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Protein

Desmin

Gene

Des

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Muscle-specific type III intermediate filament essential for proper muscular structure and function. Plays a crucial role in maintaining the structure of sarcomeres, inter-connecting the Z-disks and forming the myofibrils, linking them not only to the sarcolemmal cytoskeleton, but also to the nucleus and mitochondria, thus providing strength for the muscle fiber during activity (By similarity). In adult striated muscle they form a fibrous network connecting myofibrils to each other and to the plasma membrane from the periphery of the Z-line structures (PubMed:25394388). May act as a sarcomeric microtubule-anchoring protein: specifically associates with detyrosinated tubulin-alpha chains, leading to buckled microtubules and mechanical resistance to contraction (PubMed:27102488). 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 (PubMed:27733623).By similarity3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei353Stutter1

GO - Molecular functioni

  • cytoskeletal protein binding Source: MGI
  • identical protein binding Source: MGI
  • structural constituent of cytoskeleton Source: MGI

GO - Biological processi

  • intermediate filament organization Source: UniProtKB
  • muscle organ development Source: MGI

Keywordsi

Molecular functionMuscle protein

Enzyme and pathway databases

ReactomeiR-MMU-390522. Striated Muscle Contraction.

Names & Taxonomyi

Protein namesi
Recommended name:
Desmin
Gene namesi
Name:Des
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:94885. Des.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Intermediate filament, Membrane, Nucleus

Pathology & Biotechi

Disruption phenotypei

Mice hearts have reduced nebulette (NEB) and elevated actin levels, with intact myofibers showing disordered NEB organization.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi7S → A: Reduced phosphorylation. Almost complete loss of phosphorylation; when associated with A-28 and A-32. 1 Publication1
Mutagenesisi28S → A: Reduced phosphorylation. Almost complete loss of phosphorylation; when associated with A-7 and A-32. 1 Publication1
Mutagenesisi32S → A: Reduced phosphorylation and formation of unusual long bridge-like intermediate filament structures between two daughter cells during cytokinesis. Almost complete loss of phosphorylation; when associated with A-7 and A-28. Increased formation of unusual long bridge-like intermediate filament structures between two daughter cells during cytokinesis; when associated with A-60 and A-76. 1 Publication1
Mutagenesisi60S → A: Formation of unusual long bridge-like intermediate filament structures between two daughter cells during cytokinesis; when associated with A-76. Increased formation of unusual long bridge-like intermediate filament structures between two daughter cells during cytokinesis; when associated with A-32 and A-76. 1 Publication1
Mutagenesisi76T → A: Formation of unusual long bridge-like intermediate filament structures between two daughter cells during cytokinesis; when associated with A-60. Increased formation of unusual long bridge-like intermediate filament structures between two daughter cells during cytokinesis; when associated with A-32 and A-60. 1 Publication1
Mutagenesisi349R → P: Increases protein decay. forms subsarcolemmal aggregates. Changes the subcellular localization and turnover of its direct, extrasarcomeric binding partners. Knockin mice develop age-dependent desmin-positive protein aggregation pathology, skeletal muscle weakness, dilated cardiomyopathy, as well as cardiac arrhythmias and conduction defects. Knockin mice exhibit altered axial myofibrillar lattice arrangement in fast- and slow-twitch muscle fibers, increased axial stiffness and stretch-induced vulnerability in soleus muscle fiber bundles, reduced Ca(2+)-sensitivity in heterozygous fiber bundles and increased Ca(2+)-sensitivity in homozygous fiber bundles. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000637732 – 469DesminAdd BLAST468

