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Protein

Desmin

Gene

DES

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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
Sitei354Stutter1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Enzyme and pathway databases

ReactomeiR-BTA-390522. Striated Muscle Contraction.

Names & Taxonomyi

Protein namesi
Recommended name:
Desmin
Gene namesi
Name:DES
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 2

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_00000637691 – 470DesminAdd BLAST470

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 residuei290PhosphoserineBy similarity1
Modified residuei358PhosphoserineBy similarity1
Modified residuei361PhosphoserineBy similarity1
Modified residuei424PhosphoserineBy similarity1

Post-translational modificationi

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

Keywords - PTMi

ADP-ribosylation, Methylation, Phosphoprotein

Proteomic databases

PaxDbiO62654.
PeptideAtlasiO62654.
PRIDEiO62654.

Expressioni

Gene expression databases

BgeeiENSBTAG00000005353.

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

STRINGi9913.ENSBTAP00000007041.

Structurei

3D structure databases

ProteinModelPortaliO62654.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 108HeadAdd BLAST108
Regioni109 – 412RodAdd BLAST304
Regioni109 – 141Coil 1AAdd BLAST33
Regioni142 – 151Linker 110
Regioni152 – 252Coil 1BAdd BLAST101
Regioni253 – 268Linker 12Add BLAST16
Regioni269 – 287Coil 2AAdd BLAST19
Regioni288 – 295Linker 28
Regioni296 – 412Coil 2BAdd BLAST117
Regioni413 – 470TailAdd 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.
HOGENOMiHOG000230977.
HOVERGENiHBG013015.
InParanoidiO62654.
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.

O62654-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQAYSSSQR VSSYRRTFGG APSFPLGSPL SSPVFPRAGF GTKGSSSSVT
60 70 80 90 100
SRVYQVSRTS GGAGGLGALR ASRLGSTRVP SSYGAGELLD FSLADAVNQE
110 120 130 140 150
FLTTRTNEKV ELQELNDRFA NYIEKVRFLE QQNAALAAEV NRLKGREPTR
160 170 180 190 200
VAEIYEEELR ELRRQVEVLT NQRARVDVER DNLLDDLQRL KAKLQEEIQL
210 220 230 240 250
KEEAENNLAA FRADVDAATL ARIDLERRIE SLNEEIAFLK KVHEEEIREL
260 270 280 290 300
QAQLQEQQVQ VEMDMSKPDL TAALRDIRAQ YETIAAKNIS EAEEWYKSKV
310 320 330 340 350
SDLTQAANKN NDALRQAKQE MMEYRHQIQS YTCEIDALKG TNDSLMRQMR
360 370 380 390 400
ELEDRFASEA SGYQDNIARL EEEIRHLKDE MARHLREYQD LLNVKMALDV
410 420 430 440 450
EIATYRKLLE GEESRINLPI QTFSALNFRE TSPEQRGSEV HTKKTVMIKT
460 470
IETRDGEVVS EATQQQHEVL
Length:470
Mass (Da):53,532
Last modified:January 23, 2007 - v3
Checksum:iB642D20280B3FD54
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB011675 Genomic DNA. Translation: BAA25135.1.
AB011673 mRNA. Translation: BAA25133.1.
BC133410 mRNA. Translation: AAI33411.1.
RefSeqiNP_001075044.1. NM_001081575.1.
UniGeneiBt.6141.

Genome annotation databases

EnsembliENSBTAT00000007041; ENSBTAP00000007041; ENSBTAG00000005353.
GeneIDi280765.
KEGGibta:280765.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB011675 Genomic DNA. Translation: BAA25135.1.
AB011673 mRNA. Translation: BAA25133.1.
BC133410 mRNA. Translation: AAI33411.1.
RefSeqiNP_001075044.1. NM_001081575.1.
UniGeneiBt.6141.

3D structure databases

ProteinModelPortaliO62654.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000007041.

Proteomic databases

PaxDbiO62654.
PeptideAtlasiO62654.
PRIDEiO62654.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000007041; ENSBTAP00000007041; ENSBTAG00000005353.
GeneIDi280765.
KEGGibta:280765.

Organism-specific databases

CTDi1674.

Phylogenomic databases

eggNOGiENOG410IFZ1. Eukaryota.
ENOG410XRBS. LUCA.
GeneTreeiENSGT00830000128228.
HOGENOMiHOG000230977.
HOVERGENiHBG013015.
InParanoidiO62654.
KOiK07610.
OMAiANEASGY.
OrthoDBiEOG091G12MK.
TreeFamiTF330122.

Enzyme and pathway databases

ReactomeiR-BTA-390522. Striated Muscle Contraction.

Gene expression databases

BgeeiENSBTAG00000005353.

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_BOVIN
AccessioniPrimary (citable) accession number: O62654
Secondary accession number(s): A2VDU8, O62655
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 113 of the entry and version 3 of the sequence. [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

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.