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UniProtKB - P17661 (DESM_HUMAN)

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Protein

Desmin

Gene

DES

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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
View the complete GO annotation on QuickGO ...

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
View the complete GO annotation on QuickGO ...

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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

EuPathDBiHostDB:ENSG00000175084.11
HGNCiHGNC:2770 DES
MIMi125660 gene
neXtProtiNX_P17661

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 disk and myofibrils, and replacement of the normal myofibrillar markings by small dense granules, or larger hyaline masses, or amorphous material. MFM1 is characterized by skeletal muscle weakness associated with cardiac conduction blocks, arrhythmias, restrictive heart failure, and accumulation of desmin-reactive deposits in cardiac and skeletal muscle cells.
See also OMIM:601419
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0424482S → I in MFM1. 1 PublicationCorresponds to variant dbSNP:rs58999456EnsemblClinVar.1
Natural variantiVAR_0672077S → F in MFM1. 1 PublicationCorresponds to variant dbSNP:rs903985237Ensembl.1
Natural variantiVAR_06720813S → F in MFM1; some patients manifest a severe cardiac phenotype with right ventricular predominance. 2 PublicationsCorresponds to variant dbSNP:rs62636495EnsemblClinVar.1
Natural variantiVAR_07904816R → C in MFM1. 1 PublicationCorresponds to variant dbSNP:rs60798368EnsemblClinVar.1
Natural variantiVAR_04244946S → F in MFM1; exhibits significantly delayed filament assembly kinetics when bound to NEB; enhanced binding affinity towards NEB. 2 PublicationsCorresponds to variant dbSNP:rs60794845EnsemblClinVar.1
Natural variantiVAR_04245046S → Y in MFM1. 1 PublicationCorresponds to variant dbSNP:rs60794845EnsemblClinVar.1
Natural variantiVAR_069191116N → S in MFM1; the clinical picture is dominated by arrhythmogenic right ventricular cardiomyopathy and terminal heart failure; results in impaired filaments formation. 1 PublicationCorresponds to variant dbSNP:rs267607499EnsemblClinVar.1
Natural variantiVAR_009188173 – 179Missing in MFM1; severe form. 1 Publication7
Natural variantiVAR_070101240Missing in MFM1; the mutant cannot form de novo desmin intermediate filaments causing disruption of the endogenous intermediate filament network and formation of pathologic aggregates. 1 Publication1
Natural variantiVAR_042452245E → D in MFM1; exhibits significantly delayed filament assembly kinetics when bound to NEB and NEBL; enhanced binding affinity towards NEB and NEBL. 1 PublicationCorresponds to variant dbSNP:rs267607486EnsemblClinVar.1
Natural variantiVAR_007900337A → P in MFM1; mild adult-onset; unable to form a functional filamentous network. 2 PublicationsCorresponds to variant dbSNP:rs59962885EnsemblClinVar.1
Natural variantiVAR_067209338L → R in MFM1; results in the formation of a filamentous network disrupted by multiple breaks and clumps or large aggregates. 1 PublicationCorresponds to variant dbSNP:rs57496341EnsemblClinVar.1
Natural variantiVAR_042453342N → D in MFM1; unable to form a filamentous network; abolishes binding to MTM1. 3 PublicationsCorresponds to variant dbSNP:rs267607482EnsemblClinVar.1
Natural variantiVAR_009189345L → P in MFM1; distal onset; incapable of forming filamentous networks. 1 PublicationCorresponds to variant dbSNP:rs57639980EnsemblClinVar.1
Natural variantiVAR_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_079049453T → I in MFM1; exhibits significantly delayed filament assembly kinetics when bound to NEB and NEBL; enhanced binding affinity towards NEB and NEBL. 2 PublicationsCorresponds to variant dbSNP:rs267607488EnsemblClinVar.1
Natural variantiVAR_042462454R → W in MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions; increased interaction with CRYAB. 3 PublicationsCorresponds to variant dbSNP:rs267607490EnsemblClinVar.1
Natural variantiVAR_042463460S → I in MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions. 1 PublicationCorresponds to variant dbSNP:rs267607491EnsemblClinVar.1
Cardiomyopathy, dilated 1I (CMD1I)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.
See also OMIM:604765
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_075228120A → D in CMD1I; results in impaired filaments formation, does not localize at intercalated disks. 1 Publication1
Natural variantiVAR_075229136L → P in CMD1I; results in impaired filaments formation, does not localize at intercalated disks. 1 Publication1
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
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
ChainiPRO_00000637711 – 470DesminAdd BLAST470

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

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

EPDiP17661
PaxDbiP17661
PeptideAtlasiP17661
PRIDEiP17661
ProteomicsDBi53502

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
View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi108038, 46 interactors
IntActiP17661, 58 interactors
MINTiP17661
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
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

Sequence similaritiesi

Belongs to the intermediate filament family.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IFZ1 Eukaryota
ENOG410XRBS LUCA
GeneTreeiENSGT00910000143989
HOVERGENiHBG013015
InParanoidiP17661
KOiK07610
OMAiNQRARVE
OrthoDBiEOG091G12MK
PhylomeDBiP17661
TreeFamiTF330122

Family and domain databases

InterProiView protein in InterPro
IPR027698 DES
IPR001664 IF
IPR018039 IF_conserved
IPR039008 IF_rod_dom
IPR006821 Intermed_filament_DNA-bd
PANTHERiPTHR23239 PTHR23239, 1 hit
PTHR23239:SF28 PTHR23239:SF28, 1 hit
PfamiView protein in Pfam
PF00038 Filament, 1 hit
PF04732 Filament_head, 1 hit
SMARTiView protein in SMART
SM01391 Filament, 1 hit
PROSITEiView protein in PROSITE
PS00226 IF_ROD_1, 1 hit
PS51842 IF_ROD_2, 1 hit

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 dbSNP:rs58999456EnsemblClinVar.1
Natural variantiVAR_0672077S → F in MFM1. 1 PublicationCorresponds to variant dbSNP:rs903985237Ensembl.1
Natural variantiVAR_06720813S → F in MFM1; some patients manifest a severe cardiac phenotype with right ventricular predominance. 2 PublicationsCorresponds to variant dbSNP:rs62636495EnsemblClinVar.1
Natural variantiVAR_07904816R → C in MFM1. 1 PublicationCorresponds to variant dbSNP:rs60798368EnsemblClinVar.1
Natural variantiVAR_04244946S → F in MFM1; exhibits significantly delayed filament assembly kinetics when bound to NEB; enhanced binding affinity towards NEB. 2 PublicationsCorresponds to variant dbSNP:rs60794845EnsemblClinVar.1
Natural variantiVAR_04245046S → Y in MFM1. 1 PublicationCorresponds to variant dbSNP:rs60794845EnsemblClinVar.1
Natural variantiVAR_069191116N → S in MFM1; the clinical picture is dominated by arrhythmogenic right ventricular cardiomyopathy and terminal heart failure; results in impaired filaments formation. 1 PublicationCorresponds to variant dbSNP:rs267607499EnsemblClinVar.1
Natural variantiVAR_075228120A → D in CMD1I; results in impaired filaments formation, does not localize at intercalated disks. 1 Publication1
Natural variantiVAR_075229136L → P in CMD1I; results in impaired filaments formation, does not localize at intercalated disks. 1 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: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:
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: July 18, 2018
This is version 197 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

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