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Protein

Desmin

Gene

DES

Organism
Homo sapiens (Human)
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 (PubMed:25358400). 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:24200904, PubMed:25394388, PubMed:26724190). May act as a sarcomeric microtubule-anchoring protein: specifically associates with detyrosinated tubulin-alpha chains, leading to buckled microtubules and mechanical resistance to contraction. 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 (By similarity).1 PublicationBy similarity3 Publications

<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

  • cytoskeletal protein binding Source: BHF-UCL
  • identical protein binding Source: IntAct
  • structural constituent of cytoskeleton Source: ProtInc

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

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Reactomei
R-HSA-390522 Striated Muscle Contraction

SIGNOR Signaling Network Open Resource

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SIGNORi
P17661

<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <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 2

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000175084.11

Human Gene Nomenclature Database

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HGNCi
HGNC:2770 DES

Online Mendelian Inheritance in Man (OMIM)

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MIMi
125660 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P17661

<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; 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 provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Myopathy, myofibrillar, 1 (MFM1)28 Publications
The disease is caused by mutations affecting the gene represented in this entry. Mutations in the DES gene are associated with a variable clinical phenotype which encompasses isolated myopathies, pure cardiac phenotypes (including dilated cardiomyopathy, restrictive cardiomyopathy and arrhythmogenic right ventricular cardiomyopathy), cardiac conduction disease, and combinations of these disorders. If both cardiologic and neurologic features occur, they can manifest in any order, as cardiologic features can precede, occur simultaneously with, or follow manifestation of generalized neuromuscular disease (PubMed:19879535).1 Publication
Disease descriptionA form of myofibrillar myopathy, a group of chronic neuromuscular disorders characterized at ultrastructural level by disintegration of the sarcomeric Z disk and myofibrils, and replacement of the normal myofibrillar markings by small dense granules, or larger hyaline masses, or amorphous material. MFM1 is characterized by skeletal muscle weakness associated with cardiac conduction blocks, arrhythmias, restrictive heart failure, and accumulation of desmin-reactive deposits in cardiac and skeletal muscle cells.
See also OMIM:601419
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_0424482S → I in MFM1. 1 PublicationCorresponds to variant dbSNP:rs58999456EnsemblClinVar.1
Natural variantiVAR_0672077S → F in MFM1. 1 PublicationCorresponds to variant dbSNP:rs903985237Ensembl.1
Natural variantiVAR_06720813S → F in MFM1; some patients manifest a severe cardiac phenotype with right ventricular predominance. 2 PublicationsCorresponds to variant dbSNP:rs62636495EnsemblClinVar.1
Natural variantiVAR_07904816R → C in MFM1. 1 PublicationCorresponds to variant dbSNP:rs60798368EnsemblClinVar.1
Natural variantiVAR_04244946S → F in MFM1; exhibits significantly delayed filament assembly kinetics when bound to NEB; enhanced binding affinity towards NEB. 2 PublicationsCorresponds to variant dbSNP:rs60794845EnsemblClinVar.1
