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UniProtKB - P17661 (DESM_HUMAN)

Entry version 213 (07 Oct 2020)
Sequence version 3 (23 Jan 2007)
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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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P17661

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-390522, Striated Muscle Contraction

SIGNOR Signaling Network Open Resource

More...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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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

More...EuPathDBi		HostDB:ENSG00000175084.11

Human Gene Nomenclature Database

More...HGNCi		HGNC:2770, DES

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		125660, gene

neXtProt; the human protein knowledge platform

More...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 & 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 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.
Related information in OMIM
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:rs903985237EnsemblClinVar.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.
Related information in OMIM
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.
Related information in OMIM
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%5Fand%5Fbiotech%5Fsection">'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

More...DisGeNETi		1674

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

More...GeneReviewsi		DES

MalaCards human disease database

More...MalaCardsi		DES
MIMi181400, phenotype
601419, phenotype
604765, phenotype

Open Targets

More...OpenTargetsi		ENSG00000175084

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

More...Orphaneti		98909, Desminopathy
154, Familial isolated dilated cardiomyopathy
85146, Neurogenic scapuloperoneal syndrome, Kaeser type

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA27253

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P17661, Tbio

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		DES

Domain mapping of disease mutations (DMDM)

More...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 or proteolytic cleavage.<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%5Fprocessing%5Fsection">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

More...EPDi		P17661

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P17661

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P17661

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

More...PaxDbi		P17661

PeptideAtlas

More...PeptideAtlasi		P17661

PRoteomics IDEntifications database

More...PRIDEi		P17661

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		53502

2D gel databases

REPRODUCTION-2DPAGE

More...REPRODUCTION-2DPAGEi		IPI00465084
P17661

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

More...SWISS-2DPAGEi		P17661

University College Dublin 2-DE Proteome Database

More...UCD-2DPAGEi		P17661

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P17661

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

More...PhosphoSitePlusi		P17661

SwissPalm database of S-palmitoylation events

More...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

More...Bgeei		ENSG00000175084, Expressed in esophagogastric junction muscularis propria and 232 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P17661, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P17661, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000175084, Tissue enhanced (heart muscle, skeletal muscle, smooth muscle)

<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%5Fsection">'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%5Fsection">'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%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details
P17661
With#Exp.IntAct
BAG5 [Q9UL15]3EBI-1055572,EBI-356517
C1orf216 [Q8TAB5]3EBI-1055572,EBI-747505
CT55 [Q8WUE5]6EBI-1055572,EBI-6873363
CWF19L2 [Q2TBE0]3EBI-1055572,EBI-5453285
DDX6 [P26196]3EBI-1055572,EBI-351257
itself7EBI-1055572,EBI-1055572
DUX1 [O43812]4EBI-1055572,EBI-11599346
DUX4 [Q9UBX2]3EBI-1055572,EBI-11600078
DUX4L9 [Q6RFH8]4EBI-1055572,EBI-11599882
DYSF [O75923]3EBI-1055572,EBI-2799016
EHHADH [Q08426]6EBI-1055572,EBI-2339219
GFAP [P14136]3EBI-1055572,EBI-744302
GOLGA6L9 [A6NEM1]3EBI-1055572,EBI-5916454
KRT13 [P13646]3EBI-1055572,EBI-1223876
KRT15 [P19012]3EBI-1055572,EBI-739566
KRT20 [P35900]3EBI-1055572,EBI-742094
KRT33B [Q14525]3EBI-1055572,EBI-1049638
KRT37 [O76014]3EBI-1055572,EBI-1045716
KRT75 [O95678]3EBI-1055572,EBI-2949715
LBX1 [P52954]3EBI-1055572,EBI-20141748
LENG1 [Q96BZ8]3EBI-1055572,EBI-726510
LMO4 [P61968]3EBI-1055572,EBI-2798728
LONRF3 [Q496Y0]3EBI-1055572,EBI-2690768
M1AP [Q8TC57]3EBI-1055572,EBI-748182
MLH1 [P40692]7EBI-1055572,EBI-744248
MTM1 [Q13496]13EBI-1055572,EBI-2864109
NEFL [P07196]7EBI-1055572,EBI-475646
NEK6 - isoform 4 [Q9HC98-4]3EBI-1055572,EBI-11750983
PIAS2 - isoform PIAS2-alpha [O75928-2]3EBI-1055572,EBI-348567
PIH1D2 [Q8WWB5]3EBI-1055572,EBI-10232538
POLR2G [P62487]3EBI-1055572,EBI-347928
PPL [O60437]3EBI-1055572,EBI-368321
PPP1R18 [Q6NYC8]6EBI-1055572,EBI-2557469
PRPH [P41219]3EBI-1055572,EBI-752074
RNF4 [P78317]3EBI-1055572,EBI-2340927
TCEA2 [Q15560]3EBI-1055572,EBI-710310
TFIP11 [Q9UBB9]3EBI-1055572,EBI-1105213
UBE2I [Q7KZS0]3EBI-1055572,EBI-10180829
VIM [P08670]6EBI-1055572,EBI-353844
YES1 [P07947]3EBI-1055572,EBI-515331
ZMYM5 - isoform 2 [Q9UJ78-2]3EBI-1055572,EBI-17634549

