P17661 (DESM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Desmin

Gene names

Name:

DES

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	470 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.11
Subcellular location	Cytoplasm.
Post-translational modification	ADP-ribosylation prevents ability to form intermediate filaments By similarity.
Involvement in disease	Defects in DES are the cause of myopathy myofibrillar type 1 (MFM1) [MIM:601419]; also known as desmin-related myopathy (DRM). 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. Ref.4 Ref.6 Ref.7 Ref.9 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.23 Defects in DES are the cause of cardiomyopathy dilated type 1I (CMD1I) [MIM:604765]. Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. Ref.5 Defects in DES are the cause of neurogenic scapuloperoneal syndrome Kaeser type (Kaeser syndrome) [MIM:181400]. Kaeser syndrome is an 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.
Sequence similarities	Belongs to the intermediate filament family.

Ontologies

Keywords
Cellular component	Cytoplasm Intermediate filament
Disease	Cardiomyopathy Desmin-related myopathy Disease mutation Myofibrillar myopathy
Domain	Coiled coil
Molecular function	Muscle protein
PTM	ADP-ribosylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cytoskeleton organization Traceable author statement. Source: ProtInc muscle filament sliding Traceable author statement. Source: Reactome regulation of heart contraction Traceable author statement. Source: ProtInc
Cellular component	Z disc Inferred from direct assay. Source: MGI cytosol Traceable author statement. Source: Reactome
Molecular function	nebulin binding Inferred from physical interaction. Source: BHF-UCL structural constituent of cytoskeleton Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MLH1	P40692	7	EBI-1055572,EBI-744248

