Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Desmin

Gene

Des

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Names & Taxonomyi

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

Organism-specific databases

RGDi620686. Des.

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

  • gap junction Source: BHF-UCL
  • intercalated disc Source: UniProtKB
  • sarcolemma Source: UniProtKB
  • type III intermediate filament Source: RGD
  • Z disc Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Intermediate filament, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 469469DesminPRO_0000063775Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei12 – 121Phosphoserine; by AURKBBy similarity
Modified residuei17 – 171Phosphothreonine; by AURKBBy similarity
Modified residuei25 – 251PhosphoserineCombined sources
Modified residuei28 – 281PhosphoserineCombined sources
Modified residuei31 – 311PhosphoserineBy similarity
Modified residuei32 – 321PhosphoserineCombined sources
Modified residuei45 – 451PhosphoserineCombined sources
Modified residuei58 – 581ADP-ribosylarginine1 Publication
Modified residuei60 – 601Phosphoserine; by AURKBBy similarity
Modified residuei68 – 681PhosphoserineCombined sources
Modified residuei81 – 811PhosphoserineCombined sources
Modified residuei289 – 2891PhosphoserineCombined sources
Modified residuei357 – 3571PhosphoserineCombined sources
Modified residuei360 – 3601PhosphoserineCombined sources
Modified residuei423 – 4231PhosphoserineCombined sources

Post-translational modificationi

ADP-ribosylation prevents ability to form intermediate filaments.

Keywords - PTMi

ADP-ribosylation, Phosphoprotein

Proteomic databases

PaxDbiP48675.
PRIDEiP48675.

PTM databases

iPTMnetiP48675.
PhosphoSiteiP48675.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiP48675. 3 interactions.
STRINGi10116.ENSRNOP00000026860.

Structurei

3D structure databases

ProteinModelPortaliP48675.
SMRiP48675. Positions 105-142, 332-410.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 108108HeadAdd
BLAST
Regioni109 – 411303RodAdd
BLAST
Regioni109 – 14032Coil 1AAdd
BLAST
Regioni141 – 15010Linker 1
Regioni151 – 251101Coil 1BAdd
BLAST
Regioni252 – 26716Linker 12Add
BLAST
Regioni268 – 28619Coil 2AAdd
BLAST
Regioni287 – 2948Linker 2
Regioni295 – 411117Coil 2BAdd
BLAST
Regioni412 – 46958TailAdd
BLAST

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IFZ1. Eukaryota.
ENOG410XRBS. LUCA.
HOGENOMiHOG000230977.
HOVERGENiHBG013015.
InParanoidiP48675.
KOiK07610.
PhylomeDBiP48675.

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.

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP48675.
SMRiP48675. Positions 105-142, 332-410.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP48675. 3 interactions.
STRINGi10116.ENSRNOP00000026860.

PTM databases

iPTMnetiP48675.
PhosphoSiteiP48675.

Proteomic databases

PaxDbiP48675.
PRIDEiP48675.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi64362.
KEGGirno:64362.
UCSCiRGD:620686. rat.

Organism-specific databases

CTDi1674.
RGDi620686. Des.

Phylogenomic databases

eggNOGiENOG410IFZ1. Eukaryota.
ENOG410XRBS. LUCA.
HOGENOMiHOG000230977.
HOVERGENiHBG013015.
InParanoidiP48675.
KOiK07610.
PhylomeDBiP48675.

Miscellaneous databases

NextBioi613070.
PROiP48675.

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

« Hide 'large scale' publications
  1. "Rat desmin gene structure and expression."
    van Groningen J.J.M., Bloemers H.P.J., Swart G.W.M.
    Biochim. Biophys. Acta 1217:107-109(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Wistar.
    Tissue: Aorta.
  2. "Characterization of ADP-ribosylation sites on desmin and restoration of desmin intermediate filament assembly by de-ADP-ribosylation."
    Zhou H., Huiatt T.W., Robson R.M., Sernett S.W., Graves D.J.
    Arch. Biochem. Biophys. 334:214-222(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: ADP-RIBOSYLATION AT ARG-58.
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-28; SER-32; SER-45; SER-68; SER-81; SER-289; SER-357; SER-360 AND SER-423, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDESM_RAT
AccessioniPrimary (citable) accession number: P48675
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 108 of the entry and version 2 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.