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Desmin

 DESM_HUMAN              Reviewed;         470 AA.
P17661; Q15787; Q549R7; Q549R8; Q549R9; Q8IZR1; Q8IZR6; Q8NES2;
Q8NEU6; Q8TAC4; Q8TCX2; Q8TD99; Q9UHN5; Q9UJ80;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 190.
RecName: Full=Desmin;
Name=DES;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2673923; DOI=10.1016/0378-1119(89)90227-8;
Li Z., Lilienbaum A., Butler-Browne G., Paulin D.;
"Human desmin-coding gene: complete nucleotide sequence,
characterization and regulation of expression during myogenesis and
development.";
Gene 78:243-254(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2007603;
Li Z., Paulin D.;
"High level desmin expression depends on a muscle-specific enhancer.";
J. Biol. Chem. 266:6562-6570(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Muscle;
PubMed=8792816; DOI=10.1007/s004390050233;
Vicart P., Dupret J.-M., Hazan J., Li Z., Gyapay G.,
Krishnamoorthy R., Weissenbach J., Fardeau M., Paulin D.;
"Human desmin gene: cDNA sequence, regional localization and exclusion
of the locus in a familial desmin-related myopathy.";
Hum. Genet. 98:422-429(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS MFM1 PRO-337; PRO-360 AND
ILE-393.
PubMed=9697706; DOI=10.1038/1300;
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.;
"Missense mutations in desmin associated with familial cardiac and
skeletal myopathy.";
Nat. Genet. 19:402-403(1998).
[5]
NUCLEOTIDE SEQUENCE [MRNA], VARIANT CMD1I MET-451, AND INVOLVEMENT IN
CMD1I.
PubMed=10430757; DOI=10.1161/01.CIR.100.5.461;
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.;
"Desmin mutation responsible for idiopathic dilated cardiomyopathy.";
Circulation 100:461-464(1999).
[6]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT MFM1 PRO-389.
PubMed=11668632; DOI=10.1002/humu.1210;
Goudeau B., Dagvadorj A., Rodrigues-Lima F., Nedellec P.,
Casteras-Simon M., Perret E., Langlois S., Goldfarb L., Vicart P.;
"Structural and functional analysis of a new desmin variant causing
desmin-related myopathy.";
Hum. Mutat. 18:388-396(2001).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS MFM1 ASP-342; PRO-357;
359-GLU--SER-361 DEL; ASN-366 DEL AND PRO-370, AND VARIANT VAL-213.
PubMed=14648196; DOI=10.1007/s00439-003-1057-7;
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.;
"Small deletions disturb desmin architecture leading to breakdown of
muscle cells and development of skeletal or cardioskeletal myopathy.";
Hum. Genet. 114:306-313(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 337-353, VARIANT MFM1 PRO-345, AND
CHARACTERIZATION OF VARIANT MFM1 PRO-345.
TISSUE=Skeletal muscle;
PubMed=10545598; DOI=10.1093/hmg/8.12.2191;
Sjoeberg G., Saavedra-Matiz C.A., Rosen D.R., Wijsman E.M., Borg K.,
Horowitz S.H., Sejersen T.;
"A missense mutation in the desmin rod domain is associated with
autosomal dominant distal myopathy, and exerts a dominant negative
effect on filament formation.";
Hum. Mol. Genet. 8:2191-2198(1999).
[10]
PHOSPHORYLATION AT THR-17; THR-76 AND THR-77.
PubMed=9875213; DOI=10.1006/bbrc.1998.9732;
Inada H., Goto H., Tanabe K., Nishi Y., Kaibuchi K., Inagaki M.;
"Rho-associated kinase phosphorylates desmin, the myogenic
intermediate filament protein, at unique amino-terminal sites.";
Biochem. Biophys. Res. Commun. 253:21-25(1998).
[11]
PHOSPHORYLATION AT SER-12; THR-17 AND SER-60.
PubMed=12686604; DOI=10.1091/mbc.E02-09-0612;
Kawajiri A., Yasui Y., Goto H., Tatsuka M., Takahashi M., Nagata K.,
Inagaki M.;
"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.";
Mol. Biol. Cell 14:1489-1500(2003).
[12]
INTERACTION WITH EPPK1.
PubMed=16923132; DOI=10.1111/j.1346-8138.2006.00127.x;
Wang W., Sumiyoshi H., Yoshioka H., Fujiwara S.;
"Interactions between epiplakin and intermediate filaments.";
J. Dermatol. 33:518-527(2006).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[14]
INTERACTION WITH MTM1, CHARACTERIZATION OF VARIANTS ASP-342; PRO-357;
PRO-360 AND PRO-370, AND SUBUNIT.
PubMed=21135508; DOI=10.1172/JCI44021;
Hnia K., Tronchere H., Tomczak K.K., Amoasii L., Schultz P.,
Beggs A.H., Payrastre B., Mandel J.L., Laporte J.;
"Myotubularin controls desmin intermediate filament architecture and
mitochondrial dynamics in human and mouse skeletal muscle.";
J. Clin. Invest. 121:70-85(2011).
[15]
REVIEW ON VARIANTS MFM1.
PubMed=14724127; DOI=10.1093/brain/awh033;
Goldfarb L.G., Vicart P., Goebel H.H., Dalakas M.C.;
"Desmin myopathy.";
Brain 127:723-734(2004).
[16]
REVIEW ON VARIANTS MFM1.
PubMed=15495235; DOI=10.1002/path.1639;
Paulin D., Huet A., Khanamyrian L., Xue Z.;
"Desminopathies in muscle disease.";
J. Pathol. 204:418-427(2004).
[17]
INVOLVEMENT IN LGMD2R.
