SENP8

From Wikipedia, the free encyclopedia


SUMO/sentrin specific peptidase family member 8
PDB rendering based on 1xt9.
Available structures: 1xt9, 2bkq, 2bkr
Identifiers
Symbol(s) SENP8; DEN1; HsT17512; NEDP1; PRSC2
External IDs OMIM: 608659 MGI1918849 HomoloGene14084
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 123228 71599
Ensembl ENSG00000166192 ENSMUSG00000051705
Uniprot Q96LD8 Q3UWN3
Refseq NM_145204 (mRNA)
NP_660205 (protein)
NM_027838 (mRNA)
NP_082114 (protein)
Location Chr 15: 70.19 - 70.22 Mb Chr 9: 59.53 - 59.55 Mb
Pubmed search [1] [2]

SUMO/sentrin specific peptidase family member 8, also known as SENP8, is a human gene.[1]

NEDD8 (MIM 603171) is a ubiquitin-like protein that becomes conjugated to the cullin (see CUL1; MIM 603134) subunit of several ubiquitin ligases. This conjugation, called neddylation, is required for optimal ubiquitin ligase activity. NEDD8-specific deneddylases, such as NEDP1, or DEN1, are required to process the NEDD8 propeptide at a C-terminal diglycine motif and to remove NEDD8 from cullins (Gan-Erdene et al., 2003).[supplied by OMIM][1]

[edit] References

[edit] Further reading

  • Mikolajczyk J, Drag M, Békés M, Cao JT, Ronai Z, Salvesen GS. (2007). "Small ubiquitin-related modifier (SUMO)-specific proteases: profiling the specificities and activities of human SENPs.". J. Biol. Chem. 282 (36): 26217–24. doi:10.1074/jbc.M702444200. PMID 17591783. 
  • Drag M, Mikolajczyk J, Krishnakumar IM, Huang Z, Salvesen GS. (2008). "Activity profiling of human deSUMOylating enzymes (SENPs) with synthetic substrates suggests an unexpected specificity of two newly characterized members of the family.". Biochem J. 409 (2): 461–9. doi:10.1042/BJ20070940. PMID 17916063. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932. 
  • Mendoza HM, Shen LN, Botting C, et al. (2003). "NEDP1, a highly conserved cysteine protease that deNEDDylates Cullins.". J. Biol. Chem. 278 (28): 25637–43. doi:10.1074/jbc.M212948200. PMID 12730221. 
  • Gan-Erdene T, Nagamalleswari K, Yin L, et al. (2003). "Identification and characterization of DEN1, a deneddylase of the ULP family.". J. Biol. Chem. 278 (31): 28892–900. doi:10.1074/jbc.M302890200. PMID 12759362. 
  • Wu K, Yamoah K, Dolios G, et al. (2003). "DEN1 is a dual function protease capable of processing the C terminus of Nedd8 and deconjugating hyper-neddylated CUL1.". J. Biol. Chem. 278 (31): 28882–91. doi:10.1074/jbc.M302888200. PMID 12759363. 
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039. 
  • Xirodimas DP, Saville MK, Bourdon JC, et al. (2004). "Mdm2-mediated NEDD8 conjugation of p53 inhibits its transcriptional activity.". Cell 118 (1): 83–97. doi:10.1016/j.cell.2004.06.016. PMID 15242646. 
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334. 
  • Reverter D, Wu K, Erdene TG, et al. (2005). "Structure of a complex between Nedd8 and the Ulp/Senp protease family member Den1.". J. Mol. Biol. 345 (1): 141–51. doi:10.1016/j.jmb.2004.10.022. PMID 15567417. 
  • Shen LN, Liu H, Dong C, et al. (2005). "Structural basis of NEDD8 ubiquitin discrimination by the deNEDDylating enzyme NEDP1.". EMBO J. 24 (7): 1341–51. doi:10.1038/sj.emboj.7600628. PMID 15775960.