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P17661 (DESM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Desmin
Gene names
Name:DES
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length470 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Desmin are class-III intermediate filaments found in muscle cells. In adult striated muscle they form a fibrous network connecting myofibrils to each other and to the plasma membrane from the periphery of the Z-line structures.

Subunit structure

Homopolymer. Interacts with DST By similarity. Interacts with MTM1. Ref.12

Subcellular location

Cytoplasm.

Post-translational modification

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

Involvement in disease

Myopathy, myofibrillar, 1 (MFM1) [MIM:601419]: A neuromuscular disorder characterized by skeletal muscle weakness associated with cardiac conduction blocks, arrhythmias, restrictive heart failure, and by myofibrillar destruction with intracytoplasmic accumulation of desmin-reactive deposits in cardiac and skeletal muscle cells.
Note: 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 (Ref.30). Ref.4 Ref.6 Ref.7 Ref.9 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.28 Ref.29 Ref.30 Ref.31 Ref.33 Ref.34

Cardiomyopathy, dilated 1I (CMD1I) [MIM:604765]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5

Neurogenic scapuloperoneal syndrome Kaeser type (Kaeser syndrome) [MIM:181400]: Autosomal 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Limb-girdle muscular dystrophy 2R (LGMD2R) [MIM:615325]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15

Sequence similarities

Belongs to the intermediate filament family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 470470Desmin
PRO_0000063771

Regions

Region1 – 108108Head
Region109 – 412304Rod
Region109 – 14133Coil 1A
Region142 – 15110Linker 1
Region152 – 252101Coil 1B
Region253 – 26816Linker 12
Region269 – 28719Coil 2A
Region288 – 2958Linker 2
Region296 – 412117Coil 2B
Region413 – 47058Tail

Amino acid modifications

Modified residue121Phosphoserine; by AURKB Ref.10
Modified residue171Phosphothreonine; by AURKB Ref.10
Modified residue581ADP-ribosylarginine By similarity
Modified residue601Phosphoserine; by AURKB Ref.10
Modified residue681Phosphoserine By similarity