PubMed=23687351; DOI=10.1136/jmedgenet-2012-101487;
Cetin N., Balci-Hayta B., Gundesli H., Korkusuz P., Purali N.,
Talim B., Tan E., Selcen D., Erdem-Ozdamar S., Dincer P.;
"A novel desmin mutation leading to autosomal recessive limb-girdle
muscular dystrophy: distinct histopathological outcomes compared with
desminopathies.";
J. Med. Genet. 50:437-443(2013).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[19]
REVIEW.
PubMed=25358400; DOI=10.1007/s00441-014-2016-4;
Hnia K., Ramspacher C., Vermot J., Laporte J.;
"Desmin in muscle and associated diseases: beyond the structural
function.";
Cell Tissue Res. 360:591-608(2015).
[20]
PHOSPHORYLATION AT SER-32.
PubMed=27565725; DOI=10.1016/j.bbrc.2016.08.122;
Makihara H., Inaba H., Enomoto A., Tanaka H., Tomono Y., Ushida K.,
Goto M., Kurita K., Nishida Y., Kasahara K., Goto H., Inagaki M.;
"Desmin phosphorylation by Cdk1 is required for efficient separation
of desmin intermediate filaments in mitosis and detected in murine
embryonic/newborn muscle and human rhabdomyosarcoma tissues.";
Biochem. Biophys. Res. Commun. 478:1323-1329(2016).
[21]
VARIANT MFM1 173-ARG--GLU-179 DEL.
PubMed=9736733; DOI=10.1073/pnas.95.19.11312;
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.;
"A dysfunctional desmin mutation in a patient with severe generalized
myopathy.";
Proc. Natl. Acad. Sci. U.S.A. 95:11312-11317(1998).
[22]
VARIANT MFM1 TRP-406.
PubMed=10905661; DOI=10.1034/j.1399-0004.2000.570604.x;
Park K.-Y., Dalakas M.C., Semino-Mora C., Lee H.-S., Litvak S.,
Takeda K., Ferrans V.J., Goldfarb L.G.;
"Sporadic cardiac and skeletal myopathy caused by a de novo desmin
mutation.";
Clin. Genet. 57:423-429(2000).
[23]
VARIANT MFM1 PRO-385.
PubMed=11061256; DOI=10.1212/WNL.55.7.986;
Sugawara M., Kato K., Komatsu M., Wada C., Kawamura K., Shindo P.S.,
Yoshioka P.N., Tanaka K., Watanabe S., Toyoshima I.;
"A novel de novo mutation in the desmin gene causes desmin myopathy
with toxic aggregates.";
Neurology 55:986-990(2000).
[24]
VARIANTS MFM1 PRO-337; ASP-342; PRO-360; ILE-393; TRP-406 AND MET-451,
AND CHARACTERIZATION OF VARIANTS MFM1 PRO-337; ASP-342; PRO-360;
ILE-393; TRP-406 AND MET-451.
PubMed=10717012; DOI=10.1056/NEJM200003163421104;
Dalakas M.C., Park K.-Y., Semino-Mora C., Lee H.S., Sivakumar K.,
Goldfarb L.G.;
"Desmin myopathy, a skeletal myopathy with cardiomyopathy caused by
mutations in the desmin gene.";
N. Engl. J. Med. 342:770-780(2000).
[25]
VARIANT MFM1 LYS-240 DEL, AND CHARACTERIZATION OF VARIANT MFM1 LYS-240
DEL.
PubMed=12620971; DOI=10.1093/hmg/ddg060;
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.;
"On noxious desmin: functional effects of a novel heterozygous desmin
insertion mutation on the extrasarcomeric desmin cytoskeleton and
mitochondria.";
Hum. Mol. Genet. 12:657-669(2003).
[26]
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).
[27]
VARIANTS MFM1 PRO-357 AND PRO-370, AND CHARACTERIZATION OF VARIANTS
MFM1 PRO-357 AND PRO-370.
PubMed=12766977; DOI=10.1002/mus.10370;
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.;
"Respiratory insufficiency in desminopathy patients caused by
introduction of proline residues in desmin C-terminal alpha-helical
segment.";
Muscle Nerve 27:669-675(2003).
[28]
VARIANTS MFM1 ILE-2; TYR-46; PHE-46 AND THR-449.
PubMed=14711882; DOI=10.1093/brain/awh052;
Selcen D., Ohno K., Engel A.G.;
"Myofibrillar myopathy: clinical, morphological and genetic studies in
63 patients.";
Brain 127:439-451(2004).
[29]
VARIANT MFM1 PRO-350, AND CHARACTERIZATION OF VARIANT MFM1 PRO-350.
PubMed=15800015; DOI=10.1093/hmg/ddi136;
Baer H., Fischer D., Goudeau B., Kley R.A., Clemen C.S., Vicart P.,
Herrmann H., Vorgerd M., Schroeder R.;
"Pathogenic effects of a novel heterozygous R350P desmin mutation on
the assembly of desmin intermediate filaments in vivo and in vitro.";
Hum. Mol. Genet. 14:1251-1260(2005).
[30]
VARIANT MFM1 PRO-355.
PubMed=16009553; DOI=10.1016/j.nmd.2005.05.006;
Fidzianska A., Kotowicz J., Sadowska M., Goudeau B., Walczak E.,
Vicart P., Hausmanowa-Petrusewicz I.;
"A novel desmin R355P mutation causes cardiac and skeletal myopathy.";
Neuromuscul. Disord. 15:525-531(2005).
[31]
VARIANTS MFM1 CYS-16; TRP-406 AND ILE-453.