Natural variantiVAR_04245046S → Y in MFM1. 1 PublicationCorresponds to variant dbSNP:rs60794845EnsemblClinVar.1
Natural variantiVAR_069191116N → S in MFM1; the clinical picture is dominated by arrhythmogenic right ventricular cardiomyopathy and terminal heart failure; results in impaired filaments formation. 1 PublicationCorresponds to variant dbSNP:rs267607499EnsemblClinVar.1
Natural variantiVAR_009188173 – 179Missing in MFM1; severe form. 1 Publication7
Natural variantiVAR_070101240Missing in MFM1; the mutant cannot form de novo desmin intermediate filaments causing disruption of the endogenous intermediate filament network and formation of pathologic aggregates. 1 Publication1
Natural variantiVAR_042452245E → D in MFM1; exhibits significantly delayed filament assembly kinetics when bound to NEB and NEBL; enhanced binding affinity towards NEB and NEBL. 1 PublicationCorresponds to variant dbSNP:rs267607486EnsemblClinVar.1
Natural variantiVAR_007900337A → P in MFM1; mild adult-onset; unable to form a functional filamentous network. 2 PublicationsCorresponds to variant dbSNP:rs59962885EnsemblClinVar.1
Natural variantiVAR_067209338L → R in MFM1; results in the formation of a filamentous network disrupted by multiple breaks and clumps or large aggregates. 1 PublicationCorresponds to variant dbSNP:rs57496341EnsemblClinVar.1
Natural variantiVAR_042453342N → D in MFM1; unable to form a filamentous network; abolishes binding to MTM1. 3 PublicationsCorresponds to variant dbSNP:rs267607482EnsemblClinVar.1
Natural variantiVAR_009189345L → P in MFM1; distal onset; incapable of forming filamentous networks. 1 PublicationCorresponds to variant dbSNP:rs57639980EnsemblClinVar.1
Natural variantiVAR_042454350R → P in Kaeser syndrome and MFM1; incapable of de novo formation of a desmin intermediate filaments network; exerts a dominant negative effect on the ordered lateral arrangement of desmin subunits; may produce structural changes; forms subsarcolemmal aggregates. 3 PublicationsCorresponds to variant dbSNP:rs57965306EnsemblClinVar.1
Natural variantiVAR_042455355R → P in MFM1. 1 PublicationCorresponds to variant dbSNP:rs61368398EnsemblClinVar.1
Natural variantiVAR_042456357A → P in MFM1; unable to polymerize and form an intracellular filamentous network; abolishes binding to MTM1. 3 PublicationsCorresponds to variant dbSNP:rs58898021EnsemblClinVar.1
Natural variantiVAR_018769359 – 361Missing in MFM1. 1 Publication3
Natural variantiVAR_007901360A → P in MFM1; heterozygous with I-393 gives a severe childhood-onset; unable to form a functional filamentous network in the presence of I-393; abolishes binding to MTM1. 4 PublicationsCorresponds to variant dbSNP:rs121913000EnsemblClinVar.1
Natural variantiVAR_018770366Missing in MFM1. 1 Publication1
Natural variantiVAR_042457370L → P in MFM1; unable to polymerize and form an intracellular filamentous network; does not affect binding to MTM1. 3 PublicationsCorresponds to variant dbSNP:rs59308628EnsemblClinVar.1
Natural variantiVAR_018771385L → P in MFM1. 1 PublicationCorresponds to variant dbSNP:rs57955682EnsemblClinVar.1
Natural variantiVAR_018772389Q → P in MFM1. 1 PublicationCorresponds to variant dbSNP:rs121913004EnsemblClinVar.1
Natural variantiVAR_007902393N → I in MFM1; heterozygous with P-360 gives a severe childhood-onset; filamentous network is not affected however several spots indicate focal disorganization. 3 PublicationsCorresponds to variant dbSNP:rs121913001EnsemblClinVar.1
Natural variantiVAR_067210399D → Y in MFM1; results in the formation of a filamentous network disrupted by multiple breaks and clumps or large aggregates. 1 PublicationCorresponds to variant dbSNP:rs61130669EnsemblClinVar.1