Natural variations

Natural variant21S → I in MFM1; entirely similar expression patterns as the wild-type. Ref.23
Corresponds to variant rs58999456 [ dbSNP | Ensembl ].
VAR_042448
Natural variant71S → F in MFM1. Ref.33
VAR_067207
Natural variant131S → F in MFM1; some patients manifest a severe cardiac phenotype with right ventricular predominance. Ref.29 Ref.30
VAR_067208
Natural variant461S → F in MFM1; entirely similar expression patterns as the wild-type. Ref.23
Corresponds to variant rs60794845 [ dbSNP | Ensembl ].
VAR_042449
Natural variant461S → Y in MFM1; entirely similar expression patterns as the wild-type. Ref.23
VAR_042450
Natural variant1161N → S in MFM1; the clinical picture is dominated by arrhythmogenic right ventricular cardiomyopathy and terminal heart failure; results in impaired filaments formation. Ref.31
Corresponds to variant rs267607499 [ dbSNP | Ensembl ].
VAR_069191
Natural variant173 – 1797Missing in MFM1; severe form.
VAR_009188
Natural variant2131A → 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. Ref.7 Ref.26 Ref.32 Ref.35
Corresponds to variant rs41272699 [ dbSNP | Ensembl ].
VAR_042451
Natural variant2401Missing in MFM1; the mutant cannot form de novo desmin intermediate filaments causing disruption of the endogenous intermediate filament network and formation of pathologic aggregates. Ref.20
VAR_070101
Natural variant2411K → E Found in a patient with severe arrhythmogenic right ventricular cardiomyopathy also carrying a pathogenic frameshift mutation in PKP2. Ref.35
Corresponds to variant rs201945924 [ dbSNP | Ensembl ].
VAR_069192
Natural variant2451E → D in MFM1.
VAR_042452
Natural variant3371A → P in MFM1; mild adult-onset; unable to form a functional filamentous network. Ref.4 Ref.19
Corresponds to variant rs59962885 [ dbSNP | Ensembl ].
VAR_007900
Natural variant3381L → R in MFM1; results in the formation of a filamentous network disrupted by multiple breaks and clumps or large aggregates. Ref.26
VAR_067209
Natural variant3421N → D in MFM1; unable to form a filamentous network; abolishes binding to MTM1. Ref.7 Ref.12 Ref.19
VAR_042453
Natural variant3451L → P in MFM1; distal onset; incapable of forming filamentous networks. Ref.9
Corresponds to variant rs57639980 [ dbSNP | Ensembl ].
VAR_009189
Natural variant3501R → 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. Ref.24 Ref.27
Corresponds to variant rs57965306 [ dbSNP | Ensembl ].
VAR_042454
Natural variant3551R → P in MFM1. Ref.25
Corresponds to variant rs61368398 [ dbSNP | Ensembl ].
VAR_042455
Natural variant3571A → P in MFM1; unable to polymerize and form an intracellular filamentous network; abolishes binding to MTM1. Ref.7 Ref.12 Ref.22
Corresponds to variant rs58898021 [ dbSNP | Ensembl ].
VAR_042456
Natural variant359 – 3613Missing in MFM1.
VAR_018769
Natural variant3601A → 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. Ref.4 Ref.12 Ref.19 Ref.26
VAR_007901
Natural variant3661Missing in MFM1. Ref.7
VAR_018770
Natural variant3701L → P in MFM1; unable to polymerize and form an intracellular filamentous network; does not affect binding to MTM1. Ref.7 Ref.12 Ref.22
Corresponds to variant rs59308628 [ dbSNP | Ensembl ].
VAR_042457
Natural variant3851L → P in MFM1. Ref.18
Corresponds to variant rs57955682 [ dbSNP | Ensembl ].
VAR_018771
Natural variant3891Q → P in MFM1. Ref.6
Corresponds to variant rs28930075 [ dbSNP | Ensembl ].
VAR_018772
Natural variant3931N → 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. Ref.4 Ref.19 Ref.26
VAR_007902
Natural variant3991D → Y in MFM1; results in the formation of a filamentous network disrupted by multiple breaks and clumps or large aggregates. Ref.26
VAR_067210
Natural variant4011E → K in MFM1; results in the formation of a filamentous network disrupted by multiple breaks and clumps or large aggregates. Ref.26
VAR_067211
Natural variant4061R → W in MFM1; unable to form a filamentous network. Ref.17 Ref.19
Corresponds to variant rs61726465 [ dbSNP | Ensembl ].
VAR_042458
Natural variant4191P → S in MFM1; found in a family with myofibrillar myopathy and arrhythmogenic right ventricular cardiomyopathy. Ref.34
VAR_069074
Natural variant4421T → I in MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions, indicating an inherent incompaibility of mutant and wild-type protein to form mixed filaments. Ref.28
VAR_042459
Natural variant4491K → M in MFM1.
VAR_042460
Natural variant4491K → T in MFM1; entirely similar expression patterns as the wild-type. Ref.23
VAR_042461
Natural variant4511I → M in CMD1I and MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions, indicating an inherent incompaibility of mutant and wild-type protein to form mixed filaments. Ref.5 Ref.19 Ref.28
Corresponds to variant rs121913002 [ dbSNP | Ensembl ].
VAR_018773
Natural variant4541R → W in MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions, indicating an inherent incompaibility of mutant and wild-type protein to form mixed filaments. Ref.28 Ref.33
VAR_042462
Natural variant4601S → I in MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions, indicating an inherent incompaibility of mutant and wild-type protein to form mixed filaments. Ref.28
VAR_042463

Experimental info

Sequence conflict23 – 253GFP → VFS Ref.1
Sequence conflict23 – 253GFP → VFS in AAA99221. Ref.2
Sequence conflict391G → P Ref.1
Sequence conflict391G → P in AAA99221. Ref.2
Sequence conflict119 – 1235FANYI → SPIYM Ref.1
Sequence conflict119 – 1235FANYI → SPIYM in AAA99221. Ref.2
Sequence conflict1341Missing Ref.1
Sequence conflict1341Missing in AAA99221. Ref.2
Sequence conflict1341Missing in AAC50680. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P17661 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 1B5D9EA93C3BB319

FASTA47053,536
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MSQAYSSSQR VSSYRRTFGG APGFPLGSPL SSPVFPRAGF GSKGSSSSVT SRVYQVSRTS 

        70         80         90        100        110        120 
GGAGGLGSLR ASRLGTTRTP SSYGAGELLD FSLADAVNQE FLTTRTNEKV ELQELNDRFA 