PubMed=16376610; DOI=10.1016/j.ejheart.2005.11.003;
Arbustini E., Pasotti M., Pilotto A., Pellegrini C., Grasso M.,
Previtali S., Repetto A., Bellini O., Azan G., Scaffino M.,
Campana C., Piccolo G., Vigano M., Tavazzi L.;
"Desmin accumulation restrictive cardiomyopathy and atrioventricular
block associated with desmin gene defects.";
Eur. J. Heart Fail. 8:477-483(2006).
[32]
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, AND CHARACTERIZATION OF VARIANT VAL-213.
PubMed=16865695; DOI=10.1002/humu.20351;
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.;
"Variable pathogenic potentials of mutations located in the desmin
alpha-helical domain.";
Hum. Mutat. 27:906-913(2006).
[33]
VARIANT KAESER SYNDROME PRO-350.
PubMed=17439987; DOI=10.1093/brain/awm039;
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.;
"Scapuloperoneal syndrome type Kaeser and a wide phenotypic spectrum
of adult-onset, dominant myopathies are associated with the desmin
mutation R350P.";
Brain 130:1485-1496(2007).
[34]
VARIANTS MFM1 ILE-442; TRP-454 AND ILE-460, AND CHARACTERIZATION OF
VARIANTS MFM1 ILE-442; MET-451; TRP-454 AND ILE-460.
PubMed=17221859; DOI=10.1002/humu.20459;
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.;
"Conspicuous involvement of desmin tail mutations in diverse cardiac
and skeletal myopathies.";
Hum. Mutat. 28:374-386(2007).
[35]
VARIANT MFM1 PHE-13.
PubMed=18061454; DOI=10.1016/j.nmd.2007.09.011;
Pica E.C., Kathirvel P., Pramono Z.A., Lai P.S., Yee W.C.;
"Characterization of a novel S13F desmin mutation associated with
desmin myopathy and heart block in a Chinese family.";
Neuromuscul. Disord. 18:178-182(2008).
[36]
VARIANT MFM1 PHE-13, AND PHENOTYPIC VARIABILITY IN MFM1 PATIENTS.
PubMed=19879535; DOI=10.1016/j.hrthm.2009.07.041;
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.;
"Severe cardiac phenotype with right ventricular predominance in a
large cohort of patients with a single missense mutation in the DES
gene.";
Heart Rhythm 6:1574-1583(2009).
[37]
VARIANT MFM1 SER-116, AND CHARACTERIZATION OF VARIANT MFM1 SER-116.
PubMed=20829228; DOI=10.1093/hmg/ddq387;
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.;
"De novo desmin-mutation N116S is associated with arrhythmogenic right
ventricular cardiomyopathy.";
Hum. Mol. Genet. 19:4595-4607(2010).
[38]
VARIANT VAL-213.
PubMed=21842594;
Kostareva A., Sjoberg G., Gudkova A., Smolina N., Semernin E.,
Shlyakhto E., Sejersen T.;
"Desmin A213V substitution represents a rare polymorphism but not a
mutation and is more prevalent in patients with heart dilation of
various origins.";
Acta Myol. 30:42-45(2011).
[39]
VARIANTS MFM1 PHE-7 AND TRP-454.
PubMed=22106715;
Vattemi G., Neri M., Piffer S., Vicart P., Gualandi F., Marini M.,
Guglielmi V., Filosto M., Tonin P., Ferlini A., Tomelleri G.;
"Clinical, morphological and genetic studies in a cohort of 21
patients with myofibrillar myopathy.";
Acta Myol. 30:121-126(2011).
[40]
VARIANT MFM1 SER-419.
PubMed=22395865; DOI=10.1038/ejhg.2012.39;
Hedberg C., Melberg A., Kuhl A., Jenne D., Oldfors A.;
"Autosomal dominant myofibrillar myopathy with arrhythmogenic right
ventricular cardiomyopathy 7 is caused by a DES mutation.";
Eur. J. Hum. Genet. 20:984-985(2012).
[41]
VARIANTS VAL-213 AND GLU-241.
PubMed=23168288; DOI=10.1016/j.amjcard.2012.10.017;
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.;
"Desmin mutations and arrhythmogenic right ventricular
cardiomyopathy.";
Am. J. Cardiol. 111:400-405(2013).
[42]
VARIANT CMD1I ASP-120, VARIANT ARG-326, CHARACTERIZATION OF VARIANT
CMD1I ASP-120, CHARACTERIZATION OF VARIANT ARG-326, FUNCTION,
SUBCELLULAR LOCATION, AND MUTAGENESIS OF ALA-120.
PubMed=24200904; DOI=10.1161/CIRCGENETICS.113.000103;
Brodehl A., Dieding M., Klauke B., Dec E., Madaan S., Huang T.,
Gargus J., Fatima A., Saric T., Cakar H., Walhorn V., Toensing K.,
Skrzipczyk T., Cebulla R., Gerdes D., Schulz U., Gummert J.,
Svendsen J.H., Olesen M.S., Anselmetti D., Christensen A.H.,
Kimonis V., Milting H.;
"The novel desmin mutant p.A120D impairs filament formation, prevents
intercalated disk localization, and causes sudden cardiac death.";
Circ. Cardiovasc. Genet. 6:615-623(2013).
[43]
CHARACTERIZATION OF VARIANTS MFM1 PHE-46; ASP-245 AND ILE-453, AND
INTERACTION WITH NEB.
PubMed=23615443; DOI=10.1091/mbc.E12-11-0840;
Baker L.K., Gillis D.C., Sharma S., Ambrus A., Herrmann H.,
Conover G.M.;
"Nebulin binding impedes mutant desmin filament assembly.";
Mol. Biol. Cell 24:1918-1932(2013).