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei7Phosphoserine; by CDK11 Publication1
Modified residuei8PhosphoserineBy similarity1
Modified residuei12Phosphoserine; by AURKBBy similarity1
Modified residuei13PhosphoserineBy similarity1
Modified residuei14Nitrated tyrosineBy similarity1
Modified residuei16Omega-N-methylarginineCombined sources1
Modified residuei17Phosphothreonine; by AURKB and ROCK1Combined sources1
Modified residuei25PhosphoserineCombined sources1
Modified residuei28Phosphoserine; by CDK1Combined sources1 Publication1
Modified residuei31PhosphoserineCombined sources1
Modified residuei32Phosphoserine; by CDK1Combined sources1 Publication1
Modified residuei37Asymmetric dimethylarginine; alternateCombined sources1
Modified residuei37Omega-N-methylarginine; alternateCombined sources1
Modified residuei45PhosphoserineBy similarity1
Modified residuei48PhosphoserineBy similarity1
Modified residuei51PhosphoserineBy similarity1
Modified residuei58ADP-ribosylarginineBy similarity1
Modified residuei60Phosphoserine; by AURKB1 Publication1
Modified residuei68PhosphoserineCombined sources1
Modified residuei70Omega-N-methylarginineCombined sources1
Modified residuei76Phosphothreonine; by ROCK11 Publication1
Modified residuei77Phosphothreonine; by ROCK1By similarity1
Modified residuei81PhosphoserineBy similarity1
Modified residuei91PhosphoserineBy similarity1
Cross-linki108Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei121PhosphotyrosineBy similarity1
Modified residuei124N6-acetyllysine; alternateBy similarity1
Modified residuei124N6-succinyllysine; alternateBy similarity1
Cross-linki124Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei143N6-acetyllysine; alternateBy similarity1
Cross-linki143Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei192N6-acetyllysine; alternateBy similarity1
Modified residuei192N6-succinyllysine; alternateBy similarity1
Modified residuei230PhosphoserineBy similarity1
Modified residuei239N6-acetyllysineBy similarity1
Cross-linki266Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei289PhosphoserineBy similarity1
Modified residuei298N6-acetyllysine; alternateBy similarity1
Modified residuei298N6-succinyllysine; alternateBy similarity1
Cross-linki298Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki317Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei329PhosphoserineBy similarity1
Modified residuei357PhosphoserineBy similarity1
Modified residuei377N6-acetyllysine; alternateBy similarity1
Cross-linki377Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei387Nitrated tyrosineBy similarity1
Modified residuei413PhosphoserineBy similarity1
Modified residuei423PhosphoserineCombined sources1
Modified residuei430PhosphothreonineBy similarity1
Cross-linki442Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei448N6-acetyllysine; alternateBy similarity1
Modified residuei448N6-succinyllysine; alternateBy similarity1
Cross-linki448Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki448Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei449PhosphothreonineBy similarity1

Post-translational modificationi

ADP-ribosylation prevents ability to form intermediate filaments.By similarity
Phosphorylation at Ser-7, Ser-28 and Ser-32 by CDK1, phosphorylation at Ser-60 by AURKB and phosphorylation at Thr-76 by ROCK1 contribute to efficient separation of desmin intermediate filaments during mitosis.1 Publication

Keywords - PTMi

Acetylation, ADP-ribosylation, Isopeptide bond, Methylation, Nitration, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP31001.
PaxDbiP31001.
PeptideAtlasiP31001.
PRIDEiP31001.

2D gel databases

SWISS-2DPAGEiP31001.

PTM databases

iPTMnetiP31001.
PhosphoSitePlusiP31001.

Miscellaneous databases

PMAP-CutDBiP31001.

Expressioni

Tissue specificityi

Cardiac progenitor cells and immature cardiomyocytes (at protein level).1 Publication

Gene expression databases

BgeeiENSMUSG00000026208.
CleanExiMM_DES.
ExpressionAtlasiP31001. baseline and differential.
GenevisibleiP31001. MM.