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 470	469	Desmin		PRO_0000063771
Regions
	Region	2 – 108	107	Head
	Region	109 – 412	304	Rod
	Region	109 – 141	33	Coil 1A
	Region	142 – 151	10	Linker 1
	Region	152 – 252	101	Coil 1B
	Region	253 – 268	16	Linker 12
	Region	269 – 287	19	Coil 2A
	Region	288 – 295	8	Linker 2
	Region	296 – 412	117	Coil 2B
	Region	413 – 470	58	Tail
Amino acid modifications
	Modified residue	12	1	Phosphoserine; by AURKB Ref.10
	Modified residue	17	1	Phosphothreonine; by AURKB Ref.10
	Modified residue	58	1	ADP-ribosylarginine By similarity
	Modified residue	60	1	Phosphoserine; by AURKB Ref.10
Natural variations
	Natural variant	2	1	S → I in MFM1; entirely similar expression patterns as the wild-type. Ref.19 Corresponds to variant rs58999456 [ dbSNP | Ensembl ].		VAR_042448
	Natural variant	46	1	S → F in MFM1; entirely similar expression patterns as the wild-type. Ref.19 Corresponds to variant rs60794845 [ dbSNP | Ensembl ].		VAR_042449
	Natural variant	46	1	S → Y in MFM1; entirely similar expression patterns as the wild-type. Ref.19		VAR_042450
	Natural variant	173 – 179	7	Missing in MFM1; severe form.		VAR_009188
	Natural variant	213	1	A → V in MFM1. Ref.7 Corresponds to variant rs41272699 [ dbSNP | Ensembl ].		VAR_042451
	Natural variant	245	1	E → D in MFM1.		VAR_042452
	Natural variant	337	1	A → P in MFM1; mild adult-onset; unable to form a filamentous network. Ref.4 Ref.17 Corresponds to variant rs59962885 [ dbSNP | Ensembl ].		VAR_007900
	Natural variant	342	1	N → D in MFM1; unable to form a filamentous network; abolishes binding to MTM1. Ref.7 Ref.11 Ref.17		VAR_042453
	Natural variant	345	1	L → P in MFM1; distal onset; incapable of forming filamentous networks. Ref.9 Corresponds to variant rs57639980 [ dbSNP | Ensembl ].		VAR_009189
	Natural variant	350	1	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. Ref.20 Ref.22 Corresponds to variant rs57965306 [ dbSNP | Ensembl ].		VAR_042454
	Natural variant	355	1	R → P in MFM1. Ref.21 Corresponds to variant rs61368398 [ dbSNP | Ensembl ].		VAR_042455
	Natural variant	357	1	A → P in MFM1; unable to polymerize and form an intracellular filamentous network; abolishes binding to MTM1. Ref.7 Ref.11 Ref.18 Corresponds to variant rs58898021 [ dbSNP | Ensembl ].		VAR_042456
	Natural variant	359 – 361	3	Missing in MFM1.		VAR_018769
	Natural variant	360	1	A → P in MFM1; heterozygous with Ile-391 gives a severe childhood-onset; unable to form a filamentous network; abolishes binding to MTM1. Ref.4 Ref.11 Ref.17		VAR_007901
	Natural variant	366	1	Missing in MFM1.		VAR_018770
	Natural variant	370	1	L → P in MFM1; unable to polymerize and form an intracellular filamentous network; does not affect binding to MTM1. Ref.7 Ref.11 Ref.18 Corresponds to variant rs59308628 [ dbSNP | Ensembl ].		VAR_042457
	Natural variant	385	1	L → P in MFM1. Ref.16 Corresponds to variant rs57955682 [ dbSNP | Ensembl ].		VAR_018771
	Natural variant	389	1	Q → P in MFM1. Ref.6 Corresponds to variant rs28930075 [ dbSNP | Ensembl ].		VAR_018772
	Natural variant	393	1	N → I in MFM1; heterozygous with Pro-358 gives a severe childhood-onset; unable to form a filamentous network. Ref.4 Ref.17		VAR_007902
	Natural variant	406	1	R → W in MFM1; unable to form a filamentous network. Ref.15 Ref.17 Corresponds to variant rs61726465 [ dbSNP | Ensembl ].		VAR_042458
	Natural variant	442	1	T → 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.23		VAR_042459
	Natural variant	449	1	K → M in MFM1.		VAR_042460
	Natural variant	449	1	K → T in MFM1; entirely similar expression patterns as the wild-type. Ref.19		VAR_042461
	Natural variant	451	1	I → M in CMD1I; 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.17 Ref.23		VAR_018773
	Natural variant	454	1	R → 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.23		VAR_042462
	Natural variant	460	1	S → 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.23		VAR_042463
Experimental info
	Sequence conflict	23 – 25	3	GFP → VFS Ref.1
	Sequence conflict	23 – 25	3	GFP → VFS in AAA99221. Ref.2
	Sequence conflict	39	1	G → P Ref.1
	Sequence conflict	39	1	G → P in AAA99221. Ref.2
	Sequence conflict	119 – 123	5	FANYI → SPIYM Ref.1
	Sequence conflict	119 – 123	5	FANYI → SPIYM in AAA99221. Ref.2
	Sequence conflict	134	1	Missing Ref.1
	Sequence conflict	134	1	Missing in AAA99221. Ref.2
	Sequence conflict	134	1	Missing in AAC50680. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P17661 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 1B5D9EA93C3BB319	FASTA	470	53,536
	10 20 30 40 50 60 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

