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Protein

Desmin

Gene

DES

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Desmin are class-III intermediate filaments found in muscle cells. 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.By similarity3 Publications

GO - Molecular functioni

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

GO - Biological processi

  • cytoskeleton organization Source: ProtInc
  • intermediate filament organization Source: UniProtKB
  • muscle contraction Source: ProtInc
  • muscle filament sliding Source: Reactome
  • regulation of heart contraction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Enzyme and pathway databases

BioCyciZFISH:ENSG00000175084-MONOMER.
ReactomeiR-HSA-390522. Striated Muscle Contraction.
SIGNORiP17661.

Names & Taxonomyi

Protein namesi
Recommended name:
Desmin
Gene namesi
Name:DES
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:2770. DES.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • fascia adherens Source: Ensembl
  • intercalated disc Source: UniProtKB
  • intermediate filament Source: ProtInc
  • intermediate filament cytoskeleton Source: HPA
  • neuromuscular junction Source: Ensembl
  • sarcolemma Source: UniProtKB
  • Z disc Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Intermediate filament, Membrane

Pathology & Biotechi

Involvement in diseasei

Myopathy, myofibrillar, 1 (MFM1)21 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 disc 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
Natural variantiVAR_0424482S → I in MFM1. 1 PublicationCorresponds to variant rs58999456dbSNPEnsembl.1
Natural variantiVAR_0672077S → F in MFM1. 1 Publication1
Natural variantiVAR_06720813S → F in MFM1; some patients manifest a severe cardiac phenotype with right ventricular predominance. 2 PublicationsCorresponds to variant rs62636495dbSNPEnsembl.1
Natural variantiVAR_04244946S → F in MFM1. 1 PublicationCorresponds to variant rs60794845dbSNPEnsembl.1
Natural variantiVAR_04245046S → Y in MFM1. 1 PublicationCorresponds to variant rs60794845dbSNPEnsembl.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 rs267607499dbSNPEnsembl.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. Corresponds to variant rs267607486dbSNPEnsembl.1
Natural variantiVAR_007900337A → P in MFM1; mild adult-onset; unable to form a functional filamentous network. 2 PublicationsCorresponds to variant rs59962885dbSNPEnsembl.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 rs57496341dbSNPEnsembl.1
Natural variantiVAR_042453342N → D in MFM1; unable to form a filamentous network; abolishes binding to MTM1. 3 PublicationsCorresponds to variant rs267607482dbSNPEnsembl.1
Natural variantiVAR_009189345L → P in MFM1; distal onset; incapable of forming filamentous networks. 1 PublicationCorresponds to variant rs57639980dbSNPEnsembl.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 rs57965306dbSNPEnsembl.1
Natural variantiVAR_042455355R → P in MFM1. 1 PublicationCorresponds to variant rs61368398dbSNPEnsembl.1
Natural variantiVAR_042456357A → P in MFM1; unable to polymerize and form an intracellular filamentous network; abolishes binding to MTM1. 3 PublicationsCorresponds to variant rs58898021dbSNPEnsembl.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 rs121913000dbSNPEnsembl.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 rs59308628dbSNPEnsembl.1
Natural variantiVAR_018771385L → P in MFM1. 1 PublicationCorresponds to variant rs57955682dbSNPEnsembl.1
Natural variantiVAR_018772389Q → P in MFM1. 1 PublicationCorresponds to variant rs28930075dbSNPEnsembl.1
Natural variantiVAR_007902393N → I in MFM1; heterozygous with P-360 gives a severe childhood-onset; unable to form a functional filamentous network in the presence of P-360. 3 PublicationsCorresponds to variant rs121913001dbSNPEnsembl.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 rs61130669dbSNPEnsembl.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 rs57694264dbSNPEnsembl.1
Natural variantiVAR_042458406R → W in MFM1; unable to form a filamentous network. 2 PublicationsCorresponds to variant rs61726465dbSNPEnsembl.1
Natural variantiVAR_069074419P → S in MFM1; found in a family with myofibrillar myopathy and arrhythmogenic right ventricular cardiomyopathy. 1 PublicationCorresponds to variant rs62635763dbSNPEnsembl.1
Natural variantiVAR_042459442T → I in MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions. 1 PublicationCorresponds to variant rs121913005dbSNPEnsembl.1
Natural variantiVAR_042460449K → M in MFM1. 1
Natural variantiVAR_042461449K → T in MFM1. 1 PublicationCorresponds to variant rs267607485dbSNPEnsembl.1
Natural variantiVAR_018773451I → M in CMD1I and MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions. 3 PublicationsCorresponds to variant rs121913002dbSNPEnsembl.1
Natural variantiVAR_042462454R → W in MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions. 2 PublicationsCorresponds to variant rs267607490dbSNPEnsembl.1
Natural variantiVAR_042463460S → I in MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions. 1 PublicationCorresponds to variant rs267607491dbSNPEnsembl.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 Publication1
Natural variantiVAR_018773451I → M in CMD1I and MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions. 3 PublicationsCorresponds to variant rs121913002dbSNPEnsembl.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 rs57965306dbSNPEnsembl.1
Limb-girdle muscular dystrophy 2R (LGMD2R)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of limb-girdle muscular dystrophy, a disease characterized by proximal weakness, weakness of the hip and shoulder girdles and prominent asymmetrical quadriceps femoris and biceps brachii atrophy.
See also OMIM:615325

