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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

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. May act as a sarcomeric microtubule-anchoring protein: specifically associates with detyrosinated tubulin-alpha chains, leading to buckled microtubules and mechanical resistance to contraction.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei355Stutter1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Muscle 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

  • CytoplasmmyofibrilsarcomereZ line By similarity
  • Cytoplasm By similarity
  • Cell membranesarcolemma By similarity

  • Note: Localizes in the intercalated disks which occur at the Z line of cardiomyocytes.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Intermediate filament, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000637741 – 471DesminAdd BLAST471

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei12Phosphoserine; by AURKBBy similarity1
Modified residuei16Omega-N-methylarginineBy similarity1
Modified residuei17Phosphothreonine; by AURKBBy similarity1
Modified residuei28PhosphoserineBy similarity1
Modified residuei31PhosphoserineBy similarity1
Modified residuei32PhosphoserineBy similarity1
Modified residuei37Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei37Omega-N-methylarginine; alternateBy similarity1
Modified residuei45PhosphoserineBy similarity1
Modified residuei58ADP-ribosylarginineBy similarity1
Modified residuei60Phosphoserine; by AURKBBy similarity1
Modified residuei70Omega-N-methylarginineBy similarity1
Modified residuei81PhosphoserineBy similarity1
Modified residuei291PhosphoserineBy similarity1
Modified residuei359PhosphoserineBy similarity1
Modified residuei362PhosphoserineBy similarity1
Modified residuei425PhosphoserineBy similarity1

Post-translational modificationi

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

Keywords - PTMi

ADP-ribosylation, Methylation, Phosphoprotein

Proteomic databases

PaxDbiP02540.
PeptideAtlasiP02540.
PRIDEiP02540.

Expressioni

Gene expression databases

BgeeiENSSSCG00000020785.
GenevisibleiP02540. SS.

Interactioni

Subunit structurei

Homopolymer. Interacts with DST (By similarity). Interacts with MTM1 (By similarity). Interacts with EPPK1; interaction is dependent of higher-order structure of intermediate filament (By similarity).By similarity

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000021504.

Structurei

3D structure databases

ProteinModelPortaliP02540.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 109HeadAdd BLAST109
Regioni110 – 413RodAdd BLAST304
Regioni110 – 142Coil 1AAdd BLAST33
Regioni143 – 152Linker 110
Regioni153 – 253Coil 1BAdd BLAST101
Regioni254 – 269Linker 12Add BLAST16
Regioni270 – 288Coil 2AAdd BLAST19
Regioni289 – 296Linker 28
Regioni297 – 413Coil 2BAdd BLAST117
Regioni414 – 471TailAdd BLAST58

Compositional bias

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

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IFZ1. Eukaryota.
ENOG410XRBS. LUCA.
GeneTreeiENSGT00830000128228.
HOVERGENiHBG013015.
InParanoidiP02540.
KOiK07610.
OMAiANEASGY.
OrthoDBiEOG091G12MK.
TreeFamiTF330122.

Family and domain databases

InterProiIPR027698. DES.
IPR001664. IF.
IPR006821. Intermed_filament_DNA-bd.
IPR018039. Intermediate_filament_CS.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PTHR23239:SF28. PTHR23239:SF28. 1 hit.
PfamiPF00038. Filament. 1 hit.
PF04732. Filament_head. 1 hit.
[Graphical view]
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP02540.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000021504.

Proteomic databases

PaxDbiP02540.
PeptideAtlasiP02540.
PRIDEiP02540.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1674.

Phylogenomic databases

eggNOGiENOG410IFZ1. Eukaryota.
ENOG410XRBS. LUCA.
GeneTreeiENSGT00830000128228.
HOVERGENiHBG013015.
InParanoidiP02540.
KOiK07610.
OMAiANEASGY.
OrthoDBiEOG091G12MK.
TreeFamiTF330122.

Enzyme and pathway databases

ReactomeiR-SSC-390522. Striated Muscle Contraction.

Gene expression databases

BgeeiENSSSCG00000020785.
GenevisibleiP02540. SS.

Family and domain databases

InterProiIPR027698. DES.
IPR001664. IF.
IPR006821. Intermed_filament_DNA-bd.
IPR018039. Intermediate_filament_CS.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PTHR23239:SF28. PTHR23239:SF28. 1 hit.
PfamiPF00038. Filament. 1 hit.
PF04732. Filament_head. 1 hit.
[Graphical view]
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDESM_PIG
AccessioniPrimary (citable) accession number: P02540
Secondary accession number(s): O62656
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 110 of the entry and version 4 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.