Natural variantiVAR_067211401E → K in MFM1; results in the formation of a filamentous network disrupted by multiple breaks and clumps or large aggregates. 1 PublicationCorresponds to variant dbSNP:rs57694264EnsemblClinVar.1
Natural variantiVAR_042458406R → W in MFM1; unable to form a filamentous network. 3 PublicationsCorresponds to variant dbSNP:rs121913003EnsemblClinVar.1
Natural variantiVAR_069074419P → S in MFM1; found in a family with myofibrillar myopathy and arrhythmogenic right ventricular cardiomyopathy. 1 PublicationCorresponds to variant dbSNP:rs62635763EnsemblClinVar.1
Natural variantiVAR_042459442T → I in MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions. 1 PublicationCorresponds to variant dbSNP:rs121913005EnsemblClinVar.1
Natural variantiVAR_042460449K → M in MFM1. 1
Natural variantiVAR_042461449K → T in MFM1. 1 PublicationCorresponds to variant dbSNP:rs267607485EnsemblClinVar.1
Natural variantiVAR_018773451I → M in CMD1I and MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions; reduced interaction with CRYAB. 4 PublicationsCorresponds to variant dbSNP:rs121913002EnsemblClinVar.1
Natural variantiVAR_079049453T → I in MFM1; exhibits significantly delayed filament assembly kinetics when bound to NEB and NEBL; enhanced binding affinity towards NEB and NEBL. 2 PublicationsCorresponds to variant dbSNP:rs267607488EnsemblClinVar.1
Natural variantiVAR_042462454R → W in MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions; increased interaction with CRYAB. 3 PublicationsCorresponds to variant dbSNP:rs267607490EnsemblClinVar.1
Natural variantiVAR_042463460S → I in MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions. 1 PublicationCorresponds to variant dbSNP:rs267607491EnsemblClinVar.1
Cardiomyopathy, dilated 1I (CMD1I)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.
See also OMIM:604765
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_075228120A → D in CMD1I; results in impaired filaments formation, does not localize at intercalated disks. 1 Publication1
Natural variantiVAR_075229136L → P in CMD1I; results in impaired filaments formation, does not localize at intercalated disks. 1 PublicationCorresponds to variant dbSNP:rs397516695EnsemblClinVar.1
Natural variantiVAR_018773451I → M in CMD1I and MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions; reduced interaction with CRYAB. 4 PublicationsCorresponds to variant dbSNP:rs121913002EnsemblClinVar.1
Neurogenic scapuloperoneal syndrome Kaeser type (Kaeser syndrome)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAutosomal dominant disorder with a peculiar scapuloperoneal distribution of weakness and atrophy. A large clinical variability is observed ranging from scapuloperoneal, limb grindle and distal phenotypes with variable cardiac or respiratory involvement. Facial weakness, dysphagia and gynaecomastia are frequent additional symptoms. Affected men seemingly bear a higher risk of sudden, cardiac death as compared to affected women. Histological and immunohistochemical examination of muscle biopsy specimens reveal a wide spectrum of findings ranging from near normal or unspecific pathology to typical, myofibrillar changes with accumulation of desmin.
See also OMIM:181400
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_042454350R → P in Kaeser syndrome and MFM1; incapable of de novo formation of a desmin intermediate filaments network; exerts a dominant negative effect on the ordered lateral arrangement of desmin subunits; may produce structural changes; forms subsarcolemmal aggregates. 3 PublicationsCorresponds to variant dbSNP:rs57965306EnsemblClinVar.1