       130        140        150        160        170        180 
NYIEKVRFLE QQNAALAAEV NRLKGREPTR VAELYEEELR ELRRQVEVLT NQRARVDVER 

       190        200        210        220        230        240 
DNLLDDLQRL KAKLQEEIQL KEEAENNLAA FRADVDAATL ARIDLERRIE SLNEEIAFLK 

       250        260        270        280        290        300 
KVHEEEIREL QAQLQEQQVQ VEMDMSKPDL TAALRDIRAQ YETIAAKNIS EAEEWYKSKV 

       310        320        330        340        350        360 
SDLTQAANKN NDALRQAKQE MMEYRHQIQS YTCEIDALKG TNDSLMRQMR ELEDRFASEA 

       370        380        390        400        410        420 
SGYQDNIARL EEEIRHLKDE MARHLREYQD LLNVKMALDV EIATYRKLLE GEESRINLPI 

       430        440        450        460        470 
QTYSALNFRE TSPEQRGSEV HTKKTVMIKT IETRDGEVVS EATQQQHEVL 

« Hide

References

« Hide 'large scale' references
[1]"Human desmin-coding gene: complete nucleotide sequence, characterization and regulation of expression during myogenesis and development."
Li Z., Lilienbaum A., Butler-Browne G., Paulin D.
Gene 78:243-254(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"High level desmin expression depends on a muscle-specific enhancer."
Li Z., Paulin D.
J. Biol. Chem. 266:6562-6570(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Human desmin gene: cDNA sequence, regional localization and exclusion of the locus in a familial desmin-related myopathy."
Vicart P., Dupret J.-M., Hazan J., Li Z., Gyapay G., Krishnamoorthy R., Weissenbach J., Fardeau M., Paulin D.
Hum. Genet. 98:422-429(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Muscle.
[4]"Missense mutations in desmin associated with familial cardiac and skeletal myopathy."
Goldfarb L.G., Park K.-Y., Cervenakova L., Gorokhova S., Lee H.-S., Vasconcelos O., Nagle J.W., Semino-Mora C., Sivakumar K., Dalakas M.C.
Nat. Genet. 19:402-403(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS MFM1 PRO-337; PRO-360 AND ILE-393.
[5]"Desmin mutation responsible for idiopathic dilated cardiomyopathy."
Li D., Tapscoft T., Gonzalez O., Burch P.E., Quinones M.A., Zoghbi W.A., Hill R., Bachinski L.L., Mann D.L., Roberts R.
Circulation 100:461-464(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT CMD1I MET-451.
[6]"Structural and functional analysis of a new desmin variant causing desmin-related myopathy."
Goudeau B., Dagvadorj A., Rodrigues-Lima F., Nedellec P., Casteras-Simon M., Perret E., Langlois S., Goldfarb L., Vicart P.
Hum. Mutat. 18:388-396(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT MFM1 PRO-389.
[7]"Small deletions disturb desmin architecture leading to breakdown of muscle cells and development of skeletal or cardioskeletal myopathy."
Kaminska A., Strelkov S.V., Goudeau B., Olive M., Dagvadorj A., Fidzianska A., Simon-Casteras M., Shatunov A., Dalakas M.C., Ferrer I., Kwiecinski H., Vicart P., Goldfarb L.G.
Hum. Genet. 114:306-313(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS MFM1 ASP-342; PRO-357; 359-GLU--SER-361 DEL; ASN-366 DEL AND PRO-370, VARIANT VAL-213.
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Muscle.
[9]"A missense mutation in the desmin rod domain is associated with autosomal dominant distal myopathy, and exerts a dominant negative effect on filament formation."
Sjoeberg G., Saavedra-Matiz C.A., Rosen D.R., Wijsman E.M., Borg K., Horowitz S.H., Sejersen T.
Hum. Mol. Genet. 8:2191-2198(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 337-353, VARIANT MFM1 PRO-345, CHARACTERIZATION OF VARIANT MFM1 PRO-345.
Tissue: Skeletal muscle.
[10]"Functional significance of the specific sites phosphorylated in desmin at cleavage furrow: Aurora-B may phosphorylate and regulate type III intermediate filaments during cytokinesis coordinatedly with Rho-kinase."
Kawajiri A., Yasui Y., Goto H., Tatsuka M., Takahashi M., Nagata K., Inagaki M.
Mol. Biol. Cell 14:1489-1500(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-12; THR-17 AND SER-60.
[11]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Myotubularin controls desmin intermediate filament architecture and mitochondrial dynamics in human and mouse skeletal muscle."
Hnia K., Tronchere H., Tomczak K.K., Amoasii L., Schultz P., Beggs A.H., Payrastre B., Mandel J.L., Laporte J.
