SENP6 (6q14.1) , SSP1, SUSP1

SENP6 provided by HGNC

Official Full Name

SUMO specific peptidase 6 provided by HGNC

Also known as

SSP1; SUSP1

Summary

Ubiquitin-like molecules (UBLs), such as SUMO1 (UBL1; MIM 601912), are structurally related to ubiquitin (MIM 191339) and can be ligated to target proteins in a similar manner as ubiquitin. However, covalent attachment of UBLs does not result in degradation of the modified proteins. SUMO1 modification is implicated in the targeting of RANGAP1 (MIM 602362) to the nuclear pore complex, as well as in stabilization of I-kappa-B-alpha (NFKBIA; MIM 164008) from degradation by the 26S proteasome. Like ubiquitin, UBLs are synthesized as precursor proteins, with 1 or more amino acids following the C-terminal glycine-glycine residues of the mature UBL protein. Thus, the tail sequences of the UBL precursors need to be removed by UBL-specific proteases, such as SENP6, prior to their conjugation to target proteins (Kim et al., 2000 [PubMed 10799485]). SENPs also display isopeptidase activity for deconjugation of SUMO-conjugated substrates (Lima and Reverter, 2008 [PubMed 18799455]).[supplied by OMIM, Jun 2009]

Expression Ubiquitous expression in thyroid (RPKM 14.2), testis (RPKM 12.7) and 25 other tissues .

.

Preferred Names

sentrin-specific protease 6

Names

2810017C20Rik

SUMO-1-specific protease 1

SUMO1/sentrin specific peptidase 6

SUMO1/sentrin specific protease 6

sentrin/SUMO-specific protease SENP6

mRNA and Protein(s).  1105 aminoacid. (One NR site: lfrll ?)

NM_001100409.3 → NP_001093879.1  sentrin-specific protease 6 isoform 2

Related articles in PubMed

1. The Latency-Associated Nuclear Antigen of Kaposi's Sarcoma-Associated Herpesvirus Inhibits Expression of SUMO/Sentrin-Specific Peptidase 6 To Facilitate Establishment of Latency. Lin X, et al. J Virol, 2017 Sep 1. PMID 28615201, Free PMC Article
2. Structural insights into the SENP6 Loop1 structure in complex with SUMO2. Alegre KO, et al. Protein Sci, 2014 Apr. PMID 24424631, Free PMC Article
3. Structure of the human SENP7 catalytic domain and poly-SUMO deconjugation activities for SENP6 and SENP7. Lima CD, et al. J Biol Chem, 2008 Nov 14. PMID 18799455, Free PMC Article
4. Negative modulation of RXRalpha transcriptional activity by small ubiquitin-related modifier (SUMO) modification and its reversal by SUMO-specific protease SUSP1. Choi SJ, et al. J Biol Chem, 2006 Oct 13. PMID 16912044
5. A new SUMO-1-specific protease, SUSP1, that is highly expressed in reproductive organs. Kim KI, et al. J Biol Chem, 2000 May 12. PMID 10799485

See all (35) citations in PubMed

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

GeneRIFs: Gene References Into Functions

1. LANA could bind to the promoter region of the SENP6 gene and inhibit SENP6 expression while the regulated SENP6 could in turn modulate the abundance of LANA through desumoylation.
2. the structure of SENP2-Loop1 in complex with SUMO2 was solved at 2.15 A resolution, and reveals the details of anKim KI, et al. J Biol Chem, 2000 May 12. PMID 10799485 interface exclusive to SENP6/7 and the formation of unique contacts between both proteins
3. Loop 1 insertion in SENP6 and SENP7 as a platform to discriminate between SUMO1 and SUMO2/3 isoforms in this subclass of the SUMO protease family.
4. study of substrate specificity of SENP6; it is also capable of cleaving mixed chains of SUMO-1 and SUMO-2/3; mutation of catalytic cysteine of results in its accumulation in PML NBs; findings indicate SUMO-modified PML is a substrate of SENP6
5. Results reveal a novel mechanism whereby the finely balanced activities of SENP6 and RNF4 control vertebrate kinetochore assembly through SUMO-targeted destabilization of inner plate components.
6. SENP6 and SENP7 exhibit lower rates for processing pre-SUMO1, pre-SUMO2, or pre-SUMO3 in comparison with SENP2
7. SENP1 localization is influenced by expression and localization of SUMO-1-conjugated target proteins within the cell.
8. SUSP1 plays an important role in the control of the transcriptional activity of RXRalpha and thus in the RXRalpha-mediated cellular processes
9. We have investigated the specificity of SUSP1 using vinyl sulfone inhibitors and model substrates. SUSP1 has a strong paralogue bias toward SUMO2/3 and acts preferentially on substrates containing three or more SUMO2/3 moieties