version 2 (23 Jan 2007)
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Protein

MARCKS-related protein

Gene

Marcksl1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Involved in the control of cell movement by regulating actin cytoskeleton homeostasis and filopodium and lamellipodium formation (PubMed:22751924). When unphosphorylated, induces cell migration (PubMed:22751924). When phosphorylated by MAPK8, induces actin bundles formation and stabilization, thereby reducing actin plasticity, hence restricting cell movement, including neuronal migration (PubMed:22751924). May be involved in coupling the protein kinase C and calmodulin signal transduction systems (Probable).1 Publication1 Publication

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActin-binding, Calmodulin-binding

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Marcksl1
Synonyms:Mlp, Mrp
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 4

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:97143 Marcksl1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi120S → 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 Publication1
Mutagenesisi120S → 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 Publication1
Mutagenesisi148T → 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 Publication1
Mutagenesisi148T → 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 Publication1
Mutagenesisi183T → 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 Publication1
Mutagenesisi183T → 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 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001571532 – 200MARCKS-related proteinAdd BLAST199

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi2N-myristoyl glycine1 Publication1
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei14PhosphothreonineCombined sources1
Modified residuei22PhosphoserineCombined sources1
Modified residuei36PhosphoserineBy similarity1
Modified residuei48PhosphoserineCombined sources1
Modified residuei71PhosphoserineCombined sources1
Modified residuei85PhosphothreonineCombined sources1
Modified residuei93Phosphoserine; by PKCBy similarity1
Modified residuei101Phosphoserine; by PKCBy similarity1
Modified residuei104Phosphoserine; by PKCBy similarity1
Modified residuei119PhosphoserineCombined sources1
Modified residuei120Phosphoserine; by MAPK8Combined sources1 Publication1
Modified residuei132PhosphoserineCombined sources1
Modified residuei135PhosphoserineCombined sources1
Modified residuei148Phosphothreonine; by MAPK8Combined sources1 Publication1
Modified residuei151PhosphoserineBy similarity1
Modified residuei162PhosphoserineCombined sources1
Modified residuei165PhosphoserineCombined sources1
Modified residuei170PhosphothreonineCombined sources1
Modified residuei183Phosphothreonine; by MAPK8Combined sources1 Publication1
Modified residuei192PhosphothreonineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated (PubMed:1618855, PubMed:22751924). Phosphorylation at Ser-120 and Thr-183 is non-redundantly catalyzed by MAPK8 in vivo (PubMed:22751924). 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 (PubMed:22751924). May be phosphorylated by protein kinase C, which disrupts the interaction with calmodulin (PubMed:1618855).2 Publications

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P28667

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P28667

MaxQB - The MaxQuant DataBase

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MaxQBi
P28667

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P28667

PeptideAtlas

More...
PeptideAtlasi
P28667

PRoteomics IDEntifications database

More...
PRIDEi
P28667

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P28667

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P28667

SwissPalm database of S-palmitoylation events

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SwissPalmi
P28667

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
P28667

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed at high levels in brain cortex and hippocampus, including dentate gyrus, anterior olfactory nucleus, primary olfactory cortex, entorhinal cortex, medial preoptic area and dorsomedial hypothalamic nucleus (at protein level) (PubMed:1864362, PubMed:8406449, PubMed:9598313, PubMed:22751924). Expressed in neuronal cells (at protein level) (PubMed:22751924). Detected in the retina (PubMed:9598313). Strongly expressed in testis and uterus; expressed at lower levels in cerebellum, cerebrum, adipose tissue, spleen, kidney, thyroid, liver, lung, skeletal muscle and heart (PubMed:8406449). Detected in T-cells and B-cells (PubMed:8406449).4 Publications

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>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

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated in peritoneal macrophages in response to bacterial lipopolysaccharide (LPS).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSMUSG00000047945 Expressed in 319 organ(s), highest expression level in neocortex

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P28667 MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Binds to filamentous actin (F-actin), but not to monomeric G-actin, independently of its phosphorylation status (PubMed:22751924).

Interacts with calmodulin (PubMed:1618855).

2 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
201439, 2 interactors

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000055637

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni87 – 110Effector domain involved in lipid-binding and calmodulin-binding2 PublicationsAdd BLAST24

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the MARCKS family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410IDYZ Eukaryota
ENOG410Z8K4 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00730000111349

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000059262

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P28667

KEGG Orthology (KO)

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KOi
K13536

Identification of Orthologs from Complete Genome Data

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OMAi
EIGACGE

Database of Orthologous Groups

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OrthoDBi
1511774at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P28667

TreeFam database of animal gene trees

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TreeFami
TF332815

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR002101 MARCKS

The PANTHER Classification System

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PANTHERi
PTHR14353 PTHR14353, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF02063 MARCKS, 2 hits

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00963 MARCKS

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00826 MARCKS_1, 1 hit
PS00827 MARCKS_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iAA50A0E2029921AF
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti134C → S in AAH06757 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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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

The Consensus CDS (CCDS) project

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CCDSi
CCDS18695.1

Protein sequence database of the Protein Information Resource

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PIRi
S17185

NCBI Reference Sequences

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RefSeqi
NP_034937.1, NM_010807.4

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000062356; ENSMUSP00000055637; ENSMUSG00000047945

Database of genes from NCBI RefSeq genomes

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GeneIDi
17357

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:17357

UCSC genome browser

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UCSCi
uc008uxf.2 mouse

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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

3D structure databases

Database of comparative protein structure models

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ModBasei
Search...

SWISS-MODEL Interactive Workspace

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SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein-protein interaction databases

BioGridi201439, 2 interactors
STRINGi10090.ENSMUSP00000055637

PTM databases

iPTMnetiP28667
PhosphoSitePlusiP28667
SwissPalmiP28667

Proteomic databases

EPDiP28667
jPOSTiP28667
MaxQBiP28667
PaxDbiP28667
PeptideAtlasiP28667
PRIDEiP28667

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
65108
MGIiMGI:97143 Marcksl1

Phylogenomic databases

eggNOGiENOG410IDYZ Eukaryota
ENOG410Z8K4 LUCA
GeneTreeiENSGT00730000111349
HOGENOMiHOG000059262
InParanoidiP28667
KOiK13536
OMAiEIGACGE
OrthoDBi1511774at2759
PhylomeDBiP28667
TreeFamiTF332815

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
Marcksl1 mouse
PMAP-CutDBiP28667

Protein Ontology

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PROi
PR:P28667

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000047945 Expressed in 319 organ(s), highest expression level in neocortex
GenevisibleiP28667 MM

Family and domain databases

InterProiView protein in InterPro
IPR002101 MARCKS
PANTHERiPTHR14353 PTHR14353, 1 hit
PfamiView protein in Pfam
PF02063 MARCKS, 2 hits
PRINTSiPR00963 MARCKS
PROSITEiView protein in PROSITE
PS00826 MARCKS_1, 1 hit
PS00827 MARCKS_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMRP_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P28667
Secondary accession number(s): Q3TEZ4, Q91W07
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: October 16, 2019
This is version 150 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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