InterPro : 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 [].

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

1 Contains

Id Name Short Name Type
IPR019954 Ubiquitin conserved site Ubiquitin_CS Conserved_site

0 Found In

0 Parent Features

6 Publications

First Author Title Year Journal Volume Pages
Burger AM The ubiquitin-mediated protein degradation pathway in cancer: therapeutic implications. 2004 Eur J Cancer 40 2217-29
Passmore LA Getting into position: the catalytic mechanisms of protein ubiquitylation. 2004 Biochem J 379 513-25
Pickart CM Polyubiquitin chains: polymeric protein signals. 2004 Curr Opin Chem Biol 8 610-6
Hatakeyama S U-box proteins as a new family of ubiquitin ligases. 2003 Biochem Biophys Res Commun 302 635-45
Ross CA The ubiquitin-proteasome pathway in Parkinson's disease and other neurodegenerative diseases. 2004 Trends Cell Biol 14 703-11
de Napoles M Polycomb group proteins Ring1A/B link ubiquitylation of histone H2A to heritable gene silencing and X inactivation. 2004 Dev Cell 7 663-76

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)