The small ubiquitin-related modifier SUMO-1 belongs to the growing family of ubiquitin-related proteins involved in post-translational protein modification. It is present in all eukaryotic kingdoms and is highly conserved from yeast to humans. Whereas invertebrates have only one SUMO gene, three members of the SUMO family have been described in vertebrates, SUMO-1 and the close homologues SUMO-2 and SUMO-3 with some 50% homology between SUMO-1 and SUMO-2/3. The SUMO family members have a short N-terminal extension that is absent in ubiquitin, and the function of which is unknown and the sequence of which varies between the three family members. Unlike ubiquitin, SUMO-1 does not appear to target proteins for degradation but seems to be involved in the modulation of protein-protein interactions. Although having only 18% amino acid sequence identity with ubiquitin, the overall structure closely resembles that of ubiquitin. Whereas the two C-terminal glycine residues required for isopeptide bond formation are conserved between the two molecules, Lys48 found in ubiquitin, and required to generate ubiquitin polymers, is substituted by Gln69in SUMO-1 thereby providing an explanation of why SUMO-1 has not been observed to form polymers. An increasing number of SUMO-1 substrates are being described but three major substrates for SUMO-1 modification are RanGAP1, PML and IκBα proteins.
- For Immunoprecipitation, Western Blot
Recognizes human SUMO-1.
Type: Primary
Antigen: SUMO1
Clonality: Polyclonal
Clone:
Conjugation:
Epitope:
Host: Rabbit
Isotype:
Reactivity: Human
