P17661 · DESM_HUMAN
- ProteinDesmin
- GeneDES
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids470 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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. Required for nuclear membrane integrity, via anchoring at the cell tip and nuclear envelope, resulting in maintenance of microtubule-derived intracellular mechanical forces (By similarity).
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).
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. Required for nuclear membrane integrity, via anchoring at the cell tip and nuclear envelope, resulting in maintenance of microtubule-derived intracellular mechanical forces (By similarity).
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).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cardiac myofibril | |
Cellular Component | cell tip | |
Cellular Component | cell-cell junction | |
Cellular Component | cytosol | |
Cellular Component | extracellular exosome | |
Cellular Component | fascia adherens | |
Cellular Component | intercalated disc | |
Cellular Component | intermediate filament | |
Cellular Component | intermediate filament cytoskeleton | |
Cellular Component | neuromuscular junction | |
Cellular Component | nuclear envelope | |
Cellular Component | nucleus | |
Cellular Component | sarcolemma | |
Cellular Component | Z disc | |
Molecular Function | cytoskeletal protein binding | |
Molecular Function | identical protein binding | |
Molecular Function | structural constituent of cytoskeleton | |
Biological Process | cytoskeleton organization | |
Biological Process | intermediate filament organization | |
Biological Process | muscle contraction | |
Biological Process | nuclear envelope organization | |
Biological Process | regulation of heart contraction | |
Biological Process | skeletal muscle organ development |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDesmin
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP17661
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localizes in the intercalated disks which occur at the Z line of cardiomyocytes (PubMed:24200904, PubMed:26724190).
Localizes in the nucleus exclusively in differentiating cardiac progenitor cells and premature cardiomyocytes (By similarity).
PKP2 is required for correct anchoring of DES at the cell tip and nuclear envelope (By similarity).
Localizes in the nucleus exclusively in differentiating cardiac progenitor cells and premature cardiomyocytes (By similarity).
PKP2 is required for correct anchoring of DES at the cell tip and nuclear envelope (By similarity).
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Myopathy, myofibrillar, 1 (MFM1)
- Note
- 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 alsoMIM:601419
Natural variants in MFM1
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_042448 | 2 | S>I | in MFM1; dbSNP:rs58999456 | |
VAR_067207 | 7 | S>F | in MFM1; dbSNP:rs903985237 | |
VAR_067208 | 13 | S>F | in MFM1; some patients manifest a severe cardiac phenotype with right ventricular predominance; dbSNP:rs62636495 | |
VAR_079048 | 16 | R>C | in MFM1; dbSNP:rs60798368 | |
VAR_042449 | 46 | S>F | in MFM1; exhibits significantly delayed filament assembly kinetics when bound to NEB; enhanced binding affinity towards NEB; dbSNP:rs60794845 | |
VAR_042450 | 46 | S>Y | in MFM1; dbSNP:rs60794845 | |
VAR_069191 | 116 | N>S | in MFM1; the clinical picture is dominated by arrhythmogenic right ventricular cardiomyopathy and terminal heart failure; results in impaired filaments formation; dbSNP:rs267607499 | |
VAR_009188 | 173-179 | missing | in MFM1; severe form | |
VAR_070101 | 240 | missing | in MFM1; the mutant cannot form de novo desmin intermediate filaments causing disruption of the endogenous intermediate filament network and formation of pathologic aggregates; dbSNP:rs2125167652 | |
VAR_042452 | 245 | E>D | in MFM1; exhibits significantly delayed filament assembly kinetics when bound to NEB and NEBL; enhanced binding affinity towards NEB and NEBL; dbSNP:rs267607486 | |
VAR_007900 | 337 | A>P | in MFM1; mild adult-onset; unable to form a functional filamentous network; dbSNP:rs59962885 | |
VAR_067209 | 338 | L>R | in MFM1; results in the formation of a filamentous network disrupted by multiple breaks and clumps or large aggregates; dbSNP:rs57496341 | |
VAR_042453 | 342 | N>D | in MFM1; unable to form a filamentous network; abolishes binding to MTM1; dbSNP:rs267607482 | |
VAR_009189 | 345 | L>P | in MFM1; distal onset; incapable of forming filamentous networks; dbSNP:rs57639980 | |
VAR_042454 | 350 | R>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; dbSNP:rs57965306 | |
VAR_042455 | 355 | R>P | in MFM1; dbSNP:rs61368398 | |
VAR_042456 | 357 | A>P | in MFM1; unable to polymerize and form an intracellular filamentous network; abolishes binding to MTM1; dbSNP:rs58898021 | |
VAR_018769 | 359-361 | missing | in MFM1 | |