Interactioni

Subunit structurei

Homopolymer. Interacts with MTM1 (By similarity). Interacts with DST (PubMed:10357897). Interacts with tubulin-alpha; specifically associates with detyrosinated tubulin-alpha (PubMed:27102488). Interacts with EPPK1; interaction is dependent of higher-order structure of intermediate filament. Interacts with CRYAB. Interacts with NEB (via nebulin repeats 160-164). Interacts (via rod region) with NEBL (via nebulin repeats 1-5) (By similarity).By similarity2 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi199210. 5 interactors.
DIPiDIP-256N.
IntActiP31001. 10 interactors.
MINTiMINT-220806.
STRINGi10090.ENSMUSP00000027409.

Structurei

3D structure databases

ProteinModelPortaliP31001.
SMRiP31001.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini107 – 415IF rodPROSITE-ProRule annotationAdd BLAST309

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 108HeadAdd BLAST107
Regioni109 – 140Coil 1AAdd BLAST32
Regioni141 – 150Linker 110
Regioni151 – 251Coil 1BAdd BLAST101
Regioni252 – 267Linker 12Add BLAST16
Regioni267 – 414Interaction with NEBBy similarityAdd BLAST148
Regioni268 – 286Coil 2AAdd BLAST19
Regioni287 – 294Linker 28
Regioni295 – 411Coil 2BAdd BLAST117
Regioni412 – 469TailAdd BLAST58
Regioni437 – 452Interaction with CRYABBy similarityAdd BLAST16

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi45 – 48Poly-Ser4

Sequence similaritiesi

Belongs to the intermediate filament family.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IFZ1. Eukaryota.
ENOG410XRBS. LUCA.
GeneTreeiENSGT00830000128228.
HOGENOMiHOG000230977.
HOVERGENiHBG013015.
InParanoidiP31001.
KOiK07610.
OMAiNQRARVE.
OrthoDBiEOG091G12MK.
PhylomeDBiP31001.
TreeFamiTF330122.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P31001-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQAYSSSQR VSSYRRTFGG APGFSLGSPL SSPVFPRAGF GTKGSSSSMT
60 70 80 90 100
SRVYQVSRTS GGAGGLGSLR SSRLGTTRAP SYGAGELLDF SLADAVNQEF
110 120 130 140 150
LATRTNEKVE LQELNDRFAN YIEKVRFLEQ QNAALAAEVN RLKGREPTRV
160 170 180 190 200
AELYEEEMRE LRRQVEVLTN QRARVDVERD NLIDDLQRLK AKLQEEIQLR
210 220 230 240 250
EEAENNLAAF RADVDAATLA RIDLERRIES LNEEIAFLKK VHEEEIRELQ
260 270 280 290 300
AQLQEQQVQV EMDMSKPDLT AALRDIRAQY ETIAAKNISE AEEWYKSKVS
310 320 330 340 350
DLTQAANKNN DALRQAKQEM MEYRHQIQSY TCEIDALKGT NDSLMRQMRE
360 370 380 390 400
LEDRFASEAN GYQDNIARLE EEIRHLKDEM ARHLREYQDL LNVKMALDVE
410 420 430 440 450
IATYRKLLEG EESRINLPIQ TFSALNFRET SPEQRGSEVH TKKTVMIKTI
460
ETRDGEVVSE ATQQQHEVL
Length:469
Mass (Da):53,498
Last modified:January 23, 2007 - v3
Checksum:i58A8A13C7CC11EEF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L22550 mRNA. No translation available.
BC031760 mRNA. Translation: AAH31760.1.
Z18892 Genomic DNA. Translation: CAA79330.1.
CCDSiCCDS15071.1.
PIRiA54104.
RefSeqiNP_034173.1. NM_010043.2.
UniGeneiMm.6712.

Genome annotation databases

EnsembliENSMUST00000027409; ENSMUSP00000027409; ENSMUSG00000026208.
GeneIDi13346.
KEGGimmu:13346.
UCSCiuc007box.2. mouse.

Similar proteinsi

Entry informationi

Entry nameiDESM_MOUSE
AccessioniPrimary (citable) accession number: P31001
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: October 25, 2017
This is version 160 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families