[44]
CHARACTERIZATION OF VARIANT KAESER SYNDROME PRO-350, CHARACTERIZATION
OF VARIANT MFM1 PRO-350, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=25394388; DOI=10.1007/s00401-014-1363-2;
Clemen C.S., Stoeckigt F., Strucksberg K.H., Chevessier F., Winter L.,
Schuetz J., Bauer R., Thorweihe J.M., Wenzel D.,
Schloetzer-Schrehardt U., Rasche V., Krsmanovic P., Katus H.A.,
Rottbauer W., Just S., Mueller O.J., Friedrich O., Meyer R.,
Herrmann H., Schrickel J.W., Schroeder R.;
"The toxic effect of R350P mutant desmin in striated muscle of man and
mouse.";
Acta Neuropathol. 129:297-315(2015).
[45]
VARIANT CMD1I PRO-136, CHARACTERIZATION OF VARIANT CMD1I PRO-136,
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=26724190; DOI=10.1016/j.yjmcc.2015.12.015;
Brodehl A., Dieding M., Biere N., Unger A., Klauke B., Walhorn V.,
Gummert J., Schulz U., Linke W.A., Gerull B., Vorgert M.,
Anselmetti D., Milting H.;
"Functional characterization of the novel DES mutation p.L136P
associated with dilated cardiomyopathy reveals a dominant filament
assembly defect.";
J. Mol. Cell. Cardiol. 91:207-214(2016).
[46]
CHARACTERIZATION OF VARIANTS MFM1 ASP-245 AND ILE-453, AND INTERACTION
WITH NEBL.
PubMed=27733623; DOI=10.1091/mbc.E16-04-0237;
Hernandez D.A., Bennett C.M., Dunina-Barkovskaya L., Wedig T.,
Capetanaki Y., Herrmann H., Conover G.M.;
"Nebulette is a powerful cytolinker organizing desmin and actin in
mouse hearts.";
Mol. Biol. Cell 27:3869-3882(2016).
[47]
CHARACTERIZATION OF VARIANTS MFM1 MET-451 AND TRP-454, AND INTERACTION
WITH CRYAB.
PubMed=28470624; DOI=10.1007/s12192-017-0788-7;
Sharma S., Conover G.M., Elliott J.L., Der Perng M., Herrmann H.,
Quinlan R.A.;
"alphaB-crystallin is a sensor for assembly intermediates and for the
subunit topology of desmin intermediate filaments.";
Cell Stress Chaperones 22:613-626(2017).
-!- 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. 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). {ECO:0000250|UniProtKB:P31001,
ECO:0000269|PubMed:24200904, ECO:0000269|PubMed:25394388,
ECO:0000269|PubMed:26724190, ECO:0000303|PubMed:25358400}.
-!- SUBUNIT: 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).
{ECO:0000250|UniProtKB:P31001, ECO:0000269|PubMed:16923132,
ECO:0000269|PubMed:21135508, ECO:0000269|PubMed:23615443,
ECO:0000269|PubMed:27733623, ECO:0000269|PubMed:28470624}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-1055572, EBI-1055572;
Q8TAB5:C1orf216; NbExp=4; IntAct=EBI-1055572, EBI-747505;
O43812:DUX1; NbExp=4; IntAct=EBI-1055572, EBI-11599346;
Q9UBX2:DUX4; NbExp=3; IntAct=EBI-1055572, EBI-11600078;
Q6RFH8:DUX4L9; NbExp=4; IntAct=EBI-1055572, EBI-11599882;
O75923:DYSF; NbExp=3; IntAct=EBI-1055572, EBI-2799016;
Q08426:EHHADH; NbExp=7; IntAct=EBI-1055572, EBI-2339219;
P14136:GFAP; NbExp=6; IntAct=EBI-1055572, EBI-744302;
P40692:MLH1; NbExp=7; IntAct=EBI-1055572, EBI-744248;
Q13496:MTM1; NbExp=13; IntAct=EBI-1055572, EBI-2864109;
P07196:NEFL; NbExp=3; IntAct=EBI-1055572, EBI-475646;
Q6NYC8:PPP1R18; NbExp=5; IntAct=EBI-1055572, EBI-2557469;
P41219:PRPH; NbExp=4; IntAct=EBI-1055572, EBI-752074;
Q7KZS0:UBE2I; NbExp=3; IntAct=EBI-1055572, EBI-10180829;
P08670:VIM; NbExp=4; IntAct=EBI-1055572, EBI-353844;
-!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line
{ECO:0000269|PubMed:24200904, ECO:0000269|PubMed:26724190}.
Cytoplasm {ECO:0000269|PubMed:25394388}. Cell membrane, sarcolemma
{ECO:0000269|PubMed:25394388}. Nucleus
{ECO:0000250|UniProtKB:P31001}. 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).
{ECO:0000250|UniProtKB:P31001, ECO:0000269|PubMed:24200904,
ECO:0000269|PubMed:26724190}.
-!- PTM: ADP-ribosylation prevents ability to form intermediate
filaments. {ECO:0000250|UniProtKB:P48675}.
-!- PTM: 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. {ECO:0000250|UniProtKB:P31001}.
-!- DISEASE: Myopathy, myofibrillar, 1 (MFM1) [MIM:601419]: A form of
myofibrillar myopathy, a group of chronic neuromuscular disorders
characterized at ultrastructural level by disintegration of the
sarcomeric Z disc and myofibrils, and replacement of the normal
myofibrillar markings by small dense granules, or larger hyaline
masses, or amorphous material. MFM1 is characterized by skeletal
muscle weakness associated with cardiac conduction blocks,
arrhythmias, restrictive heart failure, and accumulation of
desmin-reactive deposits in cardiac and skeletal muscle cells.