VAR_007901 | 360 | A>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; dbSNP:rs121913000 | |
VAR_018770 | 366 | missing | in MFM1 | |
VAR_042457 | 370 | L>P | in MFM1; unable to polymerize and form an intracellular filamentous network; does not affect binding to MTM1; dbSNP:rs59308628 | |
VAR_018771 | 385 | L>P | in MFM1; dbSNP:rs57955682 | |
VAR_018772 | 389 | Q>P | in MFM1; dbSNP:rs121913004 | |
VAR_007902 | 393 | N>I | in MFM1; heterozygous with P-360 gives a severe childhood-onset; filamentous network is not affected however several spots indicate focal disorganization; dbSNP:rs121913001 | |
VAR_067210 | 399 | D>Y | in MFM1; results in the formation of a filamentous network disrupted by multiple breaks and clumps or large aggregates; dbSNP:rs61130669 | |
VAR_067211 | 401 | E>K | in MFM1; results in the formation of a filamentous network disrupted by multiple breaks and clumps or large aggregates; dbSNP:rs57694264 | |
VAR_042458 | 406 | R>W | in MFM1; unable to form a filamentous network; dbSNP:rs121913003 | |
VAR_069074 | 419 | P>S | in MFM1; found in a family with myofibrillar myopathy and arrhythmogenic right ventricular cardiomyopathy; dbSNP:rs62635763 | |
VAR_042459 | 442 | T>I | in MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions; dbSNP:rs121913005 | |
VAR_042460 | 449 | K>M | in MFM1 | |
VAR_042461 | 449 | K>T | in MFM1; dbSNP:rs267607485 | |
VAR_018773 | 451 | I>M | in CMD1I and MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions; reduced interaction with CRYAB; dbSNP:rs121913002 | |
VAR_079049 | 453 | T>I | in MFM1; exhibits significantly delayed filament assembly kinetics when bound to NEB and NEBL; enhanced binding affinity towards NEB and NEBL; dbSNP:rs267607488 | |
VAR_042462 | 454 | R>W | in MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions; increased interaction with CRYAB; dbSNP:rs267607490 | |
VAR_042463 | 460 | S>I | in MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions; dbSNP:rs267607491 |
Cardiomyopathy, dilated, 1I (CMD1I)
- Note
- 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 alsoMIM:604765
Natural variants in CMD1I
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_075228 | 120 | A>D | in CMD1I; results in impaired filaments formation, does not localize at intercalated disks; dbSNP:rs1954373010 | |
VAR_075229 | 136 | L>P | in CMD1I; results in impaired filaments formation, does not localize at intercalated disks; dbSNP:rs397516695 | |
VAR_075230 | 326 | H>R | in CMD1I; uncertain significance; does not affect filaments formation; dbSNP:rs2125168243 | |
VAR_086534 | 398 | L>P | in CMD1I; uncertain significance; impaired subcellular localization; dbSNP:rs796115330 | |
VAR_018773 | 451 | I>M | in CMD1I and MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions; reduced interaction with CRYAB; dbSNP:rs121913002 |
Neurogenic scapuloperoneal syndrome Kaeser type (Kaeser syndrome)
- Note
- 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 alsoMIM:181400
Natural variants in Kaeser syndrome
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_042454 | 350 | R>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; dbSNP:rs57965306 |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_042448 | 2 | in MFM1; dbSNP:rs58999456 | |||
Sequence: S → I | ||||||
Natural variant | VAR_067207 | 7 | in MFM1; dbSNP:rs903985237 | |||
Sequence: S → F | ||||||
Natural variant | VAR_067208 | 13 | in MFM1; some patients manifest a severe cardiac phenotype with right ventricular predominance; dbSNP:rs62636495 | |||
Sequence: S → F | ||||||
Natural variant | VAR_079048 | 16 | in MFM1; dbSNP:rs60798368 | |||
Sequence: R → C | ||||||
Natural variant | VAR_042449 | 46 | in MFM1; exhibits significantly delayed filament assembly kinetics when bound to NEB; enhanced binding affinity towards NEB; dbSNP:rs60794845 | |||
Sequence: S → F | ||||||
Natural variant | VAR_042450 | 46 | in MFM1; dbSNP:rs60794845 | |||
Sequence: S → Y | ||||||
Natural variant | VAR_069191 | 116 | in MFM1; the clinical picture is dominated by arrhythmogenic right ventricular cardiomyopathy and terminal heart failure; results in impaired filaments formation; dbSNP:rs267607499 | |||
Sequence: N → S | ||||||
Natural variant | VAR_075228 | 120 | in CMD1I; results in impaired filaments formation, does not localize at intercalated disks; dbSNP:rs1954373010 | |||
Sequence: A → D | ||||||
Mutagenesis | 120 | Results in impaired filaments formation. | ||||
Sequence: A → E or R | ||||||
Mutagenesis | 120 | Does not result in impaired filaments formation. | ||||
Sequence: A → K, L, or V | ||||||
Natural variant | VAR_075229 | 136 | in CMD1I; results in impaired filaments formation, does not localize at intercalated disks; dbSNP:rs397516695 | |||
Sequence: L → P | ||||||
Natural variant | VAR_009188 | 173-179 | in MFM1; severe form | |||
Sequence: Missing | ||||||
Natural variant | VAR_042451 | 213 | 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; dbSNP:rs41272699 | |||
