SENP3

Protein-coding gene in humans
SENP3
Identifiers
AliasesSENP3, SMT3IP1, SSP3, Ulp1, SUMO1/sentrin/SMT3 specific peptidase 3, SUMO specific peptidase 3
External IDsOMIM: 612844; MGI: 2158736; HomoloGene: 9236; GeneCards: SENP3; OMA:SENP3 - orthologs
Gene location (Human)
Chromosome 17 (human)
Chr.Chromosome 17 (human)[1]
Chromosome 17 (human)
Genomic location for SENP3
Genomic location for SENP3
Band17p13.1Start7,561,919 bp[1]
End7,571,969 bp[1]
Gene location (Mouse)
Chromosome 11 (mouse)
Chr.Chromosome 11 (mouse)[2]
Chromosome 11 (mouse)
Genomic location for SENP3
Genomic location for SENP3
Band11|11 B3Start69,563,941 bp[2]
End69,572,910 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • right hemisphere of cerebellum

  • right frontal lobe

  • mucosa of transverse colon

  • anterior cingulate cortex

  • ganglionic eminence

  • anterior pituitary

  • ventricular zone

  • muscle layer of sigmoid colon

  • right lung

  • right testis
Top expressed in
  • neural layer of retina

  • epiblast

  • spermatocyte

  • ciliary body

  • cumulus cell

  • maxillary prominence

  • mandibular prominence

  • ventricular zone

  • superior frontal gyrus

  • dentate gyrus of hippocampal formation granule cell
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • peptidase activity
  • cysteine-type peptidase activity
  • endopeptidase activity
  • protein binding
  • hydrolase activity
Cellular component
  • cytoplasm
  • nucleolus
  • nucleus
  • nucleoplasm
  • MLL1 complex
Biological process
  • proteolysis
  • rRNA processing
  • protein desumoylation
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

26168

80886

Ensembl

ENSG00000161956

ENSMUSG00000005204

UniProt

Q9H4L4

Q9EP97

RefSeq (mRNA)

NM_015670

NM_001163571
NM_030702

RefSeq (protein)

NP_056485

NP_001157043
NP_109627

Location (UCSC)Chr 17: 7.56 – 7.57 MbChr 11: 69.56 – 69.57 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

SUMO1/sentrin/SMT3 specific peptidase 3, also known as SENP3, is a protein which in humans is encoded by the SENP3 gene.[5][6]

SENP3 together with SENP5, belongs to the Ulp1 branch in yeast and localize to nucleolus through B23/NPM1. SENP3 is associated and regulated by B23/nucleophosmin/NPM1 and involved in the regulation of ribosome biogenesis. SENP3 may be regulated by Arf-Mdm2-p53 pathway.[7]

Further reading

  • Yeh ET, Gong L, Kamitani T (2000). "Ubiquitin-like proteins: new wines in new bottles". Gene. 248 (1–2): 1–14. doi:10.1016/S0378-1119(00)00139-6. PMID 10806345.
  • Nishida T, Tanaka H, Yasuda H (2000). "A novel mammalian Smt3-specific isopeptidase 1 (SMT3IP1) localized in the nucleolus at interphase". Eur. J. Biochem. 267 (21): 6423–7. doi:10.1046/j.1432-1327.2000.01729.x. PMID 11029585.
  • Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
  • Wiemann S, Weil B, Wellenreuther R, et al. (2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Res. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
  • Simpson JC, Wellenreuther R, Poustka A, et al. (2001). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing". EMBO Rep. 1 (3): 287–92. doi:10.1093/embo-reports/kvd058. PMC 1083732. PMID 11256614.
  • 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • 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.
  • Colland F, Jacq X, Trouplin V, et al. (2004). "Functional proteomics mapping of a human signaling pathway". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.
  • 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. PMC 528928. PMID 15489334.
  • Wiemann S, Arlt D, Huber W, et al. (2004). "From ORFeome to biology: a functional genomics pipeline". Genome Res. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMC 528930. PMID 15489336.
  • Bouras T, Fu M, Sauve AA, et al. (2005). "SIRT1 deacetylation and repression of p300 involves lysine residues 1020/1024 within the cell cycle regulatory domain 1". J. Biol. Chem. 280 (11): 10264–76. doi:10.1074/jbc.M408748200. PMID 15632193.
  • Andersen JS, Lam YW, Leung AK, et al. (2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. Bibcode:2005Natur.433...77A. doi:10.1038/nature03207. PMID 15635413. S2CID 4344740.
  • Grégoire S, Yang XJ (2005). "Association with class IIa histone deacetylases upregulates the sumoylation of MEF2 transcription factors". Mol. Cell. Biol. 25 (6): 2273–87. doi:10.1128/MCB.25.6.2273-2287.2005. PMC 1061617. PMID 15743823.
  • Mehrle A, Rosenfelder H, Schupp I, et al. (2006). "The LIFEdb database in 2006". Nucleic Acids Res. 34 (Database issue): D415–8. doi:10.1093/nar/gkj139. PMC 1347501. PMID 16381901.
  • Nousiainen M, Silljé HH, Sauer G, et al. (2006). "Phosphoproteome analysis of the human mitotic spindle". Proc. Natl. Acad. Sci. U.S.A. 103 (14): 5391–6. Bibcode:2006PNAS..103.5391N. doi:10.1073/pnas.0507066103. PMC 1459365. PMID 16565220.
  • Gong L, Yeh ET (2006). "Characterization of a family of nucleolar SUMO-specific proteases with preference for SUMO-2 or SUMO-3". J. Biol. Chem. 281 (23): 15869–77. doi:10.1074/jbc.M511658200. PMID 16608850.
  • Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.
  • Yun C, Wang Y, Mukhopadhyay D, et al. (2008). "Nucleolar protein B23/nucleophosmin regulates the vertebrate SUMO pathway through SENP3 and SENP5 proteases". J. Cell Biol. 183 (4): 589–95. doi:10.1083/jcb.200807185. PMC 2582899. PMID 19015314.
  • Haindl M, Harasim T, Eick D, Muller S (March 2008). "The nucleolar SUMO-specific protease SENP3 reverses SUMO modification of nucleophosmin and is required for rRNA processing". EMBO Rep. 9 (3): 273–9. doi:10.1038/embor.2008.3. PMC 2267381. PMID 18259216.
  • Kuo ML, den Besten W, Thomas MC, et al. (2008). "Arf-induced turnover of the nucleolar nucleophosmin-associated SUMO-2/3 protease Senp3". Cell Cycle. 7 (21): 3378–87. doi:10.4161/cc.7.21.6930. PMID 18948745.


References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000161956 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000005204 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Yeh ET, Gong L, Kamitani T (May 2000). "Ubiquitin-like proteins: new wines in new bottles". Gene. 248 (1–2): 1–14. doi:10.1016/S0378-1119(00)00139-6. PMID 10806345.
  6. ^ Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Böcher M, Blöcker H, Bauersachs S, Blum H, Lauber J, Düsterhöft A, Beyer A, Köhrer K, Strack N, Mewes HW, Ottenwälder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A (March 2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Res. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
  7. ^ "Entrez Gene: SENP3 SUMO1/sentrin/SMT3 specific peptidase 3".


  • v
  • t
  • e