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>Mutagenesisi120A → E or R: Results in impaired filaments formation. 1 Publication1
Mutagenesisi120A → K, L or V: Does not result in impaired filaments formation. 1 Publication1

Keywords - Diseasei

Cardiomyopathy, Desmin-related myopathy, Disease mutation, Limb-girdle muscular dystrophy, Myofibrillar myopathy

Organism-specific databases

DisGeNET

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DisGeNETi
1674

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
DES

MalaCards human disease database

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MalaCardsi
DES
MIMi181400 phenotype
601419 phenotype
604765 phenotype

Open Targets

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OpenTargetsi
ENSG00000175084

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
34517 Autosomal dominant limb-girdle muscular dystrophy type 1E
363543 Autosomal recessive limb-girdle muscular dystrophy type 2R
98909 Desminopathy
154 Familial isolated dilated cardiomyopathy
85146 Neurogenic scapuloperoneal syndrome, Kaeser type

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA27253

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
DES

Domain mapping of disease mutations (DMDM)

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DMDMi
6686280

<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_00000637711 – 470DesminAdd BLAST470

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 CDK1By similarity1
Modified residuei12Phosphoserine; by AURKB1 Publication1
Modified residuei16Omega-N-methylarginineBy similarity1
Modified residuei17Phosphothreonine; by AURKB and ROCK12 Publications1
Modified residuei28Phosphoserine; by CDK1Combined sources1
Modified residuei31PhosphoserineBy similarity1
Modified residuei32Phosphoserine; by CDK11 Publication1
Modified residuei37Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei37Omega-N-methylarginine; alternateBy similarity1
Modified residuei45PhosphoserineBy similarity1
Modified residuei58ADP-ribosylarginineBy similarity1
Modified residuei60Phosphoserine; by AURKB1 Publication1
Modified residuei68PhosphoserineBy similarity1
Modified residuei70Omega-N-methylarginineBy similarity1
Modified residuei76Phosphothreonine; by ROCK11 Publication1
Modified residuei77Phosphothreonine; by ROCK11 Publication1
Modified residuei81PhosphoserineBy similarity1
Modified residuei290PhosphoserineBy similarity1
Modified residuei358PhosphoserineBy similarity1
Modified residuei361PhosphoserineBy similarity1
Modified residuei424PhosphoserineBy similarity1

<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.By similarity

Keywords - PTMi

ADP-ribosylation, Methylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P17661

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P17661

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

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PaxDbi
P17661

PeptideAtlas

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PeptideAtlasi
P17661

PRoteomics IDEntifications database

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PRIDEi
P17661

ProteomicsDB human proteome resource

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ProteomicsDBi
53502

2D gel databases

REPRODUCTION-2DPAGE

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REPRODUCTION-2DPAGEi
IPI00465084
P17661

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

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SWISS-2DPAGEi
P17661

University College Dublin 2-DE Proteome Database

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UCD-2DPAGEi
P17661

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P17661

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

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PhosphoSitePlusi
P17661

SwissPalm database of S-palmitoylation events

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SwissPalmi
P17661

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000175084 Expressed in 222 organ(s), highest expression level in esophagogastric junction muscularis propria

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P17661 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P17661 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB000034
HPA018803

<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 (PubMed:21135508). Interacts with DST (By similarity). Interacts with MTM1 (PubMed:21135508). Interacts with EPPK1; interaction is dependent of higher-order structure of intermediate filament (PubMed:16923132). Interacts with CRYAB (PubMed:28470624). Interacts with NEB (via nebulin repeats 160-164) (PubMed:23615443). Interacts (via rod region) with NEBL (via nebulin repeats 1-5) (PubMed:27733623).By similarity5 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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
108038, 47 interactors

Protein interaction database and analysis system

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IntActi
P17661, 60 interactors

Molecular INTeraction database

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MINTi
P17661

STRING: functional protein association networks

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STRINGi
9606.ENSP00000363071

<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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P17661

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

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SMRi
P17661

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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>Domaini108 – 416IF 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 – 141Coil 1AAdd BLAST33
Regioni142 – 151Linker 110
Regioni152 – 252Coil 1BAdd BLAST101
Regioni253 – 268Linker 12Add BLAST16
Regioni268 – 415Interaction with NEB1 PublicationAdd BLAST148
Regioni269 – 287Coil 2AAdd BLAST19
Regioni288 – 295Linker 28
Regioni296 – 412Coil 2BAdd BLAST117
Regioni413 – 470TailAdd BLAST58
Regioni438 – 453Interaction with CRYAB1 PublicationAdd BLAST16

<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 HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG013015

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P17661

KEGG Orthology (KO)

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KOi
K07610

Identification of Orthologs from Complete Genome Data

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OMAi
NQRARVE

Database of Orthologous Groups

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OrthoDBi
614199at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P17661

TreeFam database of animal gene trees

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TreeFami
TF330122

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR027698 DES
IPR001664 IF
IPR018039 IF_conserved
IPR039008 IF_rod_dom
IPR006821 Intermed_filament_DNA-bd

The PANTHER Classification System

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PANTHERi
PTHR23239 PTHR23239, 1 hit
PTHR23239:SF28 PTHR23239:SF28, 1 hit

Pfam protein domain database

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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>.<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.