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

DisGeNETi1674.
MalaCardsiDES.
MIMi181400. phenotype.
601419. phenotype.
604765. phenotype.
615325. phenotype.
OpenTargetsiENSG00000175084.
Orphaneti34517. Autosomal dominant limb-girdle muscular dystrophy type 1E.
363543. Autosomal recessive limb-girdle muscular dystrophy due to desmin deficiency.
98909. Desminopathy.
154. Familial isolated dilated cardiomyopathy.
85146. Scapuloperoneal amyotrophy.
PharmGKBiPA27253.

Polymorphism and mutation databases

BioMutaiDES.
DMDMi6686280.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000637711 – 470DesminAdd BLAST470

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei12Phosphoserine; by AURKB1 Publication1
Modified residuei16Omega-N-methylarginineBy similarity1
Modified residuei17Phosphothreonine; by AURKB1 Publication1
Modified residuei28PhosphoserineCombined sources1
Modified residuei31PhosphoserineBy similarity1
Modified residuei32PhosphoserineBy similarity1
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 residuei81PhosphoserineBy similarity1
Modified residuei290PhosphoserineBy similarity1
Modified residuei358PhosphoserineBy similarity1
Modified residuei361PhosphoserineBy similarity1
Modified residuei424PhosphoserineBy similarity1

Post-translational modificationi

ADP-ribosylation prevents ability to form intermediate filaments.By similarity

Keywords - PTMi

ADP-ribosylation, Methylation, Phosphoprotein

Proteomic databases

EPDiP17661.
PaxDbiP17661.
PeptideAtlasiP17661.
PRIDEiP17661.

2D gel databases

REPRODUCTION-2DPAGEIPI00465084.
P17661.
SWISS-2DPAGEP17661.
UCD-2DPAGEP17661.

PTM databases

iPTMnetiP17661.
PhosphoSitePlusiP17661.
SwissPalmiP17661.

Expressioni

Gene expression databases

BgeeiENSG00000175084.
ExpressionAtlasiP17661. baseline and differential.
GenevisibleiP17661. HS.

Organism-specific databases

HPAiCAB000034.
HPA018803.

Interactioni

Subunit structurei

Homopolymer. 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).By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-1055572,EBI-1055572
DUX1O438124EBI-1055572,EBI-11599346
DUX4Q9UBX23EBI-1055572,EBI-11600078
DUX4L9Q6RFH84EBI-1055572,EBI-11599882
DYSFO759233EBI-1055572,EBI-2799016
EHHADHQ084265EBI-1055572,EBI-2339219
GFAPP141364EBI-1055572,EBI-744302
MLH1P406927EBI-1055572,EBI-744248
MTM1Q1349613EBI-1055572,EBI-2864109
NEFLP071963EBI-1055572,EBI-475646
PPP1R18Q6NYC85EBI-1055572,EBI-2557469
PRPHP412194EBI-1055572,EBI-752074
UBE2IQ7KZS03EBI-1055572,EBI-10180829
VIMP086704EBI-1055572,EBI-353844

GO - Molecular functioni

  • cytoskeletal protein binding Source: BHF-UCL
  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi108038. 39 interactors.
IntActiP17661. 39 interactors.
MINTiMINT-215829.
STRINGi9606.ENSP00000363071.

