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Protein

Desmin

Gene

DES

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 4 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. 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.HMP:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei355Stutter1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionMuscle protein

Enzyme and pathway databases

ReactomeiR-SSC-390522. Striated Muscle Contraction.

Names & Taxonomyi

Protein namesi
Recommended name:
Desmin
Gene namesi
Name:DES
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Chromosome 15

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
Initiator methionineiRemovedHMP:
ChainiPRO_00000637742 – 471DesminAdd BLAST470

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineHMP:1
Modified residuei7Phosphoserine; by CDK1HMP:1
Modified residuei8PhosphoserineHMP:1
Modified residuei12Phosphoserine; by AURKBHMP:1
Modified residuei13PhosphoserineHMP:1
Modified residuei14Nitrated tyrosineHMP:1
Modified residuei16Omega-N-methylarginineHMP:1
Modified residuei17Phosphothreonine; by AURKB and ROCK1HMP:1
Modified residuei28Phosphoserine; by CDK1HMP:1
Modified residuei31PhosphoserineHMP:1
Modified residuei32Phosphoserine; by CDK1HMP:1
Modified residuei37Asymmetric dimethylarginine; alternateHMP:1
Modified residuei37Omega-N-methylarginine; alternateHMP:1
Modified residuei45PhosphoserineHMP:1
Modified residuei48PhosphoserineHMP:1
Modified residuei51PhosphoserineHMP:1
Modified residuei58ADP-ribosylarginineHMP:1
Modified residuei60Phosphoserine; by AURKBHMP:1
Modified residuei70Omega-N-methylarginineHMP:1
Modified residuei77Phosphothreonine; by ROCK1HMP:1
Modified residuei81PhosphoserineHMP:1
Modified residuei82PhosphoserineHMP:1
Modified residuei93PhosphoserineHMP:1
Cross-linki110Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)HMP:
Modified residuei123PhosphotyrosineHMP:1
Modified residuei126N6-acetyllysine; alternateHMP:1
Modified residuei126N6-succinyllysine; alternateHMP:1
Cross-linki126Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateHMP:
Modified residuei145N6-acetyllysine; alternateHMP:1
Cross-linki145Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateHMP:
Modified residuei194N6-acetyllysine; alternateHMP:1
Modified residuei194N6-succinyllysine; alternateHMP:1
Modified residuei232PhosphoserineHMP:1
Modified residuei241N6-acetyllysineHMP:1
Cross-linki268Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)HMP:
Modified residuei291PhosphoserineHMP:1
Modified residuei300N6-acetyllysine; alternateHMP:1
Modified residuei300N6-succinyllysine; alternateHMP:1
Cross-linki300Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateHMP:
Cross-linki319Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)HMP:
Modified residuei331PhosphoserineHMP:1
Modified residuei359PhosphoserineHMP:1
Modified residuei362PhosphoserineHMP:1
Modified residuei379N6-acetyllysine; alternateHMP:1
Cross-linki379Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateHMP:
Modified residuei389Nitrated tyrosineHMP:1
Modified residuei415PhosphoserineHMP:1
Modified residuei425PhosphoserineHMP:1
Modified residuei432PhosphothreonineHMP:1
Cross-linki444Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)HMP:
Modified residuei450N6-acetyllysine; alternateHMP:1
Modified residuei450N6-succinyllysine; alternateHMP:1
Cross-linki450Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateHMP:
Cross-linki450Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateHMP:
Modified residuei451PhosphothreonineHMP:1

Post-translational modificationi

ADP-ribosylation prevents ability to form intermediate filaments.HMP:
Phosphorylation at Ser-7, Ser-28 and Ser-32 by CDK1 and phosphorylation at Ser-60 by AURKB contribute to efficient separation of desmin intermediate filaments during mitosis.HMP:

Keywords - PTMi

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

Proteomic databases

PaxDbiP02540.
PeptideAtlasiP02540.
PRIDEiP02540.

Expressioni

Gene expression databases

BgeeiENSSSCG00000020785.
GenevisibleiP02540. SS.

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).HMP:

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000021504.

Structurei

3D structure databases

ProteinModelPortaliP02540.
SMRiP02540.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini109 – 417IF rodIEP:Add BLAST309

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 109HeadAdd BLAST108
Regioni110 – 142Coil 1AAdd BLAST33
Regioni143 – 152Linker 110
Regioni153 – 253Coil 1BAdd BLAST101
Regioni254 – 269Linker 12Add BLAST16
Regioni269 – 416Interaction with NEBHMP:Add BLAST148
Regioni270 – 288Coil 2AAdd BLAST19
Regioni289 – 296Linker 28
Regioni297 – 413Coil 2BAdd BLAST117
Regioni414 – 471TailAdd BLAST58
Regioni439 – 454Interaction with CRYABHMP:Add BLAST16

Compositional bias

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

Sequence similaritiesi

Belongs to the intermediate filament family.IEP:

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IFZ1. Eukaryota.
ENOG410XRBS. LUCA.
GeneTreeiENSGT00830000128228.
HOVERGENiHBG013015.
InParanoidiP02540.
KOiK07610.
OMAiNQRARVE.
OrthoDBiEOG091G12MK.
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.

P02540-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQAYSSSQR VSSYRRTFGG APSFPLGSPL SSPVFPRAGF GTKGSSSSVT
60 70 80 90 100
SRVYQVSRTS GGAGGLGPLR ASRLGATRVP SSSYGAGELL DFSLADAVNQ
110 120 130 140 150
EFLTTRTNEK VELQELNDRF ANYIEKVRFL EQQNAALAAE VNRLKGREPT
160 170 180 190 200
RVAEIYEEEL RELRRQVEVL TNQRARVDVE RDNLLDDLQR LKAKLQEEIQ
210 220 230 240 250
LKEEAENNLA AFRADVDAAT LARIDLERRI ESLNEEIAFL KKVHEEEIRE
260 270 280 290 300
LQAQLQEQQV QVEMDMSKPD LTAALRDIRA QYETIAAKNI SEAEEWYKSK
310 320 330 340 350
VSDLTQAANK NNDALRQAKQ EMMEYRHQIQ SYTCEIDALK GTNDSLMRQM
360 370 380 390 400
RELEDRFASE ASGYQDNIAR LEEEIRHLKD EMARHLREYQ DLLNVKMALD
410 420 430 440 450
VEIATYRKLL EGEESRINLP IQTFSALNFR ETSPEQRGSE VHTKKTVMIK
460 470
TIETRDGEVV SEATQQQHEV L
Length:471
Mass (Da):53,629
Last modified:January 23, 2007 - v4
Checksum:i4D6992271A004630
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB011676 Genomic DNA. Translation: BAA25136.1.
AB011674 mRNA. Translation: BAA25134.1.
AF136188 mRNA. Translation: AAD46492.1.
AF363284 mRNA. Translation: AAK51087.1.
PIRiA02955. DMPG.
RefSeqiNP_001001535.1. NM_001001535.1.
UniGeneiSsc.24.

Genome annotation databases

EnsembliENSSSCT00000030104; ENSSSCP00000021504; ENSSSCG00000020785.
GeneIDi396725.
KEGGissc:396725.

Similar proteinsi

Entry informationi

Entry nameiDESM_PIG
AccessioniPrimary (citable) accession number: P02540
Secondary accession number(s): O62656
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: October 25, 2017
This is version 117 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families