J. Clin. Invest. 121:70-85(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MTM1, CHARACTERIZATION OF VARIANTS ASP-342; PRO-357; PRO-360 AND PRO-370.
[13]"Desmin myopathy."
Goldfarb L.G., Vicart P., Goebel H.H., Dalakas M.C.
Brain 127:723-734(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS MFM1.
[14]"Desminopathies in muscle disease."
Paulin D., Huet A., Khanamyrian L., Xue Z.
J. Pathol. 204:418-427(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS MFM1.
[15]"A novel desmin mutation leading to autosomal recessive limb-girdle muscular dystrophy: distinct histopathological outcomes compared with desminopathies."
Cetin N., Balci-Hayta B., Gundesli H., Korkusuz P., Purali N., Talim B., Tan E., Selcen D., Erdem-Ozdamar S., Dincer P.
J. Med. Genet. 50:437-443(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN LGMD2R.
[16]"A dysfunctional desmin mutation in a patient with severe generalized myopathy."
Munoz-Marmol A.M., Strasser G., Isamat M., Coulombe P.A., Yang Y., Roca X., Vela E., Mate J.L., Coll J., Fernandez-Figueras M.T., Navas-Palacios J.J., Ariza A., Fuchs E.
Proc. Natl. Acad. Sci. U.S.A. 95:11312-11317(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MFM1 173-ARG--GLU-179 DEL.
[17]"Sporadic cardiac and skeletal myopathy caused by a de novo desmin mutation."
Park K.-Y., Dalakas M.C., Semino-Mora C., Lee H.-S., Litvak S., Takeda K., Ferrans V.J., Goldfarb L.G.
Clin. Genet. 57:423-429(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MFM1 TRP-406.
[18]"A novel de novo mutation in the desmin gene causes desmin myopathy with toxic aggregates."
Sugawara M., Kato K., Komatsu M., Wada C., Kawamura K., Shindo P.S., Yoshioka P.N., Tanaka K., Watanabe S., Toyoshima I.
Neurology 55:986-990(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MFM1 PRO-385.
[19]"Desmin myopathy, a skeletal myopathy with cardiomyopathy caused by mutations in the desmin gene."
Dalakas M.C., Park K.-Y., Semino-Mora C., Lee H.S., Sivakumar K., Goldfarb L.G.
N. Engl. J. Med. 342:770-780(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MFM1 PRO-337; ASP-342; PRO-360; ILE-393; TRP-406 AND MET-451, CHARACTERIZATION OF VARIANTS MFM1 PRO-337; ASP-342; PRO-360; ILE-393; TRP-406 AND MET-451.
[20]"On noxious desmin: functional effects of a novel heterozygous desmin insertion mutation on the extrasarcomeric desmin cytoskeleton and mitochondria."
Schroeder R., Goudeau B., Simon M.C., Fischer D., Eggermann T., Clemen C.S., Li Z., Reimann J., Xue Z., Rudnik-Schoeneborn S., Zerres K., van der Ven P.F., Fuerst D.O., Kunz W.S., Vicart P.
Hum. Mol. Genet. 12:657-669(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MFM1 LYS-240 DEL, CHARACTERIZATION OF VARIANT MFM1 LYS-240 DEL.
[21]Erratum
Schroeder R., Goudeau B., Simon M.C., Fischer D., Eggermann T., Clemen C.S., Li Z., Reimann J., Xue Z., Rudnik-Schoeneborn S., Zerres K., van der Ven P.F., Fuerst D.O., Kunz W.S., Vicart P.
Hum. Mol. Genet. 16:2989-2990(2003)
[22]"Respiratory insufficiency in desminopathy patients caused by introduction of proline residues in desmin C-terminal alpha-helical segment."
Dagvadorj A., Goudeau B., Hilton-Jones D., Blancato J.K., Shatunov A., Simon-Casteras M., Squier W., Nagle J.W., Goldfarb L.G., Vicart P.
Muscle Nerve 27:669-675(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MFM1 PRO-357 AND PRO-370, CHARACTERIZATION OF VARIANTS MFM1 PRO-357 AND PRO-370.
[23]"Myofibrillar myopathy: clinical, morphological and genetic studies in 63 patients."
Selcen D., Ohno K., Engel A.G.
Brain 127:439-451(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MFM1 ILE-2; TYR-46; PHE-46 AND THR-449, CHARACTERIZATION OF VARIANTS MFM1 ILE-2; TYR-46; PHE-46 AND THR-449.
[24]"Pathogenic effects of a novel heterozygous R350P desmin mutation on the assembly of desmin intermediate filaments in vivo and in vitro."
Baer H., Fischer D., Goudeau B., Kley R.A., Clemen C.S., Vicart P., Herrmann H., Vorgerd M., Schroeder R.
Hum. Mol. Genet. 14:1251-1260(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MFM1 PRO-350, CHARACTERIZATION OF VARIANT MFM1 PRO-350.
[25]"A novel desmin R355P mutation causes cardiac and skeletal myopathy."
Fidzianska A., Kotowicz J., Sadowska M., Goudeau B., Walczak E., Vicart P., Hausmanowa-Petrusewicz I.
