Ubiquitin [1,2,3] is a protein of seventy six amino acid residues, found in
all eukaryotic cells and whose sequence is extremely well conserved from
protozoan to vertebrates. It plays a key role in a variety of cellular
processes, such as ATP-dependent selective degradation of cellular proteins,
maintenance of chromatin structure, regulation of gene expression, stress
response and ribosome biogenesis.
In most species, there are many genes coding for ubiquitin. However they can
be classified into two classes. The first class produces polyubiquitin
molecules consisting of exact head to tail repeats of ubiquitin. The number of
repeats is variable (up to twelve in a Xenopus gene). In the majority of
polyubiquitin precursors, there is a final amino-acid after the last repeat.
The second class of genes produces precursor proteins consisting of a single
copy of ubiquitin fused to a C-terminal extension protein (CEP). There are two
types of CEP proteins and both seem to be ribosomal proteins.
Ubiquitin is a globular protein, the last four C-terminal residues (Leu-Arg-Gly-Gly) extending from the compact structure to form a 'tail', important for
its function. The latter is mediated by the covalent conjugation of ubiquitin
to target proteins, by an isopeptide linkage between the C-terminal glycine
and the epsilon amino group of lysine residues in the target proteins.
There are a number of proteins which are evolutionary related to ubiquitin:
- Ubiquitin-like proteins from baculoviruses as well as in some strains of
bovine viral diarrhea viruses (BVDV). These proteins are highly similar to
their eukaryotic counterparts.
- Mammalian protein GDX . GDX is composed of two domains, a N-terminal
ubiquitin-like domain of 74 residues and a C-terminal domain of 83 residues
with some similarity with the thyroglobulin hormonogenic site.
- Mammalian protein FAU . FAU is a fusion protein which consist of a
N-terminal ubiquitin-like protein of 74 residues fused to ribosomal protein
- Mouse protein NEDD-8 , a ubiquitin-like protein of 81 residues.
- Human protein BAT3, a large fusion protein of 1132 residues that contains a
N-terminal ubiquitin-like domain.
- Caenorhabditis elegans protein ubl-1 . Ubl-1 is a fusion protein which
consist of a N-terminal ubiquitin-like protein of 70 residues fused to
ribosomal protein S27A.
- Yeast DNA repair protein RAD23 . RAD23 contains a N-terminal domain that
seems to be distantly, yet significantly, related to ubiquitin.
- Mammalian RAD23-related proteins RAD23A and RAD23B.
- Mammalian BCL-2 binding athanogene-1 (BAG-1). BAG-1 is a protein of 274
residues that contains a central ubiquitin-like domain.
- Human spliceosome associated protein 114 (SAP 114 or SF3A120).
- Yeast protein DSK2, a protein involved in spindle pole body duplication and
which contains a N-terminal ubiquitin-like domain.
- Human protein CKAP1/TFCB, Schizosaccharomyces pombe protein alp11 and
Caenorhabditis elegans hypothetical protein F53F4.3. These proteins contain
a N-terminal ubiquitin domain and a C-terminal CAP-Gly domain (see
- Schizosaccharomyces pombe hypothetical protein SpAC26A3.16. This protein
contains a N-terminal ubiquitin domain.
- Yeast protein SMT3.
- Human ubiquitin-like proteins SMT3A and SMT3B.
- Human ubiquitin-like protein SMT3C (also known as PIC1; Ubl1, Sumo-1; Gmp-1
or Sentrin). This protein is involved in targeting ranGAP1 to the nuclear
pore complex protein ranBP2.
- SMT3-like proteins in plants and Caenorhabditis elegans.
To identify ubiquitin and related proteins we have developed a pattern based
on conserved positions in the central section of the sequence. A profile was
also developed that spans the complete length of the ubiquitin domain.
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