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Protein Domain : IPR019956

Name  Ubiquitin Short Name  Ubiquitin
Type  Family Description  Ubiquitinylation is an ATP-dependent process that involves the action of at least three enzymes: a ubiquitin-activating enzyme (E1, ), a ubiquitin-conjugating enzyme (E2, ), and a ubiquitin ligase (E3, , ), which work sequentially in a cascade. There are many different E3 ligases, which are responsible for the type of ubiquitin chain formed, the specificity of the target protein, and the regulation of the ubiquitinylation process []. Ubiquitinylation is an important regulatory tool that controls the concentration of key signalling proteins, such as those involved in cell cycle control, as well as removing misfolded, damaged or mutant proteins that could be harmful to the cell. Several ubiquitin-like molecules have been discovered, such as Ufm1 (), SUMO1 (), NEDD8, Rad23 (), Elongin B and Parkin (), the latter being involved in Parkinson's disease [].Ubiquitin is a protein of 76 amino acid residues, found in all eukaryotic cells and whose sequence is extremely well conserved from protozoan to vertebrates. Ubiquitin acts through its post-translational attachment (ubiquitinylation) to other proteins, where these modifications alter the function, location or trafficking of the protein, or targets it for destruction by the 26S proteasome []. The terminal glycine in the C-terminal 4-residue tail of ubiquitin can form an isopeptide bond with a lysine residue in the target protein, or with a lysine in another ubiquitin molecule to form a ubiquitin chain that attaches itself to a target protein. Ubiquitin has seven lysine residues, any one of which can be used to link ubiquitin molecules together, resulting in different structures that alter the target protein in different ways. It appears that Lys(11)-, Lys(29) and Lys(48)-linked poly-ubiquitin chains target the protein to the proteasome for degradation, while mono-ubiquitinylated and Lys(6)- or Lys(63)-linked poly-ubiquitin chains signal reversible modifications in protein activity, location or trafficking []. For example, Lys(63)-linked poly-ubiquitinylation is known to be involved in DNA damage tolerance, inflammatory response, protein trafficking and signal transduction through kinase activation []. In addition, the length of the ubiquitin chain alters the fate of the target protein. Regulatory proteins such as transcription factors and histones are frequent targets of ubquitinylation [].

Publication Counts Displayer

0 Child Features

1 Contains

DB identifier Name Short Name Type
IPR019954 Ubiquitin conserved site Ubiquitin_CS Conserved_site

1 Cross References

Source . Name

Subject . Primary Identifier
PR00348 PRINTS IPR019956

2 Data Sets

Name URL
Swiss-Prot data set
InterPro data set  

0 Found In

0 GO Annotation

0 Ontology Annotations

0 Parent Features

67 Proteins

DB identifier Primary Accession
Organism . Name
FBpp0073035 P0CG69 Drosophila melanogaster
FBpp0079606 P15357 Drosophila melanogaster
FBpp0080733 Q9VJ33 Drosophila melanogaster
FBpp0305700 R9PY16 Drosophila melanogaster
FBpp0082817 Q9VEP9 Drosophila melanogaster
FBpp0077159 P18101 Drosophila melanogaster
FBpp0070894 Q9W418 Drosophila melanogaster
FBpp0291618 I5AMR3 Drosophila pseudoobscura
FBpp0276130 B5DVA8 Drosophila pseudoobscura
FBpp0280758 Q29LT5 Drosophila pseudoobscura
FBpp0285214 Q29NP1 Drosophila pseudoobscura
FBpp0281785 Q297I7 Drosophila pseudoobscura
FBpp0165699 B4KFP9 Drosophila mojavensis
FBpp0159835 B4KHP5 Drosophila mojavensis
FBpp0161987 B4KXU3 Drosophila mojavensis
FBpp0163489 B4LAP3 Drosophila mojavensis
FBpp0166389 B4KJQ0 Drosophila mojavensis
FBpp0170743 B4L5F4 Drosophila mojavensis
FBpp0172964 B4KBM1 Drosophila mojavensis
FBpp0173096 B4KCD3 Drosophila mojavensis
FBpp0225010 B4M5K1 Drosophila virilis
FBpp0230417 B4MAX6 Drosophila virilis
FBpp0230485 B4MGL9 Drosophila virilis
FBpp0232095 B4LSJ8 Drosophila virilis
FBpp0257703 B4PAD3 Drosophila yakuba
FBpp0261482 B4PYQ8 Drosophila yakuba
FBpp0263026 B4PH74 Drosophila yakuba
FBpp0265678 B4PH73 Drosophila yakuba
FBpp0271126 B4PM97 Drosophila yakuba
RS27A_CAEBR P37164 Caenorhabditis briggsae