P17661-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSQAYSSSQR VSSYRRTFGG APGFPLGSPL SSPVFPRAGF GSKGSSSSVT
60 70 80 90 100
SRVYQVSRTS GGAGGLGSLR ASRLGTTRTP SSYGAGELLD FSLADAVNQE
110 120 130 140 150
FLTTRTNEKV ELQELNDRFA NYIEKVRFLE QQNAALAAEV NRLKGREPTR
160 170 180 190 200
VAELYEEELR ELRRQVEVLT NQRARVDVER DNLLDDLQRL KAKLQEEIQL
210 220 230 240 250
KEEAENNLAA FRADVDAATL ARIDLERRIE SLNEEIAFLK KVHEEEIREL
260 270 280 290 300
QAQLQEQQVQ VEMDMSKPDL TAALRDIRAQ YETIAAKNIS EAEEWYKSKV
310 320 330 340 350
SDLTQAANKN NDALRQAKQE MMEYRHQIQS YTCEIDALKG TNDSLMRQMR
360 370 380 390 400
ELEDRFASEA SGYQDNIARL EEEIRHLKDE MARHLREYQD LLNVKMALDV
410 420 430 440 450
EIATYRKLLE GEESRINLPI QTYSALNFRE TSPEQRGSEV HTKKTVMIKT
460 470
IETRDGEVVS EATQQQHEVL
Length:470
Mass (Da):53,536
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:i1B5D9EA93C3BB319
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 conflicti23 – 25GFP → VFS (PubMed:2673923).Curated3
Sequence conflicti23 – 25GFP → VFS in AAA99221 (PubMed:2007603).Curated3
Sequence conflicti39G → P (PubMed:2673923).Curated1
Sequence conflicti39G → P in AAA99221 (PubMed:2007603).Curated1
Sequence conflicti119 – 123FANYI → SPIYM (PubMed:2673923).Curated5
Sequence conflicti119 – 123FANYI → SPIYM in AAA99221 (PubMed:2007603).Curated5
Sequence conflicti134Missing (PubMed:2673923).Curated1
Sequence conflicti134Missing in AAA99221 (PubMed:2007603).Curated1
Sequence conflicti134Missing in AAC50680 (PubMed:8792816).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0424482S → I in MFM1. 1 PublicationCorresponds to variant dbSNP:rs58999456EnsemblClinVar.1
Natural variantiVAR_0672077S → F in MFM1. 1 PublicationCorresponds to variant dbSNP:rs903985237Ensembl.1
Natural variantiVAR_06720813S → F in MFM1; some patients manifest a severe cardiac phenotype with right ventricular predominance. 2 PublicationsCorresponds to variant dbSNP:rs62636495EnsemblClinVar.1
Natural variantiVAR_07904816R → C in MFM1. 1 PublicationCorresponds to variant dbSNP:rs60798368EnsemblClinVar.1
Natural variantiVAR_04244946S → F in MFM1; exhibits significantly delayed filament assembly kinetics when bound to NEB; enhanced binding affinity towards NEB. 2 PublicationsCorresponds to variant dbSNP:rs60794845EnsemblClinVar.1
Natural variantiVAR_04245046S → Y in MFM1. 1 PublicationCorresponds to variant dbSNP:rs60794845EnsemblClinVar.1
Natural variantiVAR_069191116N → S in MFM1; the clinical picture is dominated by arrhythmogenic right ventricular cardiomyopathy and terminal heart failure; results in impaired filaments formation. 1 PublicationCorresponds to variant dbSNP:rs267607499EnsemblClinVar.1
Natural variantiVAR_075228120A → D in CMD1I; results in impaired filaments formation, does not localize at intercalated disks. 1 Publication1
Natural variantiVAR_075229136L → P in CMD1I; results in impaired filaments formation, does not localize at intercalated disks. 1 PublicationCorresponds to variant dbSNP:rs397516695EnsemblClinVar.1
