SUMO3

SUMO proteins, such as SUMO3, and ubiquitin (see MIM 191339) posttranslationally modify numerous cellular proteins and affect their metabolism and function. However, unlike ubiquitination, which targets proteins for degradation, sumoylation participates in a number of cellular processes, such as nuclear transport, transcriptional regulation, apoptosis, and protein stability (Su and Li, 2002 [PubMed 12383504]).[supplied by OMIM

SMT3 suppressor of mif two 3 homolog 3 (S. cerevisiae)

Ubiquitin-like protein which can be covalently attached to target lysines either as a monomer or as a lysine-linked polymer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process. Plays a role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Covalent attachment to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4 (PubMed:11451954, PubMed:18538659, PubMed:21965678).
Plays a role in the regulation of sumoylation status of SETX (PubMed:24105744).

Biological Process negative regulation of DNA bindingManual Assertion Based On ExperimentIDA:CAFA
Biological Process protein sumoylationManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process regulation of protein localization to nucleusManual Assertion Based On ExperimentIDA:UniProtKB

Cytoplasm
Nucleus
Nucleus, PML body

Polymeric chains can be formed through Lys-11 cross-linking.
Cleavage of precursor form by SENP1, SENP2 or SENP5 is necessary for function.