Neuromuscul. Disord. 15:525-531(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MFM1 PRO-355.
[26]"Variable pathogenic potentials of mutations located in the desmin alpha-helical domain."
Goudeau B., Rodrigues-Lima F., Fischer D., Casteras-Simon M., Sambuughin N., de Visser M., Laforet P., Ferrer X., Chapon F., Sjoberg G., Kostareva A., Sejersen T., Dalakas M.C., Goldfarb L.G., Vicart P.
Hum. Mutat. 27:906-913(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MFM1 ARG-338; TYR-399 AND LYS-401, VARIANT VAL-213, CHARACTERIZATION OF VARIANTS MFM1 ARG-338; PRO-360; ILE-393; TYR-399 AND LYS-401, CHARACTERIZATION OF VARIANT VAL-213.
[27]"Scapuloperoneal syndrome type Kaeser and a wide phenotypic spectrum of adult-onset, dominant myopathies are associated with the desmin mutation R350P."
Walter M.C., Reilich P., Huebner A., Fischer D., Schroeder R., Vorgerd M., Kress W., Born C., Schoser B.G., Krause K.H., Klutzny U., Bulst S., Frey J.R., Lochmueller H.
Brain 130:1485-1496(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT KAESER SYNDROME PRO-350.
[28]"Conspicuous involvement of desmin tail mutations in diverse cardiac and skeletal myopathies."
Baer H., Goudeau B., Waelde S., Casteras-Simon M., Muecke N., Shatunov A., Goldberg Y.P., Clarke C., Holton J.L., Eymard B., Katus H.A., Fardeau M., Goldfarb L., Vicart P., Herrmann H.
Hum. Mutat. 28:374-386(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MFM1 ILE-442; TRP-454 AND ILE-460, CHARACTERIZATION OF VARIANTS MFM1 ILE-442; MET-451; TRP-454 AND ILE-460.
[29]"Characterization of a novel S13F desmin mutation associated with desmin myopathy and heart block in a Chinese family."
Pica E.C., Kathirvel P., Pramono Z.A., Lai P.S., Yee W.C.
Neuromuscul. Disord. 18:178-182(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MFM1 PHE-13.
[30]"Severe cardiac phenotype with right ventricular predominance in a large cohort of patients with a single missense mutation in the DES gene."
van Tintelen J.P., Van Gelder I.C., Asimaki A., Suurmeijer A.J., Wiesfeld A.C., Jongbloed J.D., van den Wijngaard A., Kuks J.B., van Spaendonck-Zwarts K.Y., Notermans N., Boven L., van den Heuvel F., Veenstra-Knol H.E., Saffitz J.E., Hofstra R.M., van den Berg M.P.
Heart Rhythm 6:1574-1583(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MFM1 PHE-13, PHENOTYPIC VARIABILITY IN MFM1 PATIENTS.
[31]"De novo desmin-mutation N116S is associated with arrhythmogenic right ventricular cardiomyopathy."
Klauke B., Kossmann S., Gaertner A., Brand K., Stork I., Brodehl A., Dieding M., Walhorn V., Anselmetti D., Gerdes D., Bohms B., Schulz U., Zu Knyphausen E., Vorgerd M., Gummert J., Milting H.
Hum. Mol. Genet. 19:4595-4607(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MFM1 SER-116, CHARACTERIZATION OF VARIANT MFM1 SER-116.
[32]"Desmin A213V substitution represents a rare polymorphism but not a mutation and is more prevalent in patients with heart dilation of various origins."
Kostareva A., Sjoberg G., Gudkova A., Smolina N., Semernin E., Shlyakhto E., Sejersen T.
Acta Myol. 30:42-45(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT VAL-213.
[33]"Clinical, morphological and genetic studies in a cohort of 21 patients with myofibrillar myopathy."
Vattemi G., Neri M., Piffer S., Vicart P., Gualandi F., Marini M., Guglielmi V., Filosto M., Tonin P., Ferlini A., Tomelleri G.
Acta Myol. 30:121-126(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MFM1 PHE-7 AND TRP-454.
[34]"Autosomal dominant myofibrillar myopathy with arrhythmogenic right ventricular cardiomyopathy 7 is caused by a DES mutation."
Hedberg C., Melberg A., Kuhl A., Jenne D., Oldfors A.
Eur. J. Hum. Genet. 20:984-985(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MFM1 SER-419.
[35]"Desmin mutations and arrhythmogenic right ventricular cardiomyopathy."
Lorenzon A., Beffagna G., Bauce B., De Bortoli M., Li Mura I.E., Calore M., Dazzo E., Basso C., Nava A., Thiene G., Rampazzo A.
Am. J. Cardiol. 111:400-405(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS VAL-213 AND GLU-241.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRDMHU. JE0063.
RefSeqNP_001918.3. NM_001927.3.
UniGeneHs.594952.