Natural variantiVAR_009188173 – 179Missing in MFM1; severe form. 1 Publication7
Natural variantiVAR_042451213A → V Rare polymorphism; may play a role in cardiomyopathies and distal myopathies if combined with other DES mutations or mutations in other genes; does not affect the formation of a normal complete filamentous network. 4 PublicationsCorresponds to variant dbSNP:rs41272699EnsemblClinVar.1
Natural variantiVAR_070101240Missing in MFM1; the mutant cannot form de novo desmin intermediate filaments causing disruption of the endogenous intermediate filament network and formation of pathologic aggregates. 1 Publication1
Natural variantiVAR_069192241K → E Found in a patient with severe arrhythmogenic right ventricular cardiomyopathy also carrying a pathogenic frameshift mutation in PKP2. 1 PublicationCorresponds to variant dbSNP:rs201945924Ensembl.1
Natural variantiVAR_042452245E → D in MFM1; exhibits significantly delayed filament assembly kinetics when bound to NEB and NEBL; enhanced binding affinity towards NEB and NEBL. 1 PublicationCorresponds to variant dbSNP:rs267607486EnsemblClinVar.1
Natural variantiVAR_075230326H → R Rare polymorphism; does not result in impaired filaments formation. 1 Publication1
Natural variantiVAR_007900337A → P in MFM1; mild adult-onset; unable to form a functional filamentous network. 2 PublicationsCorresponds to variant dbSNP:rs59962885EnsemblClinVar.1
Natural variantiVAR_067209338L → R in MFM1; results in the formation of a filamentous network disrupted by multiple breaks and clumps or large aggregates. 1 PublicationCorresponds to variant dbSNP:rs57496341EnsemblClinVar.1
Natural variantiVAR_042453342N → D in MFM1; unable to form a filamentous network; abolishes binding to MTM1. 3 PublicationsCorresponds to variant dbSNP:rs267607482EnsemblClinVar.1
Natural variantiVAR_009189345L → P in MFM1; distal onset; incapable of forming filamentous networks. 1 PublicationCorresponds to variant dbSNP:rs57639980EnsemblClinVar.1
Natural variantiVAR_042454350R → P in Kaeser syndrome and MFM1; incapable of de novo formation of a desmin intermediate filaments network; exerts a dominant negative effect on the ordered lateral arrangement of desmin subunits; may produce structural changes; forms subsarcolemmal aggregates. 3 PublicationsCorresponds to variant dbSNP:rs57965306EnsemblClinVar.1
Natural variantiVAR_042455355R → P in MFM1. 1 PublicationCorresponds to variant dbSNP:rs61368398EnsemblClinVar.1
Natural variantiVAR_042456357A → P in MFM1; unable to polymerize and form an intracellular filamentous network; abolishes binding to MTM1. 3 PublicationsCorresponds to variant dbSNP:rs58898021EnsemblClinVar.1
Natural variantiVAR_018769359 – 361Missing in MFM1. 1 Publication3
