TY - JOUR

T1 - UBA domain containing proteins in fission yeast.

AU - Hartmann-Petersen, Rasmus

AU - Semple, Colin A M

AU - Ponting, Chris P

AU - Hendil, Klavs B

AU - Gordon, Colin

N1 - Keywords: Amino Acid Sequence; Animals; Carrier Proteins; Conserved Sequence; Ion Channels; Membrane Proteins; Mitochondrial Proteins; Molecular Sequence Data; Peptide Hydrolases; Proteasome Endopeptidase Complex; Protein Binding; Saccharomyces cerevisiae; Schizosaccharomyces; Schizosaccharomyces pombe Proteins; Ubiquitin

PY - 2003

Y1 - 2003

N2 - The ubiquitin-proteasome pathway for intracellular proteolysis is involved in a series of cellular and molecular functions, including the degradation of bulk proteins, cell cycle control, DNA repair, antigen presentation, vesicle transport and the regulation of signal transudation pathways and transcription. Considering this variety of cell biological processes, it is puzzling that until recently only very few proteins were known to possess the ability to interact specifically with ubiquitin chains. However, several ubiquitin binding proteins have now been identified and the binding domains have been characterised on both the functional and structural levels. One example of a widespread ubiquitin binding module is the ubiquitin associated (UBA) domain. Here, we discuss the approximately 15 UBA domain containing proteins encoded in the relatively small genome of the fission yeast Schizosaccharomyces pombe. The proteins display remarkable differences in their domain organisation, indicating that these potential ubiquitin binding proteins are involved in various cell activities.

AB - The ubiquitin-proteasome pathway for intracellular proteolysis is involved in a series of cellular and molecular functions, including the degradation of bulk proteins, cell cycle control, DNA repair, antigen presentation, vesicle transport and the regulation of signal transudation pathways and transcription. Considering this variety of cell biological processes, it is puzzling that until recently only very few proteins were known to possess the ability to interact specifically with ubiquitin chains. However, several ubiquitin binding proteins have now been identified and the binding domains have been characterised on both the functional and structural levels. One example of a widespread ubiquitin binding module is the ubiquitin associated (UBA) domain. Here, we discuss the approximately 15 UBA domain containing proteins encoded in the relatively small genome of the fission yeast Schizosaccharomyces pombe. The proteins display remarkable differences in their domain organisation, indicating that these potential ubiquitin binding proteins are involved in various cell activities.

U2 - 10.1016/S1357-2725(02)00393-X

DO - 10.1016/S1357-2725(02)00393-X

M3 - Journal article

C2 - 12672455

VL - 35

SP - 629

EP - 636

JO - International Journal of Biochemistry & Cell Biology

JF - International Journal of Biochemistry & Cell Biology

SN - 1357-2725

IS - 5

ER -