Sequence: A → V | ||||||
Natural variant | VAR_070101 | 240 | in MFM1; the mutant cannot form de novo desmin intermediate filaments causing disruption of the endogenous intermediate filament network and formation of pathologic aggregates; dbSNP:rs2125167652 | |||
Sequence: Missing | ||||||
Natural variant | VAR_069192 | 241 | found in a patient with severe arrhythmogenic right ventricular cardiomyopathy; uncertain significance; the patient also carries a frameshift mutation in PKP2; dbSNP:rs201945924 | |||
Sequence: K → E | ||||||
Natural variant | VAR_042452 | 245 | in MFM1; exhibits significantly delayed filament assembly kinetics when bound to NEB and NEBL; enhanced binding affinity towards NEB and NEBL; dbSNP:rs267607486 | |||
Sequence: E → D | ||||||
Natural variant | VAR_075230 | 326 | in CMD1I; uncertain significance; does not affect filaments formation; dbSNP:rs2125168243 | |||
Sequence: H → R | ||||||
Natural variant | VAR_007900 | 337 | in MFM1; mild adult-onset; unable to form a functional filamentous network; dbSNP:rs59962885 | |||
Sequence: A → P | ||||||
Natural variant | VAR_067209 | 338 | in MFM1; results in the formation of a filamentous network disrupted by multiple breaks and clumps or large aggregates; dbSNP:rs57496341 | |||
Sequence: L → R | ||||||
Natural variant | VAR_042453 | 342 | in MFM1; unable to form a filamentous network; abolishes binding to MTM1; dbSNP:rs267607482 | |||
Sequence: N → D | ||||||
Natural variant | VAR_009189 | 345 | in MFM1; distal onset; incapable of forming filamentous networks; dbSNP:rs57639980 | |||
Sequence: L → P | ||||||
Natural variant | VAR_042454 | 350 | 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; dbSNP:rs57965306 | |||
Sequence: R → P | ||||||
Natural variant | VAR_042455 | 355 | in MFM1; dbSNP:rs61368398 | |||
Sequence: R → P | ||||||
Natural variant | VAR_042456 | 357 | in MFM1; unable to polymerize and form an intracellular filamentous network; abolishes binding to MTM1; dbSNP:rs58898021 | |||
Sequence: A → P | ||||||
Natural variant | VAR_018769 | 359-361 | in MFM1 | |||
Sequence: Missing | ||||||
Natural variant | VAR_007901 | 360 | 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; dbSNP:rs121913000 | |||
Sequence: A → P | ||||||
Natural variant | VAR_018770 | 366 | in MFM1 | |||
Sequence: Missing | ||||||
Natural variant | VAR_042457 | 370 | in MFM1; unable to polymerize and form an intracellular filamentous network; does not affect binding to MTM1; dbSNP:rs59308628 | |||
Sequence: L → P | ||||||
Natural variant | VAR_018771 | 385 | in MFM1; dbSNP:rs57955682 | |||
Sequence: L → P | ||||||
Natural variant | VAR_018772 | 389 | in MFM1; dbSNP:rs121913004 | |||
Sequence: Q → P | ||||||
Natural variant | VAR_007902 | 393 | in MFM1; heterozygous with P-360 gives a severe childhood-onset; filamentous network is not affected however several spots indicate focal disorganization; dbSNP:rs121913001 | |||
Sequence: N → I | ||||||
Natural variant | VAR_086534 | 398 | in CMD1I; uncertain significance; impaired subcellular localization; dbSNP:rs796115330 | |||
Sequence: L → P | ||||||
Natural variant | VAR_067210 | 399 | in MFM1; results in the formation of a filamentous network disrupted by multiple breaks and clumps or large aggregates; dbSNP:rs61130669 | |||
Sequence: D → Y | ||||||
Natural variant | VAR_067211 | 401 | in MFM1; results in the formation of a filamentous network disrupted by multiple breaks and clumps or large aggregates; dbSNP:rs57694264 | |||
Sequence: E → K | ||||||
Natural variant | VAR_042458 | 406 | in MFM1; unable to form a filamentous network; dbSNP:rs121913003 | |||
Sequence: R → W | ||||||
Natural variant | VAR_069074 | 419 | in MFM1; found in a family with myofibrillar myopathy and arrhythmogenic right ventricular cardiomyopathy; dbSNP:rs62635763 | |||
Sequence: P → S | ||||||
Natural variant | VAR_042459 | 442 | in MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions; dbSNP:rs121913005 | |||
Sequence: T → I | ||||||
Natural variant | VAR_042460 | 449 | in MFM1 | |||
Sequence: K → M | ||||||
Natural variant | VAR_042461 | 449 | in MFM1; dbSNP:rs267607485 | |||
Sequence: K → T | ||||||
Natural variant | VAR_018773 | 451 | in CMD1I and MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions; reduced interaction with CRYAB; dbSNP:rs121913002 | |||
Sequence: I → M | ||||||
Natural variant | VAR_079049 | 453 | in MFM1; exhibits significantly delayed filament assembly kinetics when bound to NEB and NEBL; enhanced binding affinity towards NEB and NEBL; dbSNP:rs267607488 | |||
Sequence: T → I | ||||||
Natural variant | VAR_042462 | 454 | in MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions; increased interaction with CRYAB; dbSNP:rs267607490 | |||
Sequence: R → W | ||||||
Natural variant | VAR_042463 | 460 | in MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions; dbSNP:rs267607491 | |||