Natural variantiVAR_007901360A → P in MFM1; heterozygous with I-393 gives a severe childhood-onset; unable to form a functional filamentous network in the presence of I-393; abolishes binding to MTM1. 4 PublicationsCorresponds to variant dbSNP:rs121913000EnsemblClinVar.1
Natural variantiVAR_018770366Missing in MFM1. 1 Publication1
Natural variantiVAR_042457370L → P in MFM1; unable to polymerize and form an intracellular filamentous network; does not affect binding to MTM1. 3 PublicationsCorresponds to variant dbSNP:rs59308628EnsemblClinVar.1
Natural variantiVAR_018771385L → P in MFM1. 1 PublicationCorresponds to variant dbSNP:rs57955682EnsemblClinVar.1
Natural variantiVAR_018772389Q → P in MFM1. 1 PublicationCorresponds to variant dbSNP:rs121913004EnsemblClinVar.1
Natural variantiVAR_007902393N → I in MFM1; heterozygous with P-360 gives a severe childhood-onset; filamentous network is not affected however several spots indicate focal disorganization. 3 PublicationsCorresponds to variant dbSNP:rs121913001EnsemblClinVar.1
Natural variantiVAR_067210399D → Y in MFM1; results in the formation of a filamentous network disrupted by multiple breaks and clumps or large aggregates. 1 PublicationCorresponds to variant dbSNP:rs61130669EnsemblClinVar.1
Natural variantiVAR_067211401E → K in MFM1; results in the formation of a filamentous network disrupted by multiple breaks and clumps or large aggregates. 1 PublicationCorresponds to variant dbSNP:rs57694264EnsemblClinVar.1
Natural variantiVAR_042458406R → W in MFM1; unable to form a filamentous network. 3 PublicationsCorresponds to variant dbSNP:rs121913003EnsemblClinVar.1
Natural variantiVAR_069074419P → S in MFM1; found in a family with myofibrillar myopathy and arrhythmogenic right ventricular cardiomyopathy. 1 PublicationCorresponds to variant dbSNP:rs62635763EnsemblClinVar.1
Natural variantiVAR_042459442T → I in MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions. 1 PublicationCorresponds to variant dbSNP:rs121913005EnsemblClinVar.1
Natural variantiVAR_042460449K → M in MFM1. 1
Natural variantiVAR_042461449K → T in MFM1. 1 PublicationCorresponds to variant dbSNP:rs267607485EnsemblClinVar.1
Natural variantiVAR_018773451I → M in CMD1I and MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions; reduced interaction with CRYAB. 4 PublicationsCorresponds to variant dbSNP:rs121913002EnsemblClinVar.1
Natural variantiVAR_079049453T → I in MFM1; exhibits significantly delayed filament assembly kinetics when bound to NEB and NEBL; enhanced binding affinity towards NEB and NEBL. 2 PublicationsCorresponds to variant dbSNP:rs267607488EnsemblClinVar.1
Natural variantiVAR_042462454R → W in MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions; increased interaction with CRYAB. 3 PublicationsCorresponds to variant dbSNP:rs267607490EnsemblClinVar.1
Natural variantiVAR_042463460S → I in MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions. 1 PublicationCorresponds to variant dbSNP:rs267607491EnsemblClinVar.1

