Description: Homo sapiens small ubiquitin-like modifier 2 (SUMO2), transcript variant 1, mRNA. RefSeq Summary (NM_006937): This gene encodes a protein that is a member of the SUMO (small ubiquitin-like modifier) protein family. It 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 targets proteins for degradation, this protein 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. [provided by RefSeq, Jul 2008]. Transcript (Including UTRs) Position: hg19 chr17:73,163,825-73,179,098 Size: 15,274 Total Exon Count: 4 Strand: - Coding Region Position: hg19 chr17:73,164,434-73,178,929 Size: 14,496 Coding Exon Count: 4
ID:SUMO2_HUMAN DESCRIPTION: RecName: Full=Small ubiquitin-related modifier 2; Short=SUMO-2; AltName: Full=HSMT3; AltName: Full=SMT3 homolog 2; AltName: Full=SUMO-3; AltName: Full=Sentrin-2; AltName: Full=Ubiquitin-like protein SMT3A; Short=Smt3A; Flags: Precursor; 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. 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. Interacts with USP25; the interaction sumoylates USP25. INTERACTION: P10242:MYB; NbExp=3; IntAct=EBI-473220, EBI-298355; Q8N2W9:PIAS4; NbExp=3; IntAct=EBI-473220, EBI-473160; SUBCELLULAR LOCATION: Nucleus. Note=Nuclear bodies. TISSUE SPECIFICITY: Broadly expressed. PTM: 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. PTM: Cleavage of precursor form by SENP1 or SENP2 is necessary for function. SIMILARITY: Belongs to the ubiquitin family. SUMO subfamily. SIMILARITY: 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 (PubMed:10692421). WEB RESOURCE: Name=Wikipedia; Note=SUMO protein entry; URL="http://en.wikipedia.org/wiki/SUMO_protein";
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on P61956
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
US Server