References

	« Hide 'large scale' referencesShow '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: 2673923] [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: 2007603] [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: 8792816] [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: 9697706] [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: 10430757] [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: 11668632] [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: 14648196] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS MFM1 VAL-213; 359-GLU--SER-361 DEL; ASP-342; PRO-357; ASN-366 DEL AND PRO-370.
[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: 15489334] [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: 10545598] [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: 12686604] [Abstract] Cited for: PHOSPHORYLATION AT SER-12; THR-17 AND SER-60.
[11]	"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: 21135508] [Abstract] Cited for: INTERACTION WITH MTM1, CHARACTERIZATION OF VARIANTS ASP-342; PRO-357; PRO-360 AND PRO-370.
[12]	"Desmin myopathy." Goldfarb L.G., Vicart P., Goebel H.H., Dalakas M.C. Brain 127:723-734(2004) [PubMed: 14724127] [Abstract] Cited for: REVIEW ON VARIANTS MFM1.
[13]	"Desminopathies in muscle disease." Paulin D., Huet A., Khanamyrian L., Xue Z. J. Pathol. 204:418-427(2004) [PubMed: 15495235] [Abstract] Cited for: REVIEW ON VARIANTS MFM1.
[14]	"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: 9736733] [Abstract] Cited for: VARIANT MFM1 173-ARG--GLU-179 DEL.
[15]	"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: 10905661] [Abstract] Cited for: VARIANT MFM1 TRP-406.
[16]	"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: 11061256] [Abstract] Cited for: VARIANT MFM1 PRO-385.
[17]	"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: 10717012] [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.
[18]	"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: 12766977] [Abstract] Cited for: VARIANTS MFM1 PRO-357 AND PRO-370, CHARACTERIZATION OF VARIANTS MFM1 PRO-357 AND PRO-370.
[19]	"Myofibrillar myopathy: clinical, morphological and genetic studies in 63 patients." Selcen D., Ohno K., Engel A.G. Brain 127:439-451(2004) [PubMed: 14711882] [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.
[20]	"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: 15800015] [Abstract] Cited for: VARIANT MFM1 PRO-350, CHARACTERIZATION OF VARIANT MFM1 PRO-350.
[21]	"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: 16009553] [Abstract] Cited for: VARIANT MFM1 PRO-355.
[22]	"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: 17439987] [Abstract] Cited for: VARIANT KAESER SYNDROME PRO-350.
[23]	"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: 17221859] [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.
+	Additional computationally mapped references.

Web resources

Human Intermediate Filament Mutation Database

GeneReviews

Wikipedia

Desmin entry

Cross-references

Sequence databases
EMBL GenBank DDBJ	M63391 Genomic DNA. Translation: AAA99221.1. U59167 mRNA. Translation: AAC50680.1. 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.
IPI	IPI00465084.
PIR	DMHU. JE0063.
RefSeq	NP_001918.3. NM_001927.3.
UniGene	Hs.594952.
3D structure databases
ProteinModelPortal	P17661.
SMR	P17661. Positions 106-143, 153-254, 268-411.
ModBase	Search...
Protein-protein interaction databases
IntAct	P17661. 1 interaction.
MINT	MINT-215829.
STRING	P17661.
PTM databases
PhosphoSite	P17661.
Polymorphism databases
DMDM	6686280.
2D gel databases
SWISS-2DPAGE	P17661.
REPRODUCTION-2DPAGE	IPI00465084. P17661.
UCD-2DPAGE	P17661.
Proteomic databases
PRIDE	P17661.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000373960; ENSP00000363071; ENSG00000175084.
GeneID	1674.
KEGG	hsa:1674.
UCSC	uc002vll.1. human.
Organism-specific databases
CTD	1674.
GeneCards	GC02P220283.
H-InvDB	HIX0200296.
HGNC	HGNC:2770. DES.
HPA	CAB000034. HPA018803.
MIM	125660. gene. 181400. phenotype. 601419. phenotype. 604765. phenotype.
neXtProt	NX_P17661.
Orphanet	98909. Desminopathy. 154. Familial isolated dilated cardiomyopathy. 85146. Scapuloperoneal amyotrophy.
PharmGKB	PA27253.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG08072.
HOVERGEN	HBG013015.
InParanoid	P17661.
OMA	SSEMHSK.
OrthoDB	EOG4H9XKM.
PhylomeDB	P17661.
Enzyme and pathway databases
Pathway_Interaction_DB	aurora_b_pathway. Aurora B signaling.
Reactome	REACT_17044. Muscle contraction.
Gene expression databases
ArrayExpress	P17661.
Bgee	P17661.
Genevestigator	P17661.
GermOnline	ENSG00000175084. Homo sapiens.
Family and domain databases
InterPro	IPR016044. F. IPR001664. IF. IPR006821. Intermed_filament_DNA-bd. IPR018039. Intermediate_filament_CS. [Graphical view]
KO	K07610.
PANTHER	PTHR23239. IF. 1 hit.
Pfam	PF00038. Filament. 1 hit. PF04732. Filament_head. 1 hit. [Graphical view]
PROSITE	PS00226. IF. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	6888.
SOURCE	Search...

Entry information

Entry name

DESM_HUMAN

Accession

Primary (citable) accession number: P17661
Secondary accession number(s): Q15787 , 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:	January 25, 2012
This is version 128 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.