SENP6

SENP6
Identifiers
Aliases	SENP6, SSP1, SUSP1, SUMO1/sentrin specific peptidase 6, SUMO specific peptidase 6
External IDs	OMIM: 605003; MGI: 1922075; HomoloGene: 9196; GeneCards: SENP6; OMA:SENP6 - orthologs
Gene location (Human) Chr. Chromosome 6 (human) Band 6q14.1 Start 75,601,509 bp End 75,718,281 bp
Gene location (Mouse) Chr. Chromosome 9 (mouse) Band 9|9 E1 Start 80,066,903 bp End 80,144,953 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Achilles tendon ventricular zone gastric mucosa right uterine tube sural nerve left ovary ganglionic eminence right ovary body of uterus left lobe of thyroid gland Top expressed in genital tubercle tail of embryo ventricular zone zygote granulocyte ganglionic eminence gastric mucosa left lung lobe mucous cell of stomach epithelium of stomach More reference expression data BioGPS More reference expression data
Gene ontology Molecular function peptidase activity cysteine-type peptidase activity protein binding hydrolase activity SUMO-specific endopeptidase activity Cellular component nucleus nucleoplasm cytosol cytoplasm Biological process protein desumoylation protein modification by small protein removal regulation of spindle assembly protein sumoylation proteolysis regulation of kinetochore assembly Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 26054 215351 Ensembl ENSG00000112701 ENSMUSG00000034252 UniProt Q9GZR1 Q6P7W0 RefSeq (mRNA) NM_001100409 NM_001304792 NM_015571 NM_146003 NM_001311110 RefSeq (protein) NP_001093879 NP_001291721 NP_056386 NP_001298039 NP_666115 Location (UCSC) Chr 6: 75.6 – 75.72 Mb Chr 9: 80.07 – 80.14 Mb PubMed search
Wikidata
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Sentrin-specific protease 6 is an enzyme that in humans is encoded by the SENP6 gene.

Function

Ubiquitin-like molecules (UBLs), such as SUMO1, are structurally related to ubiquitin 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 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

See also

• small ubiquitin-related modifier 1

Further reading

• Mikolajczyk J, Drag M, Békés M, Cao JT, Ronai Z, Salvesen GS (September 2007). "Small ubiquitin-related modifier (SUMO)-specific proteases: profiling the specificities and activities of human SENPs". The Journal of Biological Chemistry. 282 (36): 26217–24. doi:10.1074/jbc.M702444200. PMID 17591783.
• Drag M, Mikolajczyk J, Krishnakumar IM, Huang Z, Salvesen GS (January 2008). "Activity profiling of human deSUMOylating enzymes (SENPs) with synthetic substrates suggests an unexpected specificity of two newly characterized members of the family". The Biochemical Journal. 409 (2): 461–9. doi:10.1042/BJ20070940. PMID 17916063. S2CID 12234952.
• 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.
• Nagase T, Ishikawa K, Suyama M, Kikuno R, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (October 1998). "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Research. 5 (5): 277–86. doi:10.1093/dnares/5.5.277. PMID 9872452.
• Kim KI, Baek SH, Jeon YJ, Nishimori S, Suzuki T, Uchida S, Shimbara N, Saitoh H, Tanaka K, Chung CH (May 2000). "A new SUMO-1-specific protease, SUSP1, that is highly expressed in reproductive organs". The Journal of Biological Chemistry. 275 (19): 14102–6. doi:10.1074/jbc.275.19.14102. PMID 10799485.
• Goodson ML, Hong Y, Rogers R, Matunis MJ, Park-Sarge OK, Sarge KD (May 2001). "Sumo-1 modification regulates the DNA binding activity of heat shock transcription factor 2, a promyelocytic leukemia nuclear body associated transcription factor". The Journal of Biological Chemistry. 276 (21): 18513–8. doi:10.1074/jbc.M008066200. PMID 11278381.
• Tojo M, Matsuzaki K, Minami T, Honda Y, Yasuda H, Chiba T, Saya H, Fujii-Kuriyama Y, Nakao M (November 2002). "The aryl hydrocarbon receptor nuclear transporter is modulated by the SUMO-1 conjugation system". The Journal of Biological Chemistry. 277 (48): 46576–85. doi:10.1074/jbc.M205987200. PMID 12354770.
• Bailey D, O'Hare P (January 2004). "Characterization of the localization and proteolytic activity of the SUMO-specific protease, SENP1". The Journal of Biological Chemistry. 279 (1): 692–703. doi:10.1074/jbc.M306195200. PMID 14563852.
• Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (August 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America. 101 (33): 12130–5. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
• Choi SJ, Chung SS, Rho EJ, Lee HW, Lee MH, Choi HS, Seol JH, Baek SH, Bang OS, Chung CH (October 2006). "Negative modulation of RXRalpha transcriptional activity by small ubiquitin-related modifier (SUMO) modification and its reversal by SUMO-specific protease SUSP1". The Journal of Biological Chemistry. 281 (41): 30669–77. doi:10.1074/jbc.M604033200. PMID 16912044.
• Mukhopadhyay D, Ayaydin F, Kolli N, Tan SH, Anan T, Kametaka A, Azuma Y, Wilkinson KD, Dasso M (September 2006). "SUSP1 antagonizes formation of highly SUMO2/3-conjugated species" (PDF). The Journal of Cell Biology. 174 (7): 939–49. doi:10.1083/jcb.200510103. PMC 2064386. PMID 17000875.
• Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (November 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.