3D structure databases

ProteinModelPortalP17661.
SMRP17661. Positions 104-253, 268-411.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108038. 28 interactions.
IntActP17661. 12 interactions.
MINTMINT-215829.

PTM databases

PhosphoSiteP17661.

Polymorphism databases

DMDM6686280.

2D gel databases

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

Proteomic databases

PaxDbP17661.
PRIDEP17661.

Protocols and materials databases

DNASU1674.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373960; ENSP00000363071; ENSG00000175084.
GeneID1674.
KEGGhsa:1674.
UCSCuc002vll.3. human.

Organism-specific databases

CTD1674.
GeneCardsGC02P220283.
HGNCHGNC:2770. DES.
HPACAB000034.
HPA018803.
MIM125660. gene.
181400. phenotype.
601419. phenotype.
604765. phenotype.
615325. phenotype.
neXtProtNX_P17661.
Orphanet34517. 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.
PharmGKBPA27253.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG147125.
HOVERGENHBG013015.
InParanoidP17661.
KOK07610.
OMASSEMHSK.
OrthoDBEOG7FV3Q8.
PhylomeDBP17661.
TreeFamTF330122.

Enzyme and pathway databases

ReactomeREACT_17044. Muscle contraction.

Gene expression databases

ArrayExpressP17661.
BgeeP17661.
GenevestigatorP17661.

Family and domain databases

InterProIPR027698. DES.
IPR001664. IF.
IPR006821. Intermed_filament_DNA-bd.
IPR018039. Intermediate_filament_CS.
[Graphical view]
PANTHERPTHR23239. PTHR23239. 1 hit.
PTHR23239:SF28. PTHR23239:SF28. 1 hit.
PfamPF00038. Filament. 1 hit.
PF04732. Filament_head. 1 hit.
[Graphical view]
PROSITEPS00226. IF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDES. human.
GeneWikiDesmin.
GenomeRNAi1674.
NextBio6888.
PROP17661.
SOURCESearch...

Entry information

Entry nameDESM_HUMAN
AccessionPrimary (citable) accession number: P17661
Secondary accession number(s): Q15787 expand/collapse secondary AC list , Q549R7, Q549R8, Q549R9, Q8IZR1, Q8IZR6, Q8NES2, Q8NEU6, Q8TAC4, Q8TCX2, Q8TD99, Q9UHN5, Q9UJ80
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 152 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM