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Protein

Desmin

Gene

Des

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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. 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. 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

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionMuscle protein

Names & Taxonomyi

Protein namesi
Recommended name:
Desmin
Gene namesi
Name:Des
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620686 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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000637751 – 469DesminAdd BLAST469

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei7Phosphoserine; by CDK1By similarity1
Modified residuei12Phosphoserine; by AURKBBy similarity1
Modified residuei16Omega-N-methylarginineBy similarity1
Modified residuei17Phosphothreonine; by AURKB and ROCK1By similarity1
Modified residuei25PhosphoserineCombined sources1
Modified residuei28Phosphoserine; by CDK1Combined sources1
Modified residuei31PhosphoserineBy similarity1
Modified residuei32Phosphoserine; by CDK1Combined sources1
Modified residuei37Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei37Omega-N-methylarginine; alternateBy similarity1
Modified residuei45PhosphoserineCombined sources1
Modified residuei58ADP-ribosylarginine1 Publication1
Modified residuei60Phosphoserine; by AURKBBy similarity1
Modified residuei68PhosphoserineCombined sources1
Modified residuei70Omega-N-methylarginineBy similarity1
Modified residuei76Phosphothreonine; by ROCK1By similarity1
Modified residuei77Phosphothreonine; by ROCK1By similarity1
Modified residuei81PhosphoserineCombined sources1
Modified residuei289PhosphoserineCombined sources1
Modified residuei357PhosphoserineCombined sources1
Modified residuei360PhosphoserineCombined sources1
Modified residuei423PhosphoserineCombined sources1

Post-translational modificationi

ADP-ribosylation prevents ability to form intermediate filaments.1 Publication
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.By similarity

Keywords - PTMi

ADP-ribosylation, Methylation, Phosphoprotein

Proteomic databases

PaxDbiP48675
PRIDEiP48675

PTM databases

iPTMnetiP48675
PhosphoSitePlusiP48675

Interactioni

Subunit structurei

Homopolymer. Interacts with DST. Interacts with MTM1. 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

Protein-protein interaction databases

IntActiP48675, 3 interactors
STRINGi10116.ENSRNOP00000026860

Structurei

3D structure databases

ProteinModelPortaliP48675
SMRiP48675
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 108HeadAdd BLAST108
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

Sequence similaritiesi

Belongs to the intermediate filament family.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IFZ1 Eukaryota
ENOG410XRBS LUCA
HOGENOMiHOG000230977
HOVERGENiHBG013015
InParanoidiP48675
KOiK07610
PhylomeDBiP48675

Family and domain databases

InterProiView protein in InterPro
IPR027698 DES
IPR001664 IF
IPR018039 IF_conserved
IPR039008 IF_rod_dom
IPR006821 Intermed_filament_DNA-bd
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.

P48675-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQAYSSSQR VSSYRRTFGG APGFSLGSPL SSPVFPRAGF GTKGSSSSVT
60 70 80 90 100
SRVYQVSRTS GGAGGLGSLR ASRLGTTRAP SYGAGELLDF SLADAVNQEF
110 120 130 140 150
LATRTNEKVE LQELNDRFAN YFEKVRFLEQ 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
LEDRFASEAS GYQDNIARLE EEIRHLKDEM ARHLREYQDL LNVKMALDVE
410 420 430 440 450
IATYRKLLEG EESRINLPIQ TFSALNFRET SPEQRGSEVH TKKTVMIKTI
460
ETRDGEVVSE ATQQQHEVL
Length:469
Mass (Da):53,457
Last modified:January 23, 2007 - v2
Checksum:i4E53A71FC1C55BDF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73524 Genomic DNA Translation: CAA51920.1
PIRiI52469
RefSeqiNP_071976.1, NM_022531.1
UniGeneiRn.39196

Genome annotation databases

GeneIDi64362
KEGGirno:64362
UCSCiRGD:620686 rat

Similar proteinsi

Entry informationi

Entry nameiDESM_RAT
AccessioniPrimary (citable) accession number: P48675
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 120 of the entry and version 2 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. SIMILARITY comments
    Index of protein domains and families

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