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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.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei355 – 3551Stutter

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 471471DesminPRO_0000063774Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei12 – 121Phosphoserine; by AURKBBy similarity
Modified residuei17 – 171Phosphothreonine; by AURKBBy similarity
Modified residuei28 – 281PhosphoserineBy similarity
Modified residuei31 – 311PhosphoserineBy similarity
Modified residuei32 – 321PhosphoserineBy similarity
Modified residuei45 – 451PhosphoserineBy similarity
Modified residuei58 – 581ADP-ribosylarginineBy similarity
Modified residuei60 – 601Phosphoserine; by AURKBBy similarity
Modified residuei81 – 811PhosphoserineBy similarity
Modified residuei291 – 2911PhosphoserineBy similarity
Modified residuei359 – 3591PhosphoserineBy similarity
Modified residuei362 – 3621PhosphoserineBy similarity
Modified residuei425 – 4251PhosphoserineBy similarity

Post-translational modificationi

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

Keywords - PTMi

ADP-ribosylation, Phosphoprotein

Proteomic databases

PaxDbiP02540.
PeptideAtlasiP02540.
PRIDEiP02540.

Expressioni

Gene expression databases

GenevisibleiP02540. SS.

Interactioni

Subunit structurei

Homopolymer. Interacts with MTM1 and DST (By similarity).By similarity

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000021504.

Structurei

3D structure databases

ProteinModelPortaliP02540.
SMRiP02540. Positions 107-144, 334-412.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 109109HeadAdd
BLAST
Regioni110 – 413304RodAdd
BLAST
Regioni110 – 14233Coil 1AAdd
BLAST
Regioni143 – 15210Linker 1
Regioni153 – 253101Coil 1BAdd
BLAST
Regioni254 – 26916Linker 12Add
BLAST
Regioni270 – 28819Coil 2AAdd
BLAST
Regioni289 – 2968Linker 2
Regioni297 – 413117Coil 2BAdd
BLAST
Regioni414 – 47158TailAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi45 – 484Poly-Ser

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IFZ1. Eukaryota.
ENOG410XRBS. LUCA.
GeneTreeiENSGT00830000128228.
HOVERGENiHBG013015.
InParanoidiP02540.
KOiK07610.
OMAiFPRTGFG.
OrthoDBiEOG7FV3Q8.
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.
SMRiP02540. Positions 107-144, 334-412.
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.
OMAiFPRTGFG.
OrthoDBiEOG7FV3Q8.
TreeFamiTF330122.

Enzyme and pathway databases

ReactomeiR-SSC-390522. Striated Muscle Contraction.

Gene expression databases

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...

Publicationsi

  1. "Desmin structure as related to meat tenderness."
    Chikuni K., Tanabe R., Muroya S.
    Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Tissue: Muscle.
  2. "Muscle ESTs II: cloning, sequencing and mapping the pig gene for the intermediate filament protein desmin (DES)."
    Tuggle C.K., Sanchez-Serrano I., Smith B., Marklund L., Ernst C.
    Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "A polymorphic CT-repeat at the porcine desmin locus with an effect on meat quality."
    Beuzen N.D., Hall A.D., Gallagher A., Chang K.-C.
    Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Longissimus muscle.
  4. "Comparison of the proteins of two immunologically distinct intermediate-sized filaments by amino acid sequence analysis: desmin and vimentin."
    Geisler N., Weber K.
    Proc. Natl. Acad. Sci. U.S.A. 78:4120-4123(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 334-471.

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: July 6, 2016
This is version 106 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.