Entry - *612844 - SENTRIN-SPECIFIC PROTEASE FAMILY, MEMBER 3; SENP3 - OMIM

 
 
* 612844

SENTRIN-SPECIFIC PROTEASE FAMILY, MEMBER 3; SENP3


Alternative titles; symbols

SUMO-SPECIFIC PROTEASE 3


HGNC Approved Gene Symbol: SENP3

Cytogenetic location: 17p13.1   Genomic coordinates (GRCh38) : 17:7,561,919-7,571,969 (from NCBI)


TEXT

▼ Description

The reversible posttranslational modification of proteins by the addition of small ubiquitin-like SUMO proteins (see SUMO1; 601912) is required for numerous biologic processes. SUMO-specific proteases, such as SENP3, 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).


▼ Cloning and Expression

Gong and Yeh (2006) determined that C-terminal catalytic domain of the deduced 574-amino acid SENP3 protein shares 62% identity with that of SENP5 (612845). SENP3 and SENP5 also share 40% amino acid identity in a region directly preceding the catalytic domain. Gong and Yeh (2006) noted that SENP3 localizes to nucleoli.

Di Bacco et al. (2006) stated that the catalytic domain of SENP3 includes the catalytic triad of his, asp, and cys.


▼ Gene Function

Yun et al. (2008) found that SENP3 and SENP5 colocalized with nucleophosmin (NPM1; 164040), a protein involved in ribosome biogenesis, within the granular component of the nucleolus. Codepletion of SENP3 and SENP5 in HeLa cells via RNA interference (RNAi), but not depletion of either SENP alone, increased the nucleolar content of SUMO1, SUMO2 (603042), and SUMO3 (602231). Depletion of SENP3 alone inhibited production of 28S rRNA from the 32S precursor RNA, whereas depletion of SENP5 alone reduced 47S transcription. RNAi-mediated depletion of nucleophosmin reduced SENP3 and SENP5 levels, likely via increased degradation rather than decreased expression. Codepletion of SENP3 and SENP5 or depletion of nucleophosmin resulted in accumulation of sumoylated RPL37A and GNL2 (609365) proteins within nucleoli. Xenopus Senp5, which is highly similar to human SENP5, bound nucleophosmin in Xenopus oocyte extracts. Yun et al. (2008) concluded that sumoylation of nucleolar proteins by SENP3 and SENP5 is involved in the control of ribosome biogenesis.

Using epitope-tagged SENP3 in a protein pull-down assay of HEK293 cell lysates, Haindl et al. (2008) showed that SENP3 interacted with nucleophosmin. SENP3 countered ARF (600160)-induced sumoylation of nucleophosmin with SUMO2. Depletion of SENP3 by short interfering RNA interfered with nucleolar ribosomal RNA processing and inhibited conversion of the 32S rRNA species to the 28S form, phenocopying the defect observed upon nucleophosmin depletion. Furthermore, mimicking constitutive modification of nucleophosmin by SUMO2 interfered with 28S rRNA maturation. Haindl et al. (2008) concluded that SENP3 is an essential factor for ribosome biogenesis and that deconjugation of SUMO2 from nucleophosmin by SENP3 is critical for 28S rRNA maturation.


▼ Mapping

Hartz (2009) mapped the SENP3 gene to chromosome 17p13.1 based on an alignment of the SENP3 sequence (GenBank AL050283) with the genomic sequence (build 36.1).

▼ REFERENCES

  1. Di Bacco, A., Ouyang, J., Lee, H.-Y., Catic, A., Ploegh, H., Gill, G. The SUMO-specific protease SENP5 is required for cell division. Molec. Cell. Biol. 26: 4489-4498, 2006. [PubMed: 16738315, images, related citations] [Full Text]

  2. Gong, L., Yeh, E. T. H. Characterization of a family of nucleolar SUMO-specific proteases with preference for SUMO-2 or SUMO-3. J. Biol. Chem. 281: 15869-15877, 2006. [PubMed: 16608850, related citations] [Full Text]

  3. Haindl, M., Harasim, T., Eick, D., Muller, S. The nucleolar SUMO-specific protease SENP3 reverses SUMO modification of nucleophosmin and is required for rRNA processing. EMBO Rep. 9: 273-279, 2008. [PubMed: 18259216, images, related citations] [Full Text]

  4. Hartz, P. A. Personal Communication. Baltimore, Md. 6/11/2009.

  5. Yun, C., Wang, Y., Mukhopadhyay, D., Backlund, P., Kolli, N., Yergey, A., Wilkinson, K. D., Dasso, M. Nucleolar protein B23/nucleophosmin regulates the vertebrate SUMO pathway through SENP3 and SENP5 proteases. J. Cell Biol. 183: 589-595, 2008. [PubMed: 19015314, images, related citations] [Full Text]


Creation Date:
Patricia A. Hartz : 6/11/2009
Edit History:
mgross : 06/11/2009

* 612844

SENTRIN-SPECIFIC PROTEASE FAMILY, MEMBER 3; SENP3


Alternative titles; symbols

SUMO-SPECIFIC PROTEASE 3


HGNC Approved Gene Symbol: SENP3

Cytogenetic location: 17p13.1   Genomic coordinates (GRCh38) : 17:7,561,919-7,571,969 (from NCBI)


TEXT

Description

The reversible posttranslational modification of proteins by the addition of small ubiquitin-like SUMO proteins (see SUMO1; 601912) is required for numerous biologic processes. SUMO-specific proteases, such as SENP3, 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).


