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Entry version 176 (11 Dec 2019)
Sequence version 3 (23 Jan 2007)
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Protein

Desmin

Gene

Des

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

Muscle-specific type III intermediate filament essential for proper muscular structure and function. Plays a crucial role in maintaining the structure of sarcomeres, inter-connecting the Z-disks and forming the myofibrils, linking them not only to the sarcolemmal cytoskeleton, but also to the nucleus and mitochondria, thus providing strength for the muscle fiber during activity (By similarity). In adult striated muscle they form a fibrous network connecting myofibrils to each other and to the plasma membrane from the periphery of the Z-line structures (PubMed:25394388). May act as a sarcomeric microtubule-anchoring protein: specifically associates with detyrosinated tubulin-alpha chains, leading to buckled microtubules and mechanical resistance to contraction (PubMed:27102488). Contributes to the transcriptional regulation of the NKX2-5 gene in cardiac progenitor cells during a short period of cardiomyogenesis and in cardiac side population stem cells in the adult. Plays a role in maintaining an optimal conformation of nebulette (NEB) on heart muscle sarcomeres to bind and recruit cardiac alpha-actin (PubMed:27733623).By similarity3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei353Stutter1

<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 functionMuscle protein

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-390522 Striated Muscle Contraction

<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:
Desmin
<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:Des
<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 1

Organism-specific databases

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

More...
MGIi
MGI:94885 Des

<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, Intermediate filament, Membrane, Nucleus

<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

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Mice hearts have reduced nebulette (NEB) and elevated actin levels, with intact myofibers showing disordered NEB organization.1 Publication

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>Mutagenesisi7S → A: Reduced phosphorylation. Almost complete loss of phosphorylation; when associated with A-28 and A-32. 1 Publication1
Mutagenesisi28S → A: Reduced phosphorylation. Almost complete loss of phosphorylation; when associated with A-7 and A-32. 1 Publication1
Mutagenesisi32S → A: Reduced phosphorylation and formation of unusual long bridge-like intermediate filament structures between two daughter cells during cytokinesis. Almost complete loss of phosphorylation; when associated with A-7 and A-28. Increased formation of unusual long bridge-like intermediate filament structures between two daughter cells during cytokinesis; when associated with A-60 and A-76. 1 Publication1
Mutagenesisi60S → A: Formation of unusual long bridge-like intermediate filament structures between two daughter cells during cytokinesis; when associated with A-76. Increased formation of unusual long bridge-like intermediate filament structures between two daughter cells during cytokinesis; when associated with A-32 and A-76. 1 Publication1
Mutagenesisi76T → A: Formation of unusual long bridge-like intermediate filament structures between two daughter cells during cytokinesis; when associated with A-60. Increased formation of unusual long bridge-like intermediate filament structures between two daughter cells during cytokinesis; when associated with A-32 and A-60. 1 Publication1
Mutagenesisi349R → P: Increases protein decay. forms subsarcolemmal aggregates. Changes the subcellular localization and turnover of its direct, extrasarcomeric binding partners. Knockin mice develop age-dependent desmin-positive protein aggregation pathology, skeletal muscle weakness, dilated cardiomyopathy, as well as cardiac arrhythmias and conduction defects. Knockin mice exhibit altered axial myofibrillar lattice arrangement in fast- and slow-twitch muscle fibers, increased axial stiffness and stretch-induced vulnerability in soleus muscle fiber bundles, reduced Ca(2+)-sensitivity in heterozygous fiber bundles and increased Ca(2+)-sensitivity in homozygous fiber bundles. 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 ‘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_00000637731 – 469DesminAdd BLAST469