Sequence: S → I |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 803 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Chain | PRO_0000063771 | 2-470 | UniProt | Desmin | |||
Sequence: SQAYSSSQRVSSYRRTFGGAPGFPLGSPLSSPVFPRAGFGSKGSSSSVTSRVYQVSRTSGGAGGLGSLRASRLGTTRTPSSYGAGELLDFSLADAVNQEFLTTRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKGREPTRVAELYEEELRELRRQVEVLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEIRELQAQLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDALKGTNDSLMRQMRELEDRFASEASGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVEIATYRKLLEGEESRINLPIQTYSALNFRETSPEQRGSEVHTKKTVMIKTIETRDGEVVSEATQQQHEVL | |||||||
Modified residue | 7 | UniProt | Phosphoserine; by CDK1 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 8 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 12 | UniProt | Phosphoserine; by AURKB | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 12 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 16 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue | 17 | UniProt | Phosphothreonine; by AURKB and ROCK1 | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 17 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 28 | UniProt | Phosphoserine; by CDK1 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 28 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 31 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 31 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 32 | UniProt | Phosphoserine; by CDK1 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 32 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 37 | UniProt | Asymmetric dimethylarginine; alternate | ||||
Sequence: R | |||||||
Modified residue | 37 | UniProt | Omega-N-methylarginine; alternate | ||||
Sequence: R | |||||||
Modified residue (large scale data) | 42 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 45 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 45 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 46 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 48 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 58 | UniProt | ADP-ribosylarginine | ||||
Sequence: R | |||||||
Modified residue (large scale data) | 59 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 60 | UniProt | Phosphoserine; by AURKB | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 60 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 68 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 68 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 70 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue (large scale data) | 72 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 76 | UniProt | Phosphothreonine; by ROCK1 | ||||
Sequence: T | |||||||
Modified residue | 77 | UniProt | Phosphothreonine; by ROCK1 | ||||
Sequence: T | |||||||
Modified residue | 81 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 81 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 82 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 92 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 149 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 231 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 290 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 290 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 301 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 330 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 344 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 358 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 358 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 361 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 361 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 363 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 424 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 424 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 432 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 438 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 453 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 460 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 463 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
ADP-ribosylation prevents ability to form intermediate filaments.
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.
Ubiquitination by a SCF-like complex containing ASB2 isoform 1 leads to proteasomal degradation.
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Interaction
Subunit
Homomer (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).
Interacts with ASB2 isoform 1; the interaction targets DES for proteasomal degradation (By similarity).
Interacts with PLEC isoform 1C (PubMed:24940650).
Interacts with PKP1 (PubMed:10852826).
Interacts with FLII (By similarity).
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).
Interacts with ASB2 isoform 1; the interaction targets DES for proteasomal degradation (By similarity).
Interacts with PLEC isoform 1C (PubMed:24940650).