Cloning and Expression

Gong and Yeh (2006) determined that C-terminal catalytic domain of the deduced 574-amino acid SENP3 protein shares 62% identity with that of SENP5 (612845). SENP3 and SENP5 also share 40% amino acid identity in a region directly preceding the catalytic domain. Gong and Yeh (2006) noted that SENP3 localizes to nucleoli.

Di Bacco et al. (2006) stated that the catalytic domain of SENP3 includes the catalytic triad of his, asp, and cys.


Gene Function

Yun et al. (2008) found that SENP3 and SENP5 colocalized with nucleophosmin (NPM1; 164040), a protein involved in ribosome biogenesis, within the granular component of the nucleolus. Codepletion of SENP3 and SENP5 in HeLa cells via RNA interference (RNAi), but not depletion of either SENP alone, increased the nucleolar content of SUMO1, SUMO2 (603042), and SUMO3 (602231). Depletion of SENP3 alone inhibited production of 28S rRNA from the 32S precursor RNA, whereas depletion of SENP5 alone reduced 47S transcription. RNAi-mediated depletion of nucleophosmin reduced SENP3 and SENP5 levels, likely via increased degradation rather than decreased expression. Codepletion of SENP3 and SENP5 or depletion of nucleophosmin resulted in accumulation of sumoylated RPL37A and GNL2 (609365) proteins within nucleoli. Xenopus Senp5, which is highly similar to human SENP5, bound nucleophosmin in Xenopus oocyte extracts. Yun et al. (2008) concluded that sumoylation of nucleolar proteins by SENP3 and SENP5 is involved in the control of ribosome biogenesis.

Using epitope-tagged SENP3 in a protein pull-down assay of HEK293 cell lysates, Haindl et al. (2008) showed that SENP3 interacted with nucleophosmin. SENP3 countered ARF (600160)-induced sumoylation of nucleophosmin with SUMO2. Depletion of SENP3 by short interfering RNA interfered with nucleolar ribosomal RNA processing and inhibited conversion of the 32S rRNA species to the 28S form, phenocopying the defect observed upon nucleophosmin depletion. Furthermore, mimicking constitutive modification of nucleophosmin by SUMO2 interfered with 28S rRNA maturation. Haindl et al. (2008) concluded that SENP3 is an essential factor for ribosome biogenesis and that deconjugation of SUMO2 from nucleophosmin by SENP3 is critical for 28S rRNA maturation.


Mapping

Hartz (2009) mapped the SENP3 gene to chromosome 17p13.1 based on an alignment of the SENP3 sequence (GenBank AL050283) with the genomic sequence (build 36.1).

REFERENCES

  1. Di Bacco, A., Ouyang, J., Lee, H.-Y., Catic, A., Ploegh, H., Gill, G. The SUMO-specific protease SENP5 is required for cell division. Molec. Cell. Biol. 26: 4489-4498, 2006. [PubMed: 16738315] [Full Text: https://doi.org/10.1128/MCB.02301-05]

  2. Gong, L., Yeh, E. T. H. Characterization of a family of nucleolar SUMO-specific proteases with preference for SUMO-2 or SUMO-3. J. Biol. Chem. 281: 15869-15877, 2006. [PubMed: 16608850] [Full Text: https://doi.org/10.1074/jbc.M511658200]

  3. Haindl, M., Harasim, T., Eick, D., Muller, S. The nucleolar SUMO-specific protease SENP3 reverses SUMO modification of nucleophosmin and is required for rRNA processing. EMBO Rep. 9: 273-279, 2008. [PubMed: 18259216] [Full Text: https://doi.org/10.1038/embor.2008.3]

  4. Hartz, P. A. Personal Communication. Baltimore, Md. 6/11/2009.

  5. Yun, C., Wang, Y., Mukhopadhyay, D., Backlund, P., Kolli, N., Yergey, A., Wilkinson, K. D., Dasso, M. Nucleolar protein B23/nucleophosmin regulates the vertebrate SUMO pathway through SENP3 and SENP5 proteases. J. Cell Biol. 183: 589-595, 2008. [PubMed: 19015314] [Full Text: https://doi.org/10.1083/jcb.200807185]


Creation Date:
Patricia A. Hartz : 6/11/2009

Edit History:
mgross : 06/11/2009



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OMIM® and Online Mendelian Inheritance in Man® are registered trademarks of the Johns Hopkins University.
Copyright® 1966-2024 Johns Hopkins University.

NOTE: OMIM is intended for use primarily by physicians and other professionals concerned with genetic disorders, by genetics researchers, and by advanced students in science and medicine. While the OMIM database is open to the public, users seeking information about a personal medical or genetic condition are urged to consult with a qualified physician for diagnosis and for answers to personal questions.
OMIM® and Online Mendelian Inheritance in Man® are registered trademarks of the Johns Hopkins University.
Copyright® 1966-2024 Johns Hopkins University.
Printed: Nov. 16, 2024