SENP5 (3q29) , SUMO1/sentriinispesifinen peptidaasi 5

https://www.ncbi.nlm.nih.gov/gene/205564

Official Symbol

SENP5 provided by HGNC

Official Full Name

SUMO specific peptidase 5 provided by HGNC

Summary

The reversible posttranslational modification of proteins by the addition of small ubiquitin-like SUMO proteins (see SUMO1; MIM 601912) is required for numerous biologic processes. SUMO-specific proteases, such as SENP5, are responsible for the initial processing of SUMO precursors to generate a C-terminal diglycine motif required for the conjugation reaction. They also have isopeptidase activity for the removal of SUMO from high molecular mass SUMO conjugates (Di Bacco et al., 2006 [PubMed 16738315]).[supplied by OMIM, Jun 2009]

Expression

Ubiquitous expression in testis (RPKM 8.4), brain (RPKM 6.3) and 25 other tissues

Preferred Names

sentrin-specific protease 5

Names

SUMO1/sentrin specific peptidase 5

SUMO1/sentrin specific protease 5

sentrin/SUMO-specific protease SENP5

NM_001308045.1 → NP_001294974.1  sentrin-specific protease 5 isoform 2

Conserved Domains (1) summary

cl23802
Location:581 → 707

Peptidase_C48; Ulp1 protease family, C-terminal catalytic domain

Related articles in PubMed

1. Sentrin/small ubiquitin-like modifier-specific protease 5 protects oral cancer cells from oxidative stress-induced apoptosis. Cheng Y, et al. Mol Med Rep, 2015 Aug. PMID 25901414
2. SENP5 mediates breast cancer invasion via a TGFβRI SUMOylation cascade. Cashman R, et al. Oncotarget, 2014 Feb 28. PMID 24658161, Free PMC ArticleIdentifying novel mechanisms, which are at the core of breast cancer biology, is of critical importance. Such mechanisms may explain response to treatment, reveal novel targets or drive detection assays. To uncover such novel mechanisms, we used survival analysis on gene expression datasets encompassing 1363 patients. By iterating over the compendia of genes, we screened for their significance as prognosis biomarkers and identified SUMO-specific protease 5 (SENP5) to significantly stratify patients into two survival groups across five unrelated tested datasets. According to these findings, low expression of SENP5 is associated with good prognosis among breast cancer patients. Following these findings, we analyzed SENP5 silencing and show it is followed by inhibition of anchorage-independence growth, proliferation, migration and invasion in breast cancer cell lines. We further show that these changes are conducted via regulation of TGFβRI levels. These data relate to recent reports about the SUMOylation of TGFβRI. Following TGFβRI changes in expression, we show that one of its target genes, MMP9, which plays a key role in degrading the extracellular matrix and contributes to TGFβ-induced invasion, is dramatically down regulated upon SENP5 silencing. This is the first report represents SENP5-TGFβ-MMP9 cascade and its mechanistic involvement in breast cancer.
3. Overexpression of SENP5 in oral squamous cell carcinoma and its association with differentiation. Ding X, et al. Oncol Rep, 2008 Nov. PMID 18949399
4. The SUMO-specific protease SENP5 is required for cell division. Di Bacco A, et al. Mol Cell Biol, 2006 Jun. PMID 16738315, Free PMC Article
5. Nucleolar protein B23/nucleophosmin regulates the vertebrate SUMO pathway through SENP3 and SENP5 proteases. Yun C, et al. J Cell Biol, 2008 Nov 17. PMID 19015314, Free PMC Article

See all (18) citations in PubMed

See citations in PubMed for homologs of this gene provided by HomoloGene
 

GeneRIFs: Gene References Into Functions

1. Results from a study on gene expression variability markers in early-stage human embryos shows that SENP5 is a putative expression variability marker for the 3-day, 8-cell embryo stage.
2. Mild oxidative stress stabilized the SENP5 protein in the oral squamous cell carcinoma cells, and only the combination of SENP5 silencing and H2O2 application led to mitochondria fragmentation and a significant increase in cell apoptosis.
3. Low expression of SENP5 is associated with good prognosis among breast cancer patients.
4. altered subcellular localization of SENP5 in oral squamous cell carcinoma (OSCC) cells and the correlation between SENP5 expression and the differentiation of OSCC.
5. Nucleolar protein B23/nucleophosmin regulates the vertebrate SUMO pathway through SENP3 and SENP5 proteases.
6. Knockdown of SENP5 resulted in increased levels of SUMO-1 and SUMO-2/3, inhibition of cell proliferation, defects in nuclear morphology, and appearance of binucleate cells, revealing an essential role for SENP5 in mitosis and/or cytokinesis.

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