A diagram of ubiquitin. The seven lysine sidechains are shown in yellow/orange. Identifiers Symbol ubiquitin Available protein structures:;; Ubiquitin is a small (8.6 ) found in most tissues of organisms, i.e. It was discovered in 1975 by Gideon Goldstein and further characterized throughout the 1970s and 1980s. Four genes in the code for ubiquitin:,,. The addition of ubiquitin to a substrate protein is called ubiquitination (or, less frequently, ubiquitylation or ubiquitinylation).

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Ubiquitination affects proteins in many ways: it can mark them for via the, alter their, affect their activity, and promote or prevent. Ubiquitination involves three main steps: activation, conjugation, and ligation, performed by (E1s), (E2s), and (E3s), respectively. The result of this sequential cascade is to bind ubiquitin to residues on the protein substrate via an, residues through a, and residues through an, or the amino group of the protein's via a. The protein modifications can be either a single ubiquitin protein (monoubiquitination) or a chain of ubiquitin (polyubiquitination). Secondary ubiquitin molecules are always linked to one of the seven residues or the N-terminal of the previous ubiquitin molecule. These 'linking' residues are represented by a 'K' or 'M' (the of lysine and methionine, respectively) and a number, referring to its position in the ubiquitin molecule as in K48, K29 or M1. The first ubiquitin molecule is covalently bound through its C-terminal carboxylate group to a particular lysine, cysteine, serine, threonine or N-terminus of the target protein.

Poly-ubiquitination occurs when the C-terminus of another ubiquitin, is then linked to one of the seven lysine residues or the first methionine on the previously added ubiquitin molecule, creating a chain. This process repeats several times, leading to the addition of several ubiquitins. Only poly-ubiquitination on defined lysines, mostly on K48 and K29, is related to degradation by the (referred to as the 'molecular kiss of death'), while other polyubiquitinations (e.g. On K63, K11, K6 and M1) and monoubiquitinations may regulate processes such as,,. The discovery that ubiquitin chains target proteins to the proteasome, which degrades and recycles proteins, was honored with the in chemistry in 2004. Surface representation of Ubiquitin. Ubiquitin (originally, ubiquitous immunopoietic polypeptide) was first identified in 1975 as an 8.6 protein of unknown function expressed in all cells.

The basic functions of ubiquitin and the components of the ubiquitination pathway were elucidated in the early 1980s at the by,, and for which the was awarded in 2004. The ubiquitination system was initially characterised as an -dependent system present in cellular extracts. A heat-stable present in these extracts, ATP-dependent proteolysis factor 1 (APF-1), was found to become covalently attached to the model protein substrate in an - and 2+-dependent process. Multiple APF-1 molecules were linked to a single molecule by an linkage, and conjugates were found to be rapidly degraded with the release of free APF-1. Soon after APF-1-protein conjugation was characterised, APF-1 was identified as ubiquitin.

The carboxyl group of the C-terminal glycine residue of ubiquitin (Gly76) was identified as the moiety conjugated to substrate residues. The protein [ ] Ubiquitin properties (human) Number of residues 76 8564.8448 (pI) 6.79 Gene names (UBA80, UBCEP1), (UBCEP2),, Sequence in MQIFV KTLTG KTITLEVEPSDTIENV KA KIQD KEGIPPD QQRLIFAG KQLEDGRTLSDYNIQ KESTLHLVLRLRGG Ubiquitin is a small that exists in all. It performs its myriad functions through conjugation to a large range of target proteins.

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A variety of can occur. The ubiquitin protein itself consists of 76 and has a of about 8.6 kDa. Key features include its C-terminal tail and the 7 residues. It is highly conserved throughout eukaryote evolution; human and yeast ubiquitin share 96%. Genes [ ] Ubiquitin is encoded in mammals by 4 different genes. And genes code for a single copy of ubiquitin fused to the ribosomal proteins L40 and S27a, respectively.

The and genes code for polyubiquitin precursor proteins. Origins [ ] Ubiquitin is believed to have descended from prokaryotic proteins similar to. These prokaryotic proteins, despite having little sequence identity (ThiS has 14% identity to ubiquitin), share the same protein fold. These proteins also share sulfur chemistry with ubiquitin. MoaD, which is involved in biosynthesis, interacts with MoeB, which acts like an for MoaD, strengthening the link between these prokaryotic proteins and the ubiquitin system. A similar system exists for ThiS, with its E1-like enzyme ThiF.