{ECO:0000269|PubMed:10545598, ECO:0000269|PubMed:10717012,
ECO:0000269|PubMed:10905661, ECO:0000269|PubMed:11061256,
ECO:0000269|PubMed:11668632, ECO:0000269|PubMed:12620971,
ECO:0000269|PubMed:12766977, ECO:0000269|PubMed:14648196,
ECO:0000269|PubMed:14711882, ECO:0000269|PubMed:14724127,
ECO:0000269|PubMed:15495235, ECO:0000269|PubMed:15800015,
ECO:0000269|PubMed:16009553, ECO:0000269|PubMed:16376610,
ECO:0000269|PubMed:16865695, ECO:0000269|PubMed:17221859,
ECO:0000269|PubMed:18061454, ECO:0000269|PubMed:19879535,
ECO:0000269|PubMed:20829228, ECO:0000269|PubMed:22106715,
ECO:0000269|PubMed:22395865, ECO:0000269|PubMed:23615443,
ECO:0000269|PubMed:25394388, ECO:0000269|PubMed:27733623,
ECO:0000269|PubMed:28470624, ECO:0000269|PubMed:9697706,
ECO:0000269|PubMed:9736733}. 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 (PubMed:19879535).
{ECO:0000269|PubMed:19879535}.
-!- DISEASE: 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.
{ECO:0000269|PubMed:10430757, ECO:0000269|PubMed:24200904,
ECO:0000269|PubMed:26724190}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: 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.
{ECO:0000269|PubMed:17439987, ECO:0000269|PubMed:25394388}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: 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. {ECO:0000269|PubMed:23687351}. Note=The disease is caused
by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the intermediate filament family.
{ECO:0000255|PROSITE-ProRule:PRU01188}.
-!- WEB RESOURCE: Name=Human Intermediate Filament Mutation Database;
URL="http://www.interfil.org";
-!- WEB RESOURCE: Name=Wikipedia; Note=Desmin entry;
URL="https://en.wikipedia.org/wiki/Desmin";
-----------------------------------------------------------------------
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EMBL; M63391; AAA99221.1; -; Genomic_DNA.
EMBL; U59167; AAC50680.1; -; mRNA.
EMBL; AF055081; AAC39938.1; -; mRNA.
EMBL; AF055082; AAC39939.1; -; mRNA.
EMBL; AF055083; AAC39940.1; -; mRNA.
EMBL; AF137053; AAF15400.1; -; mRNA.
EMBL; AF486807; AAL93205.1; -; mRNA.
EMBL; AF487828; AAL99078.1; -; mRNA.
EMBL; AF521879; AAN15036.1; -; mRNA.
EMBL; AF527578; AAN37810.1; -; mRNA.
EMBL; AY083345; AAL99215.1; -; mRNA.
EMBL; AY114212; AAM47026.1; -; Genomic_DNA.
EMBL; AY125465; AAM95238.1; -; mRNA.
EMBL; BC032116; AAH32116.1; -; mRNA.
EMBL; AJ132926; CAB62389.1; -; mRNA.
CCDS; CCDS33383.1; -.
PIR; JE0063; DMHU.
RefSeq; NP_001918.3; NM_001927.3.
UniGene; Hs.594952; -.
ProteinModelPortal; P17661; -.
SMR; P17661; -.
BioGrid; 108038; 43.
IntAct; P17661; 52.
MINT; MINT-215829; -.
STRING; 9606.ENSP00000363071; -.
iPTMnet; P17661; -.
PhosphoSitePlus; P17661; -.
SwissPalm; P17661; -.
BioMuta; DES; -.
DMDM; 6686280; -.
REPRODUCTION-2DPAGE; IPI00465084; -.
REPRODUCTION-2DPAGE; P17661; -.
SWISS-2DPAGE; P17661; -.
UCD-2DPAGE; P17661; -.
EPD; P17661; -.
PaxDb; P17661; -.
PeptideAtlas; P17661; -.
PRIDE; P17661; -.
DNASU; 1674; -.
Ensembl; ENST00000373960; ENSP00000363071; ENSG00000175084.
GeneID; 1674; -.
KEGG; hsa:1674; -.
CTD; 1674; -.
DisGeNET; 1674; -.
EuPathDB; HostDB:ENSG00000175084.11; -.
GeneCards; DES; -.
GeneReviews; DES; -.
HGNC; HGNC:2770; DES.
HPA; CAB000034; -.
HPA; HPA018803; -.
MalaCards; DES; -.
MIM; 125660; gene.
MIM; 181400; phenotype.
MIM; 601419; phenotype.
MIM; 604765; phenotype.
MIM; 615325; phenotype.
neXtProt; NX_P17661; -.
OpenTargets; ENSG00000175084; -.
Orphanet; 34517; Autosomal dominant limb-girdle muscular dystrophy type 1E.
Orphanet; 363543; Autosomal recessive limb-girdle muscular dystrophy due to desmin deficiency.
Orphanet; 98909; Desminopathy.
Orphanet; 154; Familial isolated dilated cardiomyopathy.
Orphanet; 85146; Scapuloperoneal amyotrophy.
PharmGKB; PA27253; -.
eggNOG; ENOG410IFZ1; Eukaryota.
eggNOG; ENOG410XRBS; LUCA.
GeneTree; ENSGT00830000128228; -.
HOVERGEN; HBG013015; -.
InParanoid; P17661; -.
KO; K07610; -.
OMA; NQRARVE; -.
OrthoDB; EOG091G12MK; -.
PhylomeDB; P17661; -.
TreeFam; TF330122; -.
Reactome; R-HSA-390522; Striated Muscle Contraction.