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei7Phosphoserine; by CDK11 Publication1
Modified residuei12Phosphoserine; by AURKBBy similarity1
Modified residuei16Omega-N-methylarginineCombined sources1
Modified residuei17Phosphothreonine; by AURKB and ROCK1Combined sources1
Modified residuei25PhosphoserineCombined sources1
Modified residuei28Phosphoserine; by CDK1Combined sources1 Publication1
Modified residuei31PhosphoserineCombined sources1
Modified residuei32Phosphoserine; by CDK1Combined sources1 Publication1
Modified residuei37Asymmetric dimethylarginine; alternateCombined sources1
Modified residuei37Omega-N-methylarginine; alternateCombined sources1
Modified residuei45PhosphoserineBy similarity1
Modified residuei58ADP-ribosylarginineBy similarity1
Modified residuei60Phosphoserine; by AURKB1 Publication1
Modified residuei68PhosphoserineCombined sources1
Modified residuei70Omega-N-methylarginineCombined sources1
Modified residuei76Phosphothreonine; by ROCK11 Publication1
Modified residuei77Phosphothreonine; by ROCK1By similarity1
Modified residuei81PhosphoserineBy similarity1
Modified residuei289PhosphoserineBy similarity1
Modified residuei357PhosphoserineBy similarity1
Modified residuei423PhosphoserineCombined 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

ADP-ribosylation prevents ability to form intermediate filaments.By similarity
Phosphorylation at Ser-7, Ser-28 and Ser-32 by CDK1, phosphorylation at Ser-60 by AURKB and phosphorylation at Thr-76 by ROCK1 contribute to efficient separation of desmin intermediate filaments during mitosis.1 Publication

Keywords - PTMi

ADP-ribosylation, Methylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P31001

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P31001

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

More...
PaxDbi
P31001

PeptideAtlas

More...
PeptideAtlasi
P31001

PRoteomics IDEntifications database

More...
PRIDEi
P31001

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...
SWISS-2DPAGEi
P31001

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P31001

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

More...
PhosphoSitePlusi
P31001

<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

Cardiac progenitor cells and immature cardiomyocytes (at protein level).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000026208 Expressed in 173 organ(s), highest expression level in skeletal muscle tissue

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P31001 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P31001 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

Homopolymer.

Interacts with MTM1 (By similarity).

Interacts with DST (PubMed:10357897).

Interacts with tubulin-alpha; specifically associates with detyrosinated tubulin-alpha (PubMed:27102488).

Interacts with EPPK1; interaction is dependent of higher-order structure of intermediate filament.

Interacts with CRYAB.

Interacts with NEB (via nebulin repeats 160-164).

Interacts (via rod region) with NEBL (via nebulin repeats 1-5) (By similarity).

By similarity2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
199210, 5 interactors

Database of interacting proteins

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DIPi
DIP-256N

Protein interaction database and analysis system

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IntActi
P31001, 15 interactors

Molecular INTeraction database

More...
MINTi
P31001

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000027409

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P31001 protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P31001

Database of comparative protein structure models

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ModBasei
Search...

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini107 – 415IF rodPROSITE-ProRule annotationAdd BLAST309

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>Regioni1 – 108HeadAdd BLAST108
Regioni109 – 140Coil 1AAdd BLAST32
Regioni141 – 150Linker 110
Regioni151 – 251Coil 1BAdd BLAST101
Regioni252 – 267Linker 12Add BLAST16
Regioni267 – 414Interaction with NEBBy similarityAdd BLAST148
Regioni268 – 286Coil 2AAdd BLAST19
Regioni287 – 294Linker 28
Regioni295 – 411Coil 2BAdd BLAST117
Regioni412 – 469TailAdd BLAST58
Regioni437 – 452Interaction with CRYABBy similarityAdd BLAST16

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi45 – 48Poly-Ser4

<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 intermediate filament family.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410IFZ1 Eukaryota
ENOG410XRBS LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000155522

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000230977

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P31001

KEGG Orthology (KO)

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KOi
K07610

Identification of Orthologs from Complete Genome Data

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OMAi
VEMDISK

Database of Orthologous Groups

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OrthoDBi
655109at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P31001

TreeFam database of animal gene trees

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TreeFami
TF330122

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.20.5.1160, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR018039 IF_conserved
IPR039008 IF_rod_dom
IPR042180 IF_rod_dom_coil1B
IPR006821 Intermed_filament_DNA-bd

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00038 Filament, 1 hit
PF04732 Filament_head, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM01391 Filament, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00226 IF_ROD_1, 1 hit
PS51842 IF_ROD_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.

P31001-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSQAYSSSQR VSSYRRTFGG APGFSLGSPL SSPVFPRAGF GTKGSSSSMT
60 70 80 90 100
SRVYQVSRTS GGAGGLGSLR SSRLGTTRAP SYGAGELLDF SLADAVNQEF
110 120 130 140 150
LATRTNEKVE LQELNDRFAN YIEKVRFLEQ QNAALAAEVN RLKGREPTRV
160 170 180 190 200
AELYEEEMRE LRRQVEVLTN QRARVDVERD NLIDDLQRLK AKLQEEIQLR
210 220 230 240 250
EEAENNLAAF RADVDAATLA RIDLERRIES LNEEIAFLKK VHEEEIRELQ
260 270 280 290 300
AQLQEQQVQV EMDMSKPDLT AALRDIRAQY ETIAAKNISE AEEWYKSKVS
310 320 330 340 350
DLTQAANKNN DALRQAKQEM MEYRHQIQSY TCEIDALKGT NDSLMRQMRE
360 370 380 390 400
LEDRFASEAN GYQDNIARLE EEIRHLKDEM ARHLREYQDL LNVKMALDVE
410 420 430 440 450
IATYRKLLEG EESRINLPIQ TFSALNFRET SPEQRGSEVH TKKTVMIKTI
460
ETRDGEVVSE ATQQQHEVL
Length:469
Mass (Da):53,498
Last modified:January 23, 2007 - v3
<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:i58A8A13C7CC11EEF
GO

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

More...
DDBJi
Links Updated
L22550 mRNA No translation available.
BC031760 mRNA Translation: AAH31760.1
Z18892 Genomic DNA Translation: CAA79330.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS15071.1

Protein sequence database of the Protein Information Resource

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PIRi
A54104

NCBI Reference Sequences

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RefSeqi
NP_034173.1, NM_010043.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000027409; ENSMUSP00000027409; ENSMUSG00000026208

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
13346

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:13346

UCSC genome browser

More...
UCSCi
uc007box.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
L22550 mRNA No translation available.
BC031760 mRNA Translation: AAH31760.1
Z18892 Genomic DNA Translation: CAA79330.1
CCDSiCCDS15071.1
PIRiA54104
RefSeqiNP_034173.1, NM_010043.2

3D structure databases

SMRiP31001
ModBaseiSearch...

Protein-protein interaction databases

BioGridi199210, 5 interactors
DIPiDIP-256N
IntActiP31001, 15 interactors
MINTiP31001
STRINGi10090.ENSMUSP00000027409

PTM databases

iPTMnetiP31001
PhosphoSitePlusiP31001

2D gel databases

SWISS-2DPAGEiP31001

Proteomic databases

EPDiP31001
jPOSTiP31001
PaxDbiP31001
PeptideAtlasiP31001
PRIDEiP31001

Genome annotation databases

EnsembliENSMUST00000027409; ENSMUSP00000027409; ENSMUSG00000026208
GeneIDi13346
KEGGimmu:13346
UCSCiuc007box.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1674
MGIiMGI:94885 Des

Phylogenomic databases

eggNOGiENOG410IFZ1 Eukaryota
ENOG410XRBS LUCA
GeneTreeiENSGT00940000155522
HOGENOMiHOG000230977
InParanoidiP31001
KOiK07610
OMAiVEMDISK
OrthoDBi655109at2759
PhylomeDBiP31001
TreeFamiTF330122

Enzyme and pathway databases

ReactomeiR-MMU-390522 Striated Muscle Contraction

Miscellaneous databases

Protein Ontology

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PROi
PR:P31001
RNActiP31001 protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000026208 Expressed in 173 organ(s), highest expression level in skeletal muscle tissue
ExpressionAtlasiP31001 baseline and differential
GenevisibleiP31001 MM

Family and domain databases

Gene3Di1.20.5.1160, 1 hit
InterProiView protein in InterPro
IPR018039 IF_conserved
IPR039008 IF_rod_dom
IPR042180 IF_rod_dom_coil1B
IPR006821 Intermed_filament_DNA-bd
PfamiView protein in Pfam
PF00038 Filament, 1 hit
PF04732 Filament_head, 1 hit
SMARTiView protein in SMART
SM01391 Filament, 1 hit
PROSITEiView protein in PROSITE
PS00226 IF_ROD_1, 1 hit
PS51842 IF_ROD_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiDESM_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: P31001
<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: July 1, 1993
Last sequence update: January 23, 2007
Last modified: December 11, 2019
This is version 176 of the entry and version 3 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

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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