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		108038, 78 interactors

Protein interaction database and analysis system

More...IntActi		P17661, 60 interactors

Molecular INTeraction database

More...MINTi		P17661

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000363071

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P17661, 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

More...SMRi		P17661

Database of comparative protein structure models

More...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%5Fand%5Fdomains%5Fsection">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

More...eggNOGi		KOG0977, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000155522

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_012560_7_4_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P17661

KEGG Orthology (KO)

More...KOi		K07610

Identification of Orthologs from Complete Genome Data

More...OMAi		YSTISFR

Database of Orthologous Groups

More...OrthoDBi		655109at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P17661

TreeFam database of animal gene trees

More...TreeFami		TF330122

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...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

More...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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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:rs903985237EnsemblClinVar.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

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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

More...CCDSi		CCDS33383.1

Protein sequence database of the Protein Information Resource

More...PIRi		JE0063, DMHU

NCBI Reference Sequences

More...RefSeqi		NP_001918.3, NM_001927.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000373960; ENSP00000363071; ENSG00000175084

Database of genes from NCBI RefSeq genomes

More...GeneIDi		1674

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...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%5Freferences%5Fsection">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

3D structure databases

SMRiP17661
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi108038, 78 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
MassIVEiP17661
PaxDbiP17661
PeptideAtlasiP17661
PRIDEiP17661
ProteomicsDBi53502

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		3503, 1435 antibodies

The DNASU plasmid repository

More...DNASUi		1674

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

More...GeneCardsi		DES
GeneReviewsiDES
HGNCiHGNC:2770, DES
HPAiENSG00000175084, Tissue enhanced (heart muscle, skeletal muscle, smooth muscle)
MalaCardsiDES
MIMi125660, gene
181400, phenotype
601419, phenotype
604765, phenotype
neXtProtiNX_P17661
OpenTargetsiENSG00000175084
Orphaneti98909, Desminopathy
154, Familial isolated dilated cardiomyopathy
85146, Neurogenic scapuloperoneal syndrome, Kaeser type
PharmGKBiPA27253

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0977, Eukaryota
GeneTreeiENSGT00940000155522
HOGENOMiCLU_012560_7_4_1
InParanoidiP17661
KOiK07610
OMAiYSTISFR
OrthoDBi655109at2759
PhylomeDBiP17661
TreeFamiTF330122

Enzyme and pathway databases

PathwayCommonsiP17661
ReactomeiR-HSA-390522, Striated Muscle Contraction
SIGNORiP17661

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		1674, 6 hits in 877 CRISPR screens

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

More...GeneWikii		Desmin

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

More...GenomeRNAii		1674
PharosiP17661, Tbio

Protein Ontology

More...PROi		PR:P17661
RNActiP17661, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000175084, Expressed in esophagogastric junction muscularis propria and 232 other tissues
ExpressionAtlasiP17661, baseline and differential
GenevisibleiP17661, HS

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

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...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 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%5Fand%5Fisoforms">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: October 7, 2020
This is version 213 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

Reference proteome

Documents

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