Q5XFN2 · DESM_CANLF
- ProteinDesmin
- GeneDES
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids469 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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. Required for nuclear membrane integrity, via anchoring at the cell tip and nuclear envelope, resulting in maintenance of microtubule-derived intracellular mechanical forces (By similarity).
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
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
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 353 | Stutter | ||||
Sequence: D |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cell tip | |
Cellular Component | cell-cell junction | |
Cellular Component | cytoplasm | |
Cellular Component | intercalated disc | |
Cellular Component | intermediate filament | |
Cellular Component | nuclear envelope | |
Cellular Component | nucleus | |
Cellular Component | sarcolemma | |
Cellular Component | Z disc | |
Biological Process | intermediate filament organization | |
Biological Process | nuclear envelope organization | |
Biological Process | skeletal muscle organ development |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDesmin
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Carnivora > Caniformia > Canidae > Canis
Accessions
- Primary accessionQ5XFN2
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localizes in the intercalated disks which occur at the Z line of cardiomyocytes. Localizes in the nucleus exclusively in differentiating cardiac progenitor cells and premature cardiomyocytes. PKP2 is required for correct anchoring of DES at the cell tip and nuclear envelope (By similarity).
Keywords
- Cellular component
PTM/Processing
Features
Showing features for initiator methionine, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000063770 | 2-469 | Desmin | |||
Sequence: SQAYSSSQRVSSYRRTFGGAGGFPLGSPLGSPVFPRAGFGTKGSSSSVTSRVYQVSRTSGGAGGLGALRAGRLGTGRAPSYSAGELLDFSLADAVNQEFLTTRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKGREPTRVAEIYEEELRELRRQVEVLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEIRELQAQLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDALKGTNDSLMRQMREMEDRFASEASGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVEIATYRKLLEGEESRINLPIQTYSALNFRETSPEQRGSEVHTKKTVMIKTIETRDGEVVSEATQQQHEVL | ||||||
Modified residue | 7 | Phosphoserine; by CDK1 | ||||
Sequence: S | ||||||
Modified residue | 12 | Phosphoserine; by AURKB | ||||
Sequence: S | ||||||
Modified residue | 16 | Omega-N-methylarginine | ||||
Sequence: R | ||||||
Modified residue | 17 | Phosphothreonine; by AURKB and ROCK1 | ||||
Sequence: T | ||||||
Modified residue | 28 | Phosphoserine; by CDK1 | ||||
Sequence: S | ||||||
Modified residue | 32 | Phosphoserine; by CDK1 | ||||
Sequence: S | ||||||
Modified residue | 37 | Asymmetric dimethylarginine; alternate | ||||
Sequence: R | ||||||
Modified residue | 37 | Omega-N-methylarginine; alternate | ||||
Sequence: R | ||||||
Modified residue | 45 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 58 | ADP-ribosylarginine | ||||
Sequence: R | ||||||
Modified residue | 60 | Phosphoserine; by AURKB | ||||
Sequence: S | ||||||
Modified residue | 70 | Omega-N-methylarginine | ||||
Sequence: R | ||||||
Modified residue | 76 | Phosphothreonine; by ROCK1 | ||||
Sequence: T | ||||||
Modified residue | 81 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 289 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 357 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 360 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 423 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
ADP-ribosylation prevents ability to form intermediate filaments.
Phosphorylation at Ser-7, Ser-28 and Ser-32 by CDK1, phosphorylation at Ser-60 by AURKB and phosphorylation at Thr-76 by ROCK1 contribute to efficient separation of desmin intermediate filaments during mitosis.
Ubiquitination by a SCF-like complex containing ASB2 leads to proteasomal degradation.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Homomer (PubMed:24413773).
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).
Interacts with CRYAB (By similarity).
Interacts with NEB (via nebulin repeats 160-164) (By similarity).
Interacts (via rod region) with NEBL (via nebulin repeats 1-5) (By similarity).
Interacts with ASB2; the interaction targets DES for proteasomal degradation (By similarity).
Interacts with PKP1 (By similarity).
Interacts with FLII (By similarity).
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).
Interacts with CRYAB (By similarity).
Interacts with NEB (via nebulin repeats 160-164) (By similarity).
Interacts (via rod region) with NEBL (via nebulin repeats 1-5) (By similarity).
Interacts with ASB2; the interaction targets DES for proteasomal degradation (By similarity).
Interacts with PKP1 (By similarity).
Interacts with FLII (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 2-107 | Head | ||||
Sequence: SQAYSSSQRVSSYRRTFGGAGGFPLGSPLGSPVFPRAGFGTKGSSSSVTSRVYQVSRTSGGAGGLGALRAGRLGTGRAPSYSAGELLDFSLADAVNQEFLTTRTNE | ||||||
Domain | 107-415 | IF rod | ||||
Sequence: EKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKGREPTRVAEIYEEELRELRRQVEVLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEIRELQAQLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDALKGTNDSLMRQMREMEDRFASEASGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVEIATYRKLLEGEESRI | ||||||
Region | 108-140 | Coil 1A | ||||
Sequence: KVELQELNDRFANYIEKVRFLEQQNAALAAEVN | ||||||
Region | 141-150 | Linker 1 | ||||
Sequence: RLKGREPTRV | ||||||
Region | 151-251 | Coil 1B | ||||
Sequence: AEIYEEELRELRRQVEVLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEIRELQA | ||||||
Region | 252-267 | Linker 12 | ||||
Sequence: QLQEQQVQVEMDMSKP | ||||||
Region | 267-414 | Interaction with NEB | ||||
Sequence: PDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDALKGTNDSLMRQMREMEDRFASEASGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVEIATYRKLLEGEESR | ||||||
Region | 268-286 | Coil 2A | ||||
Sequence: DLTAALRDIRAQYETIAAK | ||||||
Region | 287-294 | Linker 2 | ||||
Sequence: NISEAEEW | ||||||
Region | 295-411 | Coil 2B | ||||
Sequence: YKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDALKGTNDSLMRQMREMEDRFASEASGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVEIATYRKLLEGE | ||||||
Region | 412-469 | Tail | ||||
Sequence: ESRINLPIQTYSALNFRETSPEQRGSEVHTKKTVMIKTIETRDGEVVSEATQQQHEVL | ||||||
Region | 437-452 | Interaction with CRYAB | ||||
Sequence: SEVHTKKTVMIKTIET |
Sequence similarities
Belongs to the intermediate filament family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length469
- Mass (Da)53,321
- Last updated2007-01-23 v3
- Checksum55A18E42D6D6C31B
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BK005142 EMBL· GenBank· DDBJ | DAA05325.1 EMBL· GenBank· DDBJ | Genomic DNA |