SIGNOR; P17661; -.
ChiTaRS; DES; human.
GeneWiki; Desmin; -.
GenomeRNAi; 1674; -.
PRO; PR:P17661; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000175084; -.
ExpressionAtlas; P17661; baseline and differential.
Genevisible; P17661; HS.
GO; GO:0097512; C:cardiac myofibril; IDA:CAFA.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005916; C:fascia adherens; IEA:Ensembl.
GO; GO:0014704; C:intercalated disc; IDA:UniProtKB.
GO; GO:0005882; C:intermediate filament; TAS:ProtInc.
GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0042383; C:sarcolemma; IDA:UniProtKB.
GO; GO:0030018; C:Z disc; IDA:UniProtKB.
GO; GO:0008092; F:cytoskeletal protein binding; IPI:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
GO; GO:0007010; P:cytoskeleton organization; TAS:ProtInc.
GO; GO:0045109; P:intermediate filament organization; IMP:UniProtKB.
GO; GO:0006936; P:muscle contraction; TAS:ProtInc.
GO; GO:0030049; P:muscle filament sliding; TAS:Reactome.
GO; GO:0008016; P:regulation of heart contraction; TAS:ProtInc.
InterPro; IPR027698; DES.
InterPro; IPR001664; IF.
InterPro; IPR006821; Intermed_filament_DNA-bd.
InterPro; IPR018039; Intermediate_filament_CS.
PANTHER; PTHR23239; PTHR23239; 1.
PANTHER; PTHR23239:SF28; PTHR23239:SF28; 1.
Pfam; PF00038; Filament; 1.
Pfam; PF04732; Filament_head; 1.
SMART; SM01391; Filament; 1.
PROSITE; PS00226; IF_ROD_1; 1.
PROSITE; PS51842; IF_ROD_2; 1.
1: Evidence at protein level;
Acetylation; ADP-ribosylation; Cardiomyopathy; Cell membrane;
Coiled coil; Complete proteome; Cytoplasm; Desmin-related myopathy;
Disease mutation; Intermediate filament; Isopeptide bond;
Limb-girdle muscular dystrophy; Membrane; Methylation; Muscle protein;
Myofibrillar myopathy; Nitration; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P08670}.
CHAIN 2 470 Desmin.
/FTId=PRO_0000063771.
DOMAIN 108 416 IF rod. {ECO:0000255|PROSITE-
ProRule:PRU01188}.
REGION 2 108 Head.
REGION 109 141 Coil 1A.
REGION 142 151 Linker 1.
REGION 152 252 Coil 1B.
REGION 253 268 Linker 12.
REGION 268 415 Interaction with NEB.
{ECO:0000269|PubMed:23615443}.
REGION 269 287 Coil 2A.
REGION 288 295 Linker 2.
REGION 296 412 Coil 2B.
REGION 413 470 Tail.
REGION 438 453 Interaction with CRYAB.
{ECO:0000269|PubMed:28470624}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 7 7 Phosphoserine; by CDK1.
{ECO:0000250|UniProtKB:P31001}.
MOD_RES 8 8 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 12 12 Phosphoserine; by AURKB.
{ECO:0000269|PubMed:12686604}.
MOD_RES 13 13 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 14 14 Nitrated tyrosine.
{ECO:0000250|UniProtKB:P21807}.
MOD_RES 16 16 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P31001}.
MOD_RES 17 17 Phosphothreonine; by AURKB and ROCK1.
{ECO:0000269|PubMed:12686604,
ECO:0000269|PubMed:9875213}.
MOD_RES 28 28 Phosphoserine; by CDK1.
{ECO:0000244|PubMed:24275569}.
MOD_RES 31 31 Phosphoserine.
{ECO:0000250|UniProtKB:P31001}.
MOD_RES 32 32 Phosphoserine; by CDK1.
{ECO:0000269|PubMed:27565725}.
MOD_RES 37 37 Asymmetric dimethylarginine; alternate.
{ECO:0000250|UniProtKB:P31001}.
MOD_RES 37 37 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:P31001}.
MOD_RES 45 45 Phosphoserine.
{ECO:0000250|UniProtKB:P48675}.
MOD_RES 48 48 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 51 51 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 58 58 ADP-ribosylarginine.
{ECO:0000250|UniProtKB:P48675}.
MOD_RES 60 60 Phosphoserine; by AURKB.
{ECO:0000269|PubMed:12686604}.
MOD_RES 68 68 Phosphoserine.
{ECO:0000250|UniProtKB:P31001}.
MOD_RES 70 70 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P31001}.
MOD_RES 76 76 Phosphothreonine; by ROCK1.
{ECO:0000269|PubMed:9875213}.
MOD_RES 77 77 Phosphothreonine; by ROCK1.
{ECO:0000269|PubMed:9875213}.
MOD_RES 81 81 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 82 82 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 92 92 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 122 122 Phosphotyrosine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 125 125 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 125 125 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 144 144 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 193 193 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 193 193 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 231 231 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 240 240 N6-acetyllysine.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 290 290 Phosphoserine.
{ECO:0000250|UniProtKB:P48675}.
MOD_RES 299 299 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 299 299 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 330 330 Phosphoserine.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 358 358 Phosphoserine.
{ECO:0000250|UniProtKB:P48675}.
MOD_RES 361 361 Phosphoserine.
{ECO:0000250|UniProtKB:P48675}.
MOD_RES 378 378 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 388 388 Nitrated tyrosine.
{ECO:0000250|UniProtKB:P21807}.
MOD_RES 414 414 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 424 424 Phosphoserine.
{ECO:0000250|UniProtKB:P31001}.
MOD_RES 431 431 Phosphothreonine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 449 449 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 449 449 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 450 450 Phosphothreonine.
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 109 109 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 125 125 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 144 144 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 267 267 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 299 299 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 318 318 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 378 378 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 443 443 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 449 449 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 449 449 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P08670}.
VARIANT 2 2 S -> I (in MFM1; dbSNP:rs58999456).
{ECO:0000269|PubMed:14711882}.
/FTId=VAR_042448.
VARIANT 7 7 S -> F (in MFM1).
{ECO:0000269|PubMed:22106715}.
/FTId=VAR_067207.
VARIANT 13 13 S -> F (in MFM1; some patients manifest a
severe cardiac phenotype with right
ventricular predominance;
dbSNP:rs62636495).
{ECO:0000269|PubMed:18061454,
ECO:0000269|PubMed:19879535}.
/FTId=VAR_067208.
VARIANT 16 16 R -> C (in MFM1).
{ECO:0000269|PubMed:16376610}.
/FTId=VAR_079048.
VARIANT 46 46 S -> F (in MFM1; exhibits significantly
delayed filament assembly kinetics when
bound to NEB; enhanced binding affinity
towards NEB; dbSNP:rs60794845).
{ECO:0000269|PubMed:14711882,
ECO:0000269|PubMed:23615443}.
/FTId=VAR_042449.
VARIANT 46 46 S -> Y (in MFM1; dbSNP:rs60794845).
{ECO:0000269|PubMed:14711882}.
/FTId=VAR_042450.
VARIANT 116 116 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).
{ECO:0000269|PubMed:20829228}.
/FTId=VAR_069191.
VARIANT 120 120 A -> D (in CMD1I; results in impaired
filaments formation, does not localize at
intercalated disks).
{ECO:0000269|PubMed:24200904}.
/FTId=VAR_075228.
VARIANT 136 136 L -> P (in CMD1I; results in impaired
filaments formation, does not localize at
intercalated disks).
{ECO:0000269|PubMed:26724190}.
/FTId=VAR_075229.
VARIANT 173 179 Missing (in MFM1; severe form).
{ECO:0000269|PubMed:9736733}.
/FTId=VAR_009188.
VARIANT 213 213 A -> 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;
dbSNP:rs41272699).
{ECO:0000269|PubMed:14648196,
ECO:0000269|PubMed:16865695,
ECO:0000269|PubMed:21842594,
ECO:0000269|PubMed:23168288}.
/FTId=VAR_042451.
VARIANT 240 240 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).
{ECO:0000269|PubMed:12620971}.
/FTId=VAR_070101.
VARIANT 241 241 K -> E (found in a patient with severe
arrhythmogenic right ventricular
cardiomyopathy also carrying a pathogenic
frameshift mutation in PKP2;
dbSNP:rs201945924).
{ECO:0000269|PubMed:23168288}.
/FTId=VAR_069192.
VARIANT 245 245 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).
{ECO:0000269|PubMed:23615443}.
/FTId=VAR_042452.
VARIANT 326 326 H -> R (rare polymorphism; does not
result in impaired filaments formation).
{ECO:0000269|PubMed:24200904}.
/FTId=VAR_075230.
VARIANT 337 337 A -> P (in MFM1; mild adult-onset; unable
to form a functional filamentous network;
dbSNP:rs59962885).
{ECO:0000269|PubMed:10717012,
ECO:0000269|PubMed:9697706}.
/FTId=VAR_007900.
VARIANT 338 338 L -> R (in MFM1; results in the formation
of a filamentous network disrupted by
multiple breaks and clumps or large
aggregates; dbSNP:rs57496341).
{ECO:0000269|PubMed:16865695}.
/FTId=VAR_067209.
VARIANT 342 342 N -> D (in MFM1; unable to form a
filamentous network; abolishes binding to
MTM1; dbSNP:rs267607482).
{ECO:0000269|PubMed:10717012,
ECO:0000269|PubMed:14648196,
ECO:0000269|PubMed:21135508}.
/FTId=VAR_042453.
VARIANT 345 345 L -> P (in MFM1; distal onset; incapable
of forming filamentous networks;
dbSNP:rs57639980).
{ECO:0000269|PubMed:10545598}.
/FTId=VAR_009189.
VARIANT 350 350 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).
{ECO:0000269|PubMed:15800015,
ECO:0000269|PubMed:17439987,
ECO:0000269|PubMed:25394388}.
/FTId=VAR_042454.
VARIANT 355 355 R -> P (in MFM1; dbSNP:rs61368398).
{ECO:0000269|PubMed:16009553}.
/FTId=VAR_042455.
VARIANT 357 357 A -> P (in MFM1; unable to polymerize and
form an intracellular filamentous
network; abolishes binding to MTM1;
dbSNP:rs58898021).
{ECO:0000269|PubMed:12766977,
ECO:0000269|PubMed:14648196,
ECO:0000269|PubMed:21135508}.
/FTId=VAR_042456.
VARIANT 359 361 Missing (in MFM1).
{ECO:0000269|PubMed:14648196}.
/FTId=VAR_018769.
VARIANT 360 360 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).
{ECO:0000269|PubMed:10717012,
ECO:0000269|PubMed:16865695,
ECO:0000269|PubMed:21135508,
ECO:0000269|PubMed:9697706}.
/FTId=VAR_007901.
VARIANT 366 366 Missing (in MFM1).
{ECO:0000269|PubMed:14648196}.
/FTId=VAR_018770.
VARIANT 370 370 L -> P (in MFM1; unable to polymerize and
form an intracellular filamentous
network; does not affect binding to MTM1;
dbSNP:rs59308628).