Structurei

3D structure databases

ProteinModelPortaliP17661.
SMRiP17661.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 108HeadAdd BLAST108
Regioni109 – 412RodAdd BLAST304
Regioni109 – 141Coil 1AAdd BLAST33
Regioni142 – 151Linker 110
Regioni152 – 252Coil 1BAdd BLAST101
Regioni253 – 268Linker 12Add BLAST16
Regioni269 – 287Coil 2AAdd BLAST19
Regioni288 – 295Linker 28
Regioni296 – 412Coil 2BAdd BLAST117
Regioni413 – 470TailAdd BLAST58

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IFZ1. Eukaryota.
ENOG410XRBS. LUCA.
GeneTreeiENSGT00830000128228.
HOVERGENiHBG013015.
InParanoidiP17661.
KOiK07610.
OMAiHIHTHAG.
OrthoDBiEOG091G12MK.
PhylomeDBiP17661.
TreeFamiTF330122.

Family and domain databases

InterProiIPR027698. DES.
IPR001664. IF.
IPR006821. Intermed_filament_DNA-bd.
IPR018039. Intermediate_filament_CS.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PTHR23239:SF28. PTHR23239:SF28. 1 hit.
PfamiPF00038. Filament. 1 hit.
PF04732. Filament_head. 1 hit.
[Graphical view]
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequencei

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
Checksum:i1B5D9EA93C3BB319
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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 rs58999456dbSNPEnsembl.1
Natural variantiVAR_0672077S → F in MFM1. 1 Publication1
Natural variantiVAR_06720813S → F in MFM1; some patients manifest a severe cardiac phenotype with right ventricular predominance. 2 PublicationsCorresponds to variant rs62636495dbSNPEnsembl.1
Natural variantiVAR_04244946S → F in MFM1. 1 PublicationCorresponds to variant rs60794845dbSNPEnsembl.1
Natural variantiVAR_04245046S → Y in MFM1. 1 PublicationCorresponds to variant rs60794845dbSNPEnsembl.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 rs267607499dbSNPEnsembl.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 Publication1
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 rs41272699dbSNPEnsembl.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 rs201945924dbSNPEnsembl.1
Natural variantiVAR_042452245E → D in MFM1. Corresponds to variant rs267607486dbSNPEnsembl.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 rs59962885dbSNPEnsembl.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 rs57496341dbSNPEnsembl.1
Natural variantiVAR_042453342N → D in MFM1; unable to form a filamentous network; abolishes binding to MTM1. 3 PublicationsCorresponds to variant rs267607482dbSNPEnsembl.1
Natural variantiVAR_009189345L → P in MFM1; distal onset; incapable of forming filamentous networks. 1 PublicationCorresponds to variant rs57639980dbSNPEnsembl.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 rs57965306dbSNPEnsembl.1
Natural variantiVAR_042455355R → P in MFM1. 1 PublicationCorresponds to variant rs61368398dbSNPEnsembl.1
Natural variantiVAR_042456357A → P in MFM1; unable to polymerize and form an intracellular filamentous network; abolishes binding to MTM1. 3 PublicationsCorresponds to variant rs58898021dbSNPEnsembl.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 rs121913000dbSNPEnsembl.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 rs59308628dbSNPEnsembl.1
Natural variantiVAR_018771385L → P in MFM1. 1 PublicationCorresponds to variant rs57955682dbSNPEnsembl.1
Natural variantiVAR_018772389Q → P in MFM1. 1 PublicationCorresponds to variant rs28930075dbSNPEnsembl.1
Natural variantiVAR_007902393N → I in MFM1; heterozygous with P-360 gives a severe childhood-onset; unable to form a functional filamentous network in the presence of P-360. 3 PublicationsCorresponds to variant rs121913001dbSNPEnsembl.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 rs61130669dbSNPEnsembl.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 rs57694264dbSNPEnsembl.1
Natural variantiVAR_042458406R → W in MFM1; unable to form a filamentous network. 2 PublicationsCorresponds to variant rs61726465dbSNPEnsembl.1
Natural variantiVAR_069074419P → S in MFM1; found in a family with myofibrillar myopathy and arrhythmogenic right ventricular cardiomyopathy. 1 PublicationCorresponds to variant rs62635763dbSNPEnsembl.1
Natural variantiVAR_042459442T → I in MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions. 1 PublicationCorresponds to variant rs121913005dbSNPEnsembl.1
Natural variantiVAR_042460449K → M in MFM1. 1
Natural variantiVAR_042461449K → T in MFM1. 1 PublicationCorresponds to variant rs267607485dbSNPEnsembl.1
Natural variantiVAR_018773451I → M in CMD1I and MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions. 3 PublicationsCorresponds to variant rs121913002dbSNPEnsembl.1
Natural variantiVAR_042462454R → W in MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions. 2 PublicationsCorresponds to variant rs267607490dbSNPEnsembl.1
Natural variantiVAR_042463460S → I in MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions. 1 PublicationCorresponds to variant rs267607491dbSNPEnsembl.1

