SUMO2 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, CBX4 or ZNF451. 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. Plays a role in the regulation of sumoylation status of SETX. Belongs to the ubiquitin family. SUMO subfamily. Broadly expressed. 2 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
Protein type: Ubiquitin-like modifier
Chromosomal Location of human Ortholog: 17q25.1
Cellular Component:  nucleoplasm; nucleus; PML body
Molecular Function:  protein binding; SUMO transferase activity; transcription corepressor binding; ubiquitin protein ligase binding
Biological Process:  positive regulation of proteasomal ubiquitin-dependent protein catabolic process; positive regulation of transcription by RNA polymerase II; protein sumoylation
Reference #:  P61956 (UniProtKB)
Alt. Names/Synonyms: HSMT3; MGC117191; sentrin 2; Sentrin-2; small ubiquitin like modifier 2; small ubiquitin-like modifier 2; Small ubiquitin-related modifier 2; SMT3 homolog 2; SMT3 suppressor of mif two 3 homolog 2; SMT3 suppressor of mif two 3 homolog 2 (S. cerevisiae); Smt3A; SMT3B; SMT3H2; SUMO-2; SUMO-3; SUMO2; SUMO3; ubiquitin-like protein SMT3A; Ubiquitin-like protein SMT3B
Gene Symbols: SUMO2
Molecular weight: 10,871 Da
Basal Isoelectric point: 5.32  Predict pI for various phosphorylation states
CST Pathways:  IL6 Signaling  |  NF-kB Signaling  |  Protein Acetylation
Protein-Specific Antibodies, siRNAs or Recombinant Proteins from Cell Signaling Technology® Total Proteins
Select Structure to View Below


Protein Structure Not Found.

Cross-references to other databases:  AlphaFold  |  STRING  |  cBioPortal  |  Wikipedia  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Pfam  |  RCSB PDB  |  Phospho3D  |  Phospho.ELM  |  NetworKIN  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene  |  InnateDB  |  Ensembl Protein