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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

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

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

Keywordsi

Molecular functionMuscle protein

Enzyme and pathway databases

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

EuPathDBiHostDB:ENSG00000175084.11.
HGNCiHGNC:2770. DES.

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

Pathology & Biotechi

Involvement in diseasei

Myopathy, myofibrillar, 1 (MFM1)27 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 dbSNP:rs58999456Ensembl.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 dbSNP:rs62636495Ensembl.1
Natural variantiVAR_07904816R → C in MFM1. 1 Publication1
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:rs60794845Ensembl.1
Natural variantiVAR_04245046S → Y in MFM1. 1 PublicationCorresponds to variant dbSNP:rs60794845Ensembl.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:rs267607499Ensembl.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:rs267607486Ensembl.1
Natural variantiVAR_007900337A → P in MFM1; mild adult-onset; unable to form a functional filamentous network. 2 PublicationsCorresponds to variant dbSNP:rs59962885Ensembl.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:rs57496341Ensembl.1
Natural variantiVAR_042453342N → D in MFM1; unable to form a filamentous network; abolishes binding to MTM1. 3 PublicationsCorresponds to variant dbSNP:rs267607482Ensembl.1
Natural variantiVAR_009189345L → P in MFM1; distal onset; incapable of forming filamentous networks. 1 PublicationCorresponds to variant dbSNP:rs57639980Ensembl.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:rs57965306Ensembl.1
Natural variantiVAR_042455355R → P in MFM1. 1 PublicationCorresponds to variant dbSNP:rs61368398Ensembl.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:rs58898021Ensembl.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:rs121913000Ensembl.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:rs59308628Ensembl.1
Natural variantiVAR_018771385L → P in MFM1. 1 PublicationCorresponds to variant dbSNP:rs57955682Ensembl.1
Natural variantiVAR_018772389Q → P in MFM1. 1 PublicationCorresponds to variant dbSNP:rs28930075Ensembl.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 dbSNP:rs121913001Ensembl.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:rs61130669Ensembl.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:rs57694264Ensembl.1
Natural variantiVAR_042458406R → W in MFM1; unable to form a filamentous network. 3 PublicationsCorresponds to variant dbSNP:rs61726465Ensembl.1
Natural variantiVAR_069074419P → S in MFM1; found in a family with myofibrillar myopathy and arrhythmogenic right ventricular cardiomyopathy. 1 PublicationCorresponds to variant dbSNP:rs62635763Ensembl.1
Natural variantiVAR_042459442T → I in MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions. 1 PublicationCorresponds to variant dbSNP:rs121913005Ensembl.1
Natural variantiVAR_042460449K → M in MFM1. 1
Natural variantiVAR_042461449K → T in MFM1. 1 PublicationCorresponds to variant dbSNP:rs267607485Ensembl.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:rs121913002Ensembl.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 Publications1
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:rs267607490Ensembl.1
Natural variantiVAR_042463460S → I in MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions. 1 PublicationCorresponds to variant dbSNP:rs267607491Ensembl.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; reduced interaction with CRYAB. 4 PublicationsCorresponds to variant dbSNP:rs121913002Ensembl.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:rs57965306Ensembl.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.
GeneReviewsiDES.
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
Initiator methionineiRemovedBy similarity
ChainiPRO_00000637712 – 470DesminAdd BLAST469

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei7Phosphoserine; by CDK1By similarity1
Modified residuei8PhosphoserineBy similarity1
Modified residuei12Phosphoserine; by AURKB1 Publication1
Modified residuei13PhosphoserineBy similarity1
Modified residuei14Nitrated tyrosineBy similarity1
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 residuei48PhosphoserineBy similarity1
Modified residuei51PhosphoserineBy 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 residuei82PhosphoserineBy similarity1
Modified residuei92PhosphoserineBy similarity1
Cross-linki109Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei122PhosphotyrosineBy similarity1
Modified residuei125N6-acetyllysine; alternateBy similarity1
Modified residuei125N6-succinyllysine; alternateBy similarity1
Cross-linki125Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei144N6-acetyllysine; alternateBy similarity1
Cross-linki144Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei193N6-acetyllysine; alternateBy similarity1
Modified residuei193N6-succinyllysine; alternateBy similarity1
Modified residuei231PhosphoserineBy similarity1
Modified residuei240N6-acetyllysineBy similarity1
Cross-linki267Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei290PhosphoserineBy similarity1
Modified residuei299N6-acetyllysine; alternateBy similarity1
Modified residuei299N6-succinyllysine; alternateBy similarity1
Cross-linki299Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki318Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei330PhosphoserineBy similarity1
Modified residuei358PhosphoserineBy similarity1
Modified residuei361PhosphoserineBy similarity1
Modified residuei378N6-acetyllysine; alternateBy similarity1
Cross-linki378Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei388Nitrated tyrosineBy similarity1
Modified residuei414PhosphoserineBy similarity1
Modified residuei424PhosphoserineBy similarity1
Modified residuei431PhosphothreonineBy similarity1
Cross-linki443Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei449N6-acetyllysine; alternateBy similarity1
Modified residuei449N6-succinyllysine; alternateBy similarity1
Cross-linki449Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki449Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei450PhosphothreonineBy similarity1

