function: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.,online information:SUMO protein entry,PTM:Cleavage of precursor form by SENP1 or SENP2 is necessary for function.,PTM:Cleavage of precursor form by SENP1, SENP2 or SENP5 is necessary for function.,PTM:Polymeric chains can be formed through Lys-11 cross-linking.,similarity:Belongs to the ubiquitin family. SUMO subfamily.,similarity:Contains 1 ubiquitin-like domain.,subcellular location:Nuclear bodies.,subunit: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.,subunit:Interacts with SAE2 and UBE2I. Covalently attached to a number of proteins.,tissue specificity:Broadly expressed.,tissue specificity:Expressed predominantly in liver.,
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Function:
proteolysis, macromolecule catabolic process, protein sumoylation, modification-dependent protein catabolic process,protein catabolic process, protein modification by small protein conjugation, modification-dependent macromolecule catabolic process, cellular protein catabolic process, cellular macromolecule catabolic process, proteolysis involved in cellular protein catabolic process, protein modification by small protein conjugation or removal,