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Gene Review

SENP1  -  SUMO1/sentrin specific peptidase 1

Homo sapiens

Synonyms: Sentrin-specific protease 1, Sentrin/SUMO-specific protease SENP1
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Disease relevance of SENP1


High impact information on SENP1

  • Both the NLS and the NES are located in the nonhomologous domains of SENP2 and are not conserved among other members of the SENP family [4].
  • Both reciprocal SENP1-MESDC2 (SEME) and MESDC2-SENP1 (MESE) fusion genes are transcribed in tumor-derived cells and their open reading frames encode aberrant proteins [5].
  • Using a PML desumoylation assay, we found that translocation-associated MESE proteins exhibit desumoylation capacities similar to those observed for WT SENP1 [5].
  • Thus, SENP1 could regulate AR-dependent transcription through desumoylation of HDAC1 [6].
  • The action of SENP1 on c-Jun transcription is independent of the sumoylation and phosphorylation status of c-Jun but is critically dependent on the desumoylation activity of SENP1 [7].

Chemical compound and disease context of SENP1


Biological context of SENP1


Anatomical context of SENP1

  • A COS cell expression system was used to demonstrate the activity of SENP1 in vivo [11].
  • In addition, sentrinized PML, a tumor suppressor protein that resides in the nucleus, was selectively affected by SENP1, whereas sentrinized RanGAP1, which is associated with the cytoplasmic fibrils of the nuclear pore complex, remained intact [11].
  • The tagged SUMO-1 was recruited into high molecular mass conjugates in the cell line, and expression of SENP1 promoted loss of these species, including the modified species of PML [12].

Associations of SENP1 with chemical compounds


Regulatory relationships of SENP1

  • Both ICP0 and SENP1 protease promoted the loss of SUMO-1 from the nucleus, observed both for the endogenous species and the cell line expressing the epitope-tagged SUMO-1 [12].

Other interactions of SENP1

  • HDAC1's repressive effect on AR-dependent transcription could be reversed by SENP1 and by deletion of its sumoylation sites [6].
  • Although SENP1 is rather similar in structure to the related protease SENP2, these proteases have different SUMO-processing activities [9].
  • SENP1 upregulation modulates the transcriptional activity of androgen receptors (ARs) and c-Jun, as well as cyclin D1 expression [2].


  1. Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1. Xu, Z., Au, S.W. Biochem. J. (2005) [Pubmed]
  2. Role of desumoylation in the development of prostate cancer. Cheng, J., Bawa, T., Lee, P., Gong, L., Yeh, E.T. Neoplasia (2006) [Pubmed]
  3. SUMO-specific protease 1 (SENP1) reverses the hormone-augmented SUMOylation of androgen receptor and modulates gene responses in prostate cancer cells. Kaikkonen, S., Jääskeläinen, T., Karvonen, U., Rytinki, M.M., Makkonen, H., Gioeli, D., Paschal, B.M., Palvimo, J.J. Mol. Endocrinol. (2009) [Pubmed]
  4. Nucleocytoplasmic shuttling modulates activity and ubiquitination-dependent turnover of SUMO-specific protease 2. Itahana, Y., Yeh, E.T., Zhang, Y. Mol. Cell. Biol. (2006) [Pubmed]
  5. Fusion of the SUMO/Sentrin-specific protease 1 gene SENP1 and the embryonic polarity-related mesoderm development gene MESDC2 in a patient with an infantile teratoma and a constitutional t(12;15)(q13;q25). Veltman, I.M., Vreede, L.A., Cheng, J., Looijenga, L.H., Janssen, B., Schoenmakers, E.F., Yeh, E.T., van Kessel, A.G. Hum. Mol. Genet. (2005) [Pubmed]
  6. SENP1 enhances androgen receptor-dependent transcription through desumoylation of histone deacetylase 1. Cheng, J., Wang, D., Wang, Z., Yeh, E.T. Mol. Cell. Biol. (2004) [Pubmed]
  7. Differential regulation of c-Jun-dependent transcription by SUMO-specific proteases. Cheng, J., Perkins, N.D., Yeh, E.T. J. Biol. Chem. (2005) [Pubmed]
  8. Desumoylation of homeodomain-interacting protein kinase 2 (HIPK2) through the cytoplasmic-nuclear shuttling of the SUMO-specific protease SENP1. Kim, Y.H., Sung, K.S., Lee, S.J., Kim, Y.O., Choi, C.Y., Kim, Y. FEBS Lett. (2005) [Pubmed]
  9. The structure of SENP1-SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing. Shen, L.N., Dong, C., Liu, H., Naismith, J.H., Hay, R.T. Biochem. J. (2006) [Pubmed]
  10. Inhibition of SUMO-independent PML oligomerization by the human cytomegalovirus IE1 protein. Kang, H., Kim, E.T., Lee, H.R., Park, J.J., Go, Y.Y., Choi, C.Y., Ahn, J.H. J. Gen. Virol. (2006) [Pubmed]
  11. Differential regulation of sentrinized proteins by a novel sentrin-specific protease. Gong, L., Millas, S., Maul, G.G., Yeh, E.T. J. Biol. Chem. (2000) [Pubmed]
  12. Herpes simplex virus 1 ICP0 co-localizes with a SUMO-specific protease. Bailey, D., O'Hare, P. J. Gen. Virol. (2002) [Pubmed]
  13. PIASy-mediated repression of the Ets-1 is independent of its sumoylation. Nishida, T., Terashima, M., Fukami, K. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  14. Crystal structure of the SENP1 mutant C603S-SUMO complex reveals the hydrolytic mechanism of SUMO-specific protease. Xu, Z., Chau, S.F., Lam, K.H., Chan, H.Y., Ng, T.B., Au, S.W. Biochem. J. (2006) [Pubmed]
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