Function: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or as a lysine-linked polymer. Covalent attachment via an isopeptide bond 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. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Polymeric SUMO2 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. Ref.7 Ref.15 Ref.16
Subunit structure: Homotrimer
Potential. Crystal packing analysis suggests a possible trimeric assembly, of which the biological significance remains to be determined. Interacts with SAE2 and UBE2I. Covalently attached to a number of proteins. Interacts with PELP1. Interacts with USP25; the interaction sumoylates USP25. Interacts with SIMC1, CASP8AP2, RNF111 AND SOBP (via SIM domains). Ref.11 Ref.14 Ref.15 Ref.19 Ref.20
Subcellular location: Nucleus. Nucleus › PML body Ref.7 Ref.10 Ref.18.
Tissue specificity: Broadly expressed. Ref.7
Post-translational modification: Polymeric chains can be formed through Lys-11 cross-linking. Polymeric SUMO2 chains undergo 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination by RNF4.Cleavage of precursor form by SENP1 or SENP2 is necessary for function.
Sequence similarities: Belongs to the ubiquitin family. SUMO subfamily.Contains 1 ubiquitin-like domain.
Caution: Frequently wrongly assigned as SMT3B in many databases and publications. However, according to initial nomenclature, SUMO2 corresponds to SMT3A (Ref.8).
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