Interacts with PKP1 (PubMed:10852826).
Interacts with FLII (By similarity).
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 2-108 | Head | ||||
Sequence: SQAYSSSQRVSSYRRTFGGAPGFPLGSPLSSPVFPRAGFGSKGSSSSVTSRVYQVSRTSGGAGGLGSLRASRLGTTRTPSSYGAGELLDFSLADAVNQEFLTTRTNE | ||||||
Domain | 108-416 | IF rod | ||||
Sequence: EKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKGREPTRVAELYEEELRELRRQVEVLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEIRELQAQLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDALKGTNDSLMRQMRELEDRFASEASGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVEIATYRKLLEGEESRI | ||||||
Region | 109-141 | Coil 1A | ||||
Sequence: KVELQELNDRFANYIEKVRFLEQQNAALAAEVN | ||||||
Region | 142-151 | Linker 1 | ||||
Sequence: RLKGREPTRV | ||||||
Region | 152-252 | Coil 1B | ||||
Sequence: AELYEEELRELRRQVEVLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEIRELQA | ||||||
Region | 253-268 | Linker 12 | ||||
Sequence: QLQEQQVQVEMDMSKP | ||||||
Region | 268-415 | Interaction with NEB | ||||
Sequence: PDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDALKGTNDSLMRQMRELEDRFASEASGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVEIATYRKLLEGEESR | ||||||
Region | 269-287 | Coil 2A | ||||
Sequence: DLTAALRDIRAQYETIAAK | ||||||
Region | 288-295 | Linker 2 | ||||
Sequence: NISEAEEW | ||||||
Region | 296-412 | Coil 2B | ||||
Sequence: YKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDALKGTNDSLMRQMRELEDRFASEASGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVEIATYRKLLEGE | ||||||
Region | 413-470 | Tail | ||||
Sequence: ESRINLPIQTYSALNFRETSPEQRGSEVHTKKTVMIKTIETRDGEVVSEATQQQHEVL | ||||||
Region | 438-453 | Interaction with CRYAB | ||||
Sequence: SEVHTKKTVMIKTIET |
Sequence similarities
Belongs to the intermediate filament family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length470
- Mass (Da)53,536
- Last updated2007-01-23 v3
- Checksum1B5D9EA93C3BB319
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 23-25 | in Ref. 1 and 2; AAA99221 | ||||
Sequence: GFP → VFS | ||||||
Sequence conflict | 39 | in Ref. 1 and 2; AAA99221 | ||||
Sequence: G → P | ||||||
Sequence conflict | 119-123 | in Ref. 1 and 2; AAA99221 | ||||
Sequence: FANYI → SPIYM | ||||||
Sequence conflict | 134 | in Ref. 1, 2; AAA99221 and 3; AAC50680 | ||||
Sequence: Missing |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M63391 EMBL· GenBank· DDBJ | AAA99221.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U59167 EMBL· GenBank· DDBJ | AAC50680.1 EMBL· GenBank· DDBJ | mRNA | ||
AF055081 EMBL· GenBank· DDBJ | AAC39938.1 EMBL· GenBank· DDBJ | mRNA | ||
AF055082 EMBL· GenBank· DDBJ | AAC39939.1 EMBL· GenBank· DDBJ | mRNA | ||
AF055083 EMBL· GenBank· DDBJ | AAC39940.1 EMBL· GenBank· DDBJ | mRNA | ||
AF137053 EMBL· GenBank· DDBJ | AAF15400.1 EMBL· GenBank· DDBJ | mRNA | ||
AF486807 EMBL· GenBank· DDBJ | AAL93205.1 EMBL· GenBank· DDBJ | mRNA | ||
AF487828 EMBL· GenBank· DDBJ | AAL99078.1 EMBL· GenBank· DDBJ | mRNA | ||
AF521879 EMBL· GenBank· DDBJ | AAN15036.1 EMBL· GenBank· DDBJ | mRNA | ||
AF527578 EMBL· GenBank· DDBJ | AAN37810.1 EMBL· GenBank· DDBJ | mRNA | ||
AY083345 EMBL· GenBank· DDBJ | AAL99215.1 EMBL· GenBank· DDBJ | mRNA | ||
AY114212 EMBL· GenBank· DDBJ | AAM47026.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY125465 EMBL· GenBank· DDBJ | AAM95238.1 EMBL· GenBank· DDBJ | mRNA | ||
BC032116 EMBL· GenBank· DDBJ | AAH32116.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ132926 EMBL· GenBank· DDBJ | CAB62389.1 EMBL· GenBank· DDBJ | mRNA |