Small ubiquitin-related modifier 2 (SUMO2)
The protein contains 95 amino acids for an estimated molecular weight of 10871 Da.
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 (PubMed:26524494). 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 (PubMed:18408734, PubMed:18538659, PubMed:21965678, PubMed:9556629). Plays a role in the regulation of sumoylation status of SETX (PubMed:24105744). (updated: Oct. 10, 2018)
Protein identification was indicated in the following studies:
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
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| Variant | Description |
|---|---|
| dbSNP:rs17850328 |
The reference OMIM entry for this protein is 603042
Small ubiquitin-like modifier 2; sumo2
Smt3, yeast, homolog 2; smt3h2
Smt3b
Sentrin 2
DESCRIPTION
SUMO proteins, such as SUMO2, and ubiquitin (see 191339) posttranslationally modify numerous cellular proteins and affect their metabolism and function. However, unlike ubiquitination, which targets proteins for degradation, sumoylation participates in a number of cellular processes, such as nuclear transport, transcriptional regulation, apoptosis, and protein stability (Su and Li, 2002).CLONING
Sentrin (SUMO1; 601912), or SMT3H3, is a ubiquitin-like protein that can be conjugated to other proteins via a conserved glycine residue, after its C terminus is processed. SMT3H3 can covalently modify RANGAP1 (602362), a RAN (601179) GTPase-activating protein critically involved in nuclear transport. Kamitani et al. (1998) identified a human cDNA in the sequence databases that encodes sentrin-2, or SMT3H2, a novel member of the sentrin family of proteins. SMT3H2 is a deduced 95-amino acid polypeptide that contains a ubiquitin domain, an N-terminal extension, and the conserved C-terminal Gly-Gly residues. The amino acid sequence of SMT3H2 is 46% identical to that of SMT3H3. By Northern blot analysis, the authors found that SMT3H2 and SMT3H3 were expressed in all tissues examined. Adams et al. (1993) and Lapenta et al. (1997) independently isolated human expressed sequence tags encoding SMT3H2. Mannen et al. (1996) also cloned SMT3H2. Northern blot analysis of several human tissues detected SMT3H2 abundantly and ubiquitously expressed as a 1.35-kb transcript. Su and Li (2002) determined that all SUMO proteins from yeast to human share the conserved ubiquitin domain and the C-terminal diglycine cleavage/attachment site. The most prominent difference between SUMO proteins and ubiquitin is the presence of highly variable N-terminal extensions in the SUMO proteins. The mouse and human SUMO2 proteins are identical, and human SUMO2 shares 44% and 86% amino acid identity with SUMO1 and SUMO3 (602231), respectively. RT-PCR of HeLa, kidney, and neuronal cell lines indicated that expression of SUMO2 was intermediate between the high expression of SUMO1 and the low expression of SUMO3.GENE FUNCTION
Kamitani et al. (1998) observed that SMT3H2 formed a number of conjugates similar to those of SMT3H3, required cleavage of its C terminus for conjugation to occur, and underwent identical C-terminal processing as SMT3H3. Kamitani et al. (1998) showed that RANGAP1 could be modified by either SMT3H2 or SMT3H3, that the formation of the sentrinized RANGAP1 requires a covalent linkage between itself and SMT3H2 or SMT3H3, and that SMT3H2 derivatives are located predominantly in the nucleus. Dai and Liew (2001) demonstrated that RNF28 (606131) interacts with SMT3H2 through its RING domain. Su and Li (2002) found that expression of epitope-labeled SUMO2 in baby hamster fibroblasts resulted in its conjugation to many cellular proteins between 76 and 170 kD. Free SUMO2 was detected at about 20 kD. Immunofluorescent staining detected SUMO2 predominantly on nuclear bodies. SUMO1 and SUMO3 were predominantly detected on nuclear membranes and in the cytoplasm, respectively.GENE STRUCTURE
Su and Li (2002) reported that the SUMO2 gene contains 4 exons and spans about 14.9 kb.MAPPING
Su and Li (2002) reported that the SUMO2 gene maps to chromosome 17q25.1. There are 23 intronless SUMO2 pseudogenes that contain many mutations. ... More on the omim web site
June 30, 2020: Protein entry updated
Automatic update: OMIM entry 603042 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).