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

Acetylation, ADP-ribosylation, Isopeptide bond, Methylation, Nitration, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP17661.
PaxDbiP17661.
PeptideAtlasiP17661.
PRIDEiP17661.

2D gel databases

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

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 (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

Binary interactionsi

Show more details

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi108038. 43 interactors.
IntActiP17661. 52 interactors.
MINTiMINT-215829.
STRINGi9606.ENSP00000363071.

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini108 – 416IF rodPROSITE-ProRule annotationAdd BLAST309

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 108HeadAdd BLAST107
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

Sequence similaritiesi

Belongs to the intermediate filament family.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

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

Family and domain databases

InterProiView protein in InterPro
IPR027698. DES.
IPR001664. IF.
IPR006821. Intermed_filament_DNA-bd.
IPR018039. Intermediate_filament_CS.
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.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

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 dbSNP:rs58999456Ensembl.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 dbSNP:rs62636495Ensembl.1
Natural variantiVAR_07904816R → C in MFM1. 1 Publication1
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:rs60794845Ensembl.1
Natural variantiVAR_04245046S → Y in MFM1. 1 PublicationCorresponds to variant dbSNP:rs60794845Ensembl.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:rs267607499Ensembl.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 dbSNP:rs41272699Ensembl.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:rs267607486Ensembl.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:rs59962885Ensembl.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:rs57496341Ensembl.1
Natural variantiVAR_042453342N → D in MFM1; unable to form a filamentous network; abolishes binding to MTM1. 3 PublicationsCorresponds to variant dbSNP:rs267607482Ensembl.1
Natural variantiVAR_009189345L → P in MFM1; distal onset; incapable of forming filamentous networks. 1 PublicationCorresponds to variant dbSNP:rs57639980Ensembl.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:rs57965306Ensembl.1
Natural variantiVAR_042455355R → P in MFM1. 1 PublicationCorresponds to variant dbSNP:rs61368398Ensembl.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:rs58898021Ensembl.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:rs121913000Ensembl.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:rs59308628Ensembl.1
Natural variantiVAR_018771385L → P in MFM1. 1 PublicationCorresponds to variant dbSNP:rs57955682Ensembl.1
Natural variantiVAR_018772389Q → P in MFM1. 1 PublicationCorresponds to variant dbSNP:rs28930075Ensembl.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 dbSNP:rs121913001Ensembl.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:rs61130669Ensembl.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:rs57694264Ensembl.1
Natural variantiVAR_042458406R → W in MFM1; unable to form a filamentous network. 3 PublicationsCorresponds to variant dbSNP:rs61726465Ensembl.1
Natural variantiVAR_069074419P → S in MFM1; found in a family with myofibrillar myopathy and arrhythmogenic right ventricular cardiomyopathy. 1 PublicationCorresponds to variant dbSNP:rs62635763Ensembl.1
Natural variantiVAR_042459442T → I in MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions. 1 PublicationCorresponds to variant dbSNP:rs121913005Ensembl.1
Natural variantiVAR_042460449K → M in MFM1. 1
Natural variantiVAR_042461449K → T in MFM1. 1 PublicationCorresponds to variant dbSNP:rs267607485Ensembl.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:rs121913002Ensembl.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 Publications1
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:rs267607490Ensembl.1
Natural variantiVAR_042463460S → I in MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions. 1 PublicationCorresponds to variant dbSNP:rs267607491Ensembl.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

Similar proteinsi

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 historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: October 25, 2017
This is version 190 of the entry and version 3 of the sequence. See 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