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
M63391 Genomic DNA Translation: AAA99221.1
U59167 mRNA Translation: AAC50680.1
AF055081 mRNA Translation: AAC39938.1
AF055082 mRNA Translation: AAC39939.1
AF055083 mRNA Translation: AAC39940.1
AF137053 mRNA Translation: AAF15400.1
AF486807 mRNA Translation: AAL93205.1
AF487828 mRNA Translation: AAL99078.1
AF521879 mRNA Translation: AAN15036.1
AF527578 mRNA Translation: AAN37810.1
AY083345 mRNA Translation: AAL99215.1
AY114212 Genomic DNA Translation: AAM47026.1
AY125465 mRNA Translation: AAM95238.1
BC032116 mRNA Translation: AAH32116.1
AJ132926 mRNA Translation: CAB62389.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS33383.1

Protein sequence database of the Protein Information Resource

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PIRi
JE0063 DMHU

NCBI Reference Sequences

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RefSeqi
NP_001918.3, NM_001927.3

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.594952

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000373960; ENSP00000363071; ENSG00000175084

Database of genes from NCBI RefSeq genomes

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GeneIDi
1674

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:1674

Keywords - Coding sequence diversityi

Polymorphism

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Human Intermediate Filament Mutation Database
Wikipedia

Desmin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63391 Genomic DNA Translation: AAA99221.1
U59167 mRNA Translation: AAC50680.1
AF055081 mRNA Translation: AAC39938.1
AF055082 mRNA Translation: AAC39939.1
AF055083 mRNA Translation: AAC39940.1
AF137053 mRNA Translation: AAF15400.1
AF486807 mRNA Translation: AAL93205.1
AF487828 mRNA Translation: AAL99078.1
AF521879 mRNA Translation: AAN15036.1
AF527578 mRNA Translation: AAN37810.1
AY083345 mRNA Translation: AAL99215.1
AY114212 Genomic DNA Translation: AAM47026.1
AY125465 mRNA Translation: AAM95238.1
BC032116 mRNA Translation: AAH32116.1
AJ132926 mRNA Translation: CAB62389.1
CCDSiCCDS33383.1
PIRiJE0063 DMHU
RefSeqiNP_001918.3, NM_001927.3
UniGeneiHs.594952

3D structure databases

ProteinModelPortaliP17661
SMRiP17661
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108038, 47 interactors
IntActiP17661, 60 interactors
MINTiP17661
STRINGi9606.ENSP00000363071

PTM databases

iPTMnetiP17661
PhosphoSitePlusiP17661
SwissPalmiP17661

Polymorphism and mutation databases

BioMutaiDES
DMDMi6686280

2D gel databases

REPRODUCTION-2DPAGEiIPI00465084
P17661
SWISS-2DPAGEiP17661
UCD-2DPAGEiP17661

Proteomic databases

EPDiP17661
jPOSTiP17661
PaxDbiP17661
PeptideAtlasiP17661
PRIDEiP17661
ProteomicsDBi53502

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
1674
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000373960; ENSP00000363071; ENSG00000175084
GeneIDi1674
KEGGihsa:1674

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1674
DisGeNETi1674
EuPathDBiHostDB:ENSG00000175084.11

GeneCards: human genes, protein and diseases

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GeneCardsi
DES
GeneReviewsiDES
HGNCiHGNC:2770 DES
HPAiCAB000034
HPA018803
MalaCardsiDES
MIMi125660 gene
181400 phenotype
601419 phenotype
604765 phenotype
neXtProtiNX_P17661
OpenTargetsiENSG00000175084
Orphaneti34517 Autosomal dominant limb-girdle muscular dystrophy type 1E
363543 Autosomal recessive limb-girdle muscular dystrophy type 2R
98909 Desminopathy
154 Familial isolated dilated cardiomyopathy
85146 Neurogenic scapuloperoneal syndrome, Kaeser type
PharmGKBiPA27253

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IFZ1 Eukaryota
ENOG410XRBS LUCA
GeneTreeiENSGT00940000155522
HOVERGENiHBG013015
InParanoidiP17661
KOiK07610
OMAiNQRARVE
OrthoDBi614199at2759
PhylomeDBiP17661
TreeFamiTF330122

Enzyme and pathway databases

ReactomeiR-HSA-390522 Striated Muscle Contraction
SIGNORiP17661

Miscellaneous databases

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

More...
ChiTaRSi
DES human

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
Desmin

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
1674

Protein Ontology

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PROi
PR:P17661

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000175084 Expressed in 222 organ(s), highest expression level in esophagogastric junction muscularis propria
ExpressionAtlasiP17661 baseline and differential
GenevisibleiP17661 HS

Family and domain databases

InterProiView protein in InterPro
IPR027698 DES
IPR001664 IF
IPR018039 IF_conserved
IPR039008 IF_rod_dom
IPR006821 Intermed_filament_DNA-bd
PANTHERiPTHR23239 PTHR23239, 1 hit
PTHR23239:SF28 PTHR23239:SF28, 1 hit
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

More...
ProtoNeti
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 nameiDESM_HUMAN
<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: P17661
Secondary accession number(s): Q15787
, Q549R7, Q549R8, Q549R9, Q8IZR1, Q8IZR6, Q8NES2, Q8NEU6, Q8TAC4, Q8TCX2, Q8TD99, Q9UHN5, Q9UJ80
<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: August 1, 1990
Last sequence update: January 23, 2007
Last modified: January 16, 2019
This is version 202 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
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.

<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. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
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