{ECO:0000269|PubMed:12766977,
ECO:0000269|PubMed:14648196,
ECO:0000269|PubMed:21135508}.
/FTId=VAR_042457.
VARIANT 385 385 L -> P (in MFM1; dbSNP:rs57955682).
{ECO:0000269|PubMed:11061256}.
/FTId=VAR_018771.
VARIANT 389 389 Q -> P (in MFM1; dbSNP:rs28930075).
{ECO:0000269|PubMed:11668632}.
/FTId=VAR_018772.
VARIANT 393 393 N -> 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;
dbSNP:rs121913001).
{ECO:0000269|PubMed:10717012,
ECO:0000269|PubMed:16865695,
ECO:0000269|PubMed:9697706}.
/FTId=VAR_007902.
VARIANT 399 399 D -> Y (in MFM1; results in the formation
of a filamentous network disrupted by
multiple breaks and clumps or large
aggregates; dbSNP:rs61130669).
{ECO:0000269|PubMed:16865695}.
/FTId=VAR_067210.
VARIANT 401 401 E -> K (in MFM1; results in the formation
of a filamentous network disrupted by
multiple breaks and clumps or large
aggregates; dbSNP:rs57694264).
{ECO:0000269|PubMed:16865695}.
/FTId=VAR_067211.
VARIANT 406 406 R -> W (in MFM1; unable to form a
filamentous network; dbSNP:rs61726465).
{ECO:0000269|PubMed:10717012,
ECO:0000269|PubMed:10905661,
ECO:0000269|PubMed:16376610}.
/FTId=VAR_042458.
VARIANT 419 419 P -> S (in MFM1; found in a family with
myofibrillar myopathy and arrhythmogenic
right ventricular cardiomyopathy;
dbSNP:rs62635763).
{ECO:0000269|PubMed:22395865}.
/FTId=VAR_069074.
VARIANT 442 442 T -> I (in MFM1; reveals a severe
disturbance of filament-formation
competence and filament-filament
interactions; dbSNP:rs121913005).
{ECO:0000269|PubMed:17221859}.
/FTId=VAR_042459.
VARIANT 449 449 K -> M (in MFM1).
/FTId=VAR_042460.
VARIANT 449 449 K -> T (in MFM1; dbSNP:rs267607485).
{ECO:0000269|PubMed:14711882}.
/FTId=VAR_042461.
VARIANT 451 451 I -> M (in CMD1I and MFM1; reveals a
severe disturbance of filament-formation
competence and filament-filament
interactions; reduced interaction with
CRYAB; dbSNP:rs121913002).
{ECO:0000269|PubMed:10430757,
ECO:0000269|PubMed:10717012,
ECO:0000269|PubMed:17221859,
ECO:0000269|PubMed:28470624}.
/FTId=VAR_018773.
VARIANT 453 453 T -> I (in MFM1; exhibits significantly
delayed filament assembly kinetics when
bound to NEB and NEBL; enhanced binding
affinity towards NEB and NEBL).
{ECO:0000269|PubMed:16376610,
ECO:0000269|PubMed:23615443}.
/FTId=VAR_079049.
VARIANT 454 454 R -> W (in MFM1; reveals a severe
disturbance of filament-formation
competence and filament-filament
interactions; increased interaction with
CRYAB; dbSNP:rs267607490).
{ECO:0000269|PubMed:17221859,
ECO:0000269|PubMed:22106715,
ECO:0000269|PubMed:28470624}.
/FTId=VAR_042462.
VARIANT 460 460 S -> I (in MFM1; reveals a severe
disturbance of filament-formation
competence and filament-filament
interactions; dbSNP:rs267607491).
{ECO:0000269|PubMed:17221859}.
/FTId=VAR_042463.
MUTAGEN 120 120 A->E,R: Results in impaired filaments
formation. {ECO:0000269|PubMed:24200904}.
MUTAGEN 120 120 A->K,L,V: Does not result in impaired
filaments formation.
{ECO:0000269|PubMed:24200904}.
CONFLICT 23 25 GFP -> VFS (in Ref. 1 and 2; AAA99221).
{ECO:0000305}.
CONFLICT 39 39 G -> P (in Ref. 1 and 2; AAA99221).
{ECO:0000305}.
CONFLICT 119 123 FANYI -> SPIYM (in Ref. 1 and 2;
AAA99221). {ECO:0000305}.
CONFLICT 134 134 Missing (in Ref. 1, 2; AAA99221 and 3;
AAC50680). {ECO:0000305}.
SEQUENCE 470 AA; 53536 MW; 1B5D9EA93C3BB319 CRC64;
MSQAYSSSQR VSSYRRTFGG APGFPLGSPL SSPVFPRAGF GSKGSSSSVT SRVYQVSRTS
GGAGGLGSLR ASRLGTTRTP SSYGAGELLD FSLADAVNQE FLTTRTNEKV ELQELNDRFA
NYIEKVRFLE QQNAALAAEV NRLKGREPTR VAELYEEELR ELRRQVEVLT NQRARVDVER
DNLLDDLQRL KAKLQEEIQL KEEAENNLAA FRADVDAATL ARIDLERRIE SLNEEIAFLK
KVHEEEIREL QAQLQEQQVQ VEMDMSKPDL TAALRDIRAQ YETIAAKNIS EAEEWYKSKV
SDLTQAANKN NDALRQAKQE MMEYRHQIQS YTCEIDALKG TNDSLMRQMR ELEDRFASEA
SGYQDNIARL EEEIRHLKDE MARHLREYQD LLNVKMALDV EIATYRKLLE GEESRINLPI
QTYSALNFRE TSPEQRGSEV HTKKTVMIKT IETRDGEVVS EATQQQHEVL


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