※ Browse result(s) for Pupylation

•  There are 245 proteins containing lysine Pupylation site(s) in the PLMD database

•  About lysine Pupylation

Pupylation was recently discovered as the ubiquitous protein post-translational modification on lysine in prokaryotic actinomycetes, which could be reversibly regulated. Comparable with eukaryotes, the prokaryotic ubiquitin-like protein functioned as the tag signaling, while this system as only found in actinomycetes. In contrast to ubiquitination controlled by E1, E2 and E3 in eukaryotes, the pupylation procedure contain two steps. The PUP -GGQ C-terminal is first deamidated to -GGE by Dop/PafD, and then conjugated to specific lysine residues of substrates catalyzed by PUP ligase PafA.

•  The distribution of species for the modified proteins:

Homo sapiens (0)Mus musculus (0)Saccharomyces cerevisiae (0)Rattus norvegicus (0)
Escherichia coli (51)Emericella nidulans (0)Mycobacterium tuberculosis (54)Arabidopsis thaliana (0)
Oryza sativa (0)Vibrio parahaemolyticus (0)Sulfolobus islandicus (0)Plasmodium falciparum (0)
Bacillus subtilis (0)Spiroplasma eriocheiris (0)Drosophila melanogaster (0)Schistosoma japonicum (0)
Phytophthora sojae (0)Bacillus velezensis (0)Corynebacterium glutamicum (0)Others (140)

•  Please select one organism to view the detailed proteins