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.

Genome annotation databases

EnsembliENST00000373960; ENSP00000363071; ENSG00000175084.
GeneIDi1674.
KEGGihsa:1674.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

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. 39 interactors.
IntActiP17661. 39 interactors.
MINTiMINT-215829.
STRINGi9606.ENSP00000363071.

PTM databases

iPTMnetiP17661.
PhosphoSitePlusiP17661.
SwissPalmiP17661.

Polymorphism and mutation databases

BioMutaiDES.
DMDMi6686280.

2D gel databases

REPRODUCTION-2DPAGEIPI00465084.
P17661.
SWISS-2DPAGEP17661.
UCD-2DPAGEP17661.

Proteomic databases

EPDiP17661.
PaxDbiP17661.
PeptideAtlasiP17661.
PRIDEiP17661.

Protocols and materials databases

DNASUi1674.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000373960; ENSP00000363071; ENSG00000175084.
GeneIDi1674.
KEGGihsa:1674.

Organism-specific databases

CTDi1674.
DisGeNETi1674.
GeneCardsiDES.
GeneReviewsiDES.
HGNCiHGNC:2770. DES.
HPAiCAB000034.
HPA018803.
MalaCardsiDES.
MIMi125660. gene.
181400. phenotype.
601419. phenotype.
604765. phenotype.
615325. phenotype.
neXtProtiNX_P17661.
OpenTargetsiENSG00000175084.
Orphaneti34517. Autosomal dominant limb-girdle muscular dystrophy type 1E.
363543. Autosomal recessive limb-girdle muscular dystrophy due to desmin deficiency.
98909. Desminopathy.
154. Familial isolated dilated cardiomyopathy.
85146. Scapuloperoneal amyotrophy.
PharmGKBiPA27253.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IFZ1. Eukaryota.
ENOG410XRBS. LUCA.
GeneTreeiENSGT00830000128228.
HOVERGENiHBG013015.
InParanoidiP17661.
KOiK07610.
OMAiHIHTHAG.
OrthoDBiEOG091G12MK.
PhylomeDBiP17661.
TreeFamiTF330122.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000175084-MONOMER.
ReactomeiR-HSA-390522. Striated Muscle Contraction.
SIGNORiP17661.

Miscellaneous databases

ChiTaRSiDES. human.
GeneWikiiDesmin.
GenomeRNAii1674.
PROiP17661.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000175084.
ExpressionAtlasiP17661. baseline and differential.
GenevisibleiP17661. HS.

Family and domain databases

InterProiIPR027698. DES.
IPR001664. IF.
IPR006821. Intermed_filament_DNA-bd.
IPR018039. Intermediate_filament_CS.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PTHR23239:SF28. PTHR23239:SF28. 1 hit.
PfamiPF00038. Filament. 1 hit.
PF04732. Filament_head. 1 hit.
[Graphical view]
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDESM_HUMAN
AccessioniPrimary (citable) accession number: P17661
Secondary accession number(s): Q15787
, Q549R7, Q549R8, Q549R9, Q8IZR1, Q8IZR6, Q8NES2, Q8NEU6, Q8TAC4, Q8TCX2, Q8TD99, Q9UHN5, Q9UJ80
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 183 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.