SUMO2

Small ubiquitin-related modifier 2 is a protein that in humans is encoded by the SUMO2 gene.^[5]

SUMO2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1WM2, 1WM3, 1WZ0, 2AWT, 2CKH, 2D07, 2IO0, 2IO3, 2IYD, 2RPQ, 3UIN, 3UIO, 3ZO5, 4BKG, 4NPN, 2N9E, 5D2M, 2N1W
Identifiers
Aliases	SUMO2, HSMT3, SMT3B, SMT3H2, SUMO3, Smt3A, small ubiquitin-like modifier 2, small ubiquitin like modifier 2
External IDs	OMIM: 603042; MGI: 2158813; HomoloGene: 87858; GeneCards: SUMO2; OMA:SUMO2 - orthologs
Gene location (Human) Chr. Chromosome 17 (human)[1] Band 17q25.1 Start 75,165,586 bp[1] End 75,182,959 bp[1]
Gene location (Mouse) Chr. Chromosome 11 (mouse)[2] Band 11|11 E2 Start 115,413,928 bp[2] End 115,427,102 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in ganglionic eminence ventricular zone mucosa of paranasal sinus endothelial cell lower lobe of lung superficial temporal artery islet of Langerhans cerebellar vermis oocyte monocyte Top expressed in tail of embryo morula neural tube mesencephalon epiblast ganglionic eminence embryo ventricular zone genital tubercle ovary More reference expression data BioGPS n/a
Gene ontology Molecular function protein binding ubiquitin protein ligase binding protein tag RNA binding transcription corepressor binding SUMO transferase activity ubiquitin-like protein ligase binding Cellular component PML body nucleus nucleoplasm Biological process global genome nucleotide-excision repair positive regulation of proteasomal ubiquitin-dependent protein catabolic process protein sumoylation positive regulation of transcription by RNA polymerase II Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 6613 170930 Ensembl ENSG00000188612 ENSMUSG00000020738 UniProt P61956 P61957 RefSeq (mRNA) NM_001005849 NM_006937 NM_133354 RefSeq (protein) NP_001005849 NP_008868 NP_579932 Location (UCSC) Chr 17: 75.17 – 75.18 Mb Chr 11: 115.41 – 115.43 Mb PubMed search [3] [4]
Wikidata
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Function

This gene encodes a protein that is a member of the SUMO (small ubiquitin-like modifier) protein family. It is a ubiquitin-like protein and functions in a manner similar to ubiquitin in that it is bound to target proteins as part of a post-translational modification system. However, unlike ubiquitin, which is primarily associated with targeting proteins for proteasomal degradation, SUMO2 is involved in a variety of cellular processes, such as nuclear transport, transcriptional regulation, apoptosis, and protein stability. It is not active until the last two amino acids of the carboxy-terminus have been cleaved off. Numerous pseudogenes have been reported for this gene. Alternate transcriptional splice variants encoding different isoforms have been characterized.^[6]

Interactions

SUMO2 has been shown to interact with TRIM63^[7] and CFAP298.^[8]

Clinical significance

Deep hypothermia protects the brain from ischemic injury, which is why it's employed for major cardiovascular procedures that necessitate cardiopulmonary bypass and a period of circulatory arrest. With an experiment ^[9] conducted to moderate hypothermia, small ubiquitin-like modifier (SUMO1-3) conjugation was significantly activated in the brain. The effects of hypothermia on SUMO conjugation were evaluated in this experiment^[9] using Western blot and immunohistochemistry in animals that were either normothermic (37 °C) or deep to moderate (18 °C, 24 °C, 30 °C) hypothermic cardiopulmonary bypass. In these cells, even 30 °C hypothermia was enough to significantly boost SUMO2/3-conjugated protein levels and nucleus accumulation. Deep hypothermia caused the SUMO-conjugating enzyme Ubc9 to translocate to the nucleus, implying that the increase in nuclear levels of SUMO2/3-conjugated proteins seen in hypothermic animals' brains is an active process. Deep hypothermia caused only a small increase in the amounts of SUMO2/3-conjugated proteins in primary neuronal cells. This shows that neurons in vivo have a greater capacity to activate this endogenous possibly neuroprotective mechanism when exposed to hypothermia than neurons in vitro. Identifying proteins that are SUMO2/3 conjugated during hypothermia could aid in the development of new preventive and therapeutic therapies to make neurons more resistant to a transient blood supply interruption.