SPOP

Disambiguation: For the animated series see She-Ra: Princess of Power.

Speckle-type POZ protein
PDB rendering based on 2cr2.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2CR2​, 3HQH​, 3HQI​, 3HQL​, 3HQM​, 3HSV​, 3HTM​, 3HU6​, 3IVB​, 3IVQ​, 3IVV​, 4EOZ​, 4HS2​, 4J8Z​, 4O1V​
Identifiers
Symbols	SPOP ; BTBD32; TEF2
External IDs	OMIM: 602650 MGI: 1343085 HomoloGene: 68354 GeneCards: SPOP Gene
Gene ontology Molecular function • RNA polymerase II transcription factor binding • protein binding • ubiquitin protein ligase binding Cellular component • nucleus • nucleoplasm • nuclear speck • Cul3-RING ubiquitin ligase complex Biological process • negative regulation of transcription from RNA polymerase II promoter • glucose homeostasis • protein ubiquitination involved in ubiquitin-dependent protein catabolic process • proteasome-mediated ubiquitin-dependent protein catabolic process • negative regulation of sequence-specific DNA binding transcription factor activity • positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway • positive regulation of type B pancreatic cell apoptotic process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	8405	20747
Ensembl	ENSG00000121067	ENSMUSG00000057522
UniProt	O43791	Q6ZWS8
RefSeq (mRNA)	NM_001007226	NM_025287
RefSeq (protein)	NP_001007227	NP_079563
Location (UCSC)	Chr 17: 49.6 – 49.68 Mb	Chr 11: 95.41 – 95.49 Mb
PubMed search

Speckle-type POZ protein is a protein that in humans is encoded by the SPOP gene.^[1][2][3]

This gene encodes a protein that may modulate the transcriptional repression activities of death-associated protein 6 (DAXX), which interacts with histone deacetylase, core histones, and other histone-associated proteins. In mouse, the encoded protein binds to the putative leucine zipper domain of macroH2A1.2, a variant H2A histone that is enriched on inactivated X chromosomes. The BTB/POZ domain of this protein has been shown in other proteins to mediate transcriptional repression and to interact with components of histone deacetylase co-repressor complexes. Alternative splicing of this gene results in multiple transcript variants encoding the same protein.^[3]

Clinical relevance

Mutations in SPOP lead to a type of prostate tumor thought to be involved in about 15% of all prostate cancers.^[4][5]

References

1. Nagai Y, Kojima T, Muro Y, Hachiya T, Nishizawa Y, Wakabayashi T, Hagiwara M (Nov 1997). "Identification of a novel nuclear speckle-type protein, SPOP". FEBS Letters 418 (1-2): 23–6. doi:10.1016/S0014-5793(97)01340-9. PMID 9414087.
2. Zapata JM, Pawlowski K, Haas E, Ware CF, Godzik A, Reed JC (Jun 2001). "A diverse family of proteins containing tumor necrosis factor receptor-associated factor domains". The Journal of Biological Chemistry 276 (26): 24242–52. doi:10.1074/jbc.M100354200. PMID 11279055.
3. "Entrez Gene: SPOP speckle-type POZ protein".
4. Heidi Evans (20 May 2012). "Scientists find new type of prostate cancer - discovery may lead to tailored treatments". New York Daily News. Retrieved 20 May 2012.
5. Barbieri CE, Baca SC, Lawrence MS, Demichelis F, Blattner M, Theurillat JP, White TA, Stojanov P, Van Allen E, Stransky N, Nickerson E, Chae SS, Boysen G, Auclair D, Onofrio RC, Park K, Kitabayashi N, MacDonald TY, Sheikh K, Vuong T, Guiducci C, Cibulskis K, Sivachenko A, Carter SL, Saksena G, Voet D, Hussain WM, Ramos AH, Winckler W, Redman MC, Ardlie K, Tewari AK, Mosquera JM, Rupp N, Wild PJ, Moch H, Morrissey C, Nelson PS, Kantoff PW, Gabriel SB, Golub TR, Meyerson M, Lander ES, Getz G, Rubin MA, Garraway LA (Jun 2012). "Exome sequencing identifies recurrent SPOP, FOXA1 and MED12 mutations in prostate cancer". Nature Genetics 44 (6): 685–9. doi:10.1038/ng.2279. PMC 3673022. PMID 22610119.

Further reading

• Maruyama K, Sugano S (Jan 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Bonaldo MF, Lennon G, Soares MB (Sep 1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (Oct 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1-2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Wu J, Song Y, Bakker AB, Bauer S, Spies T, Lanier LL, Phillips JH (Jul 1999). "An activating immunoreceptor complex formed by NKG2D and DAP10". Science 285 (5428): 730–2. doi:10.1126/science.285.5428.730. PMID 10426994.
• Hartley JL, Temple GF, Brasch MA (Nov 2000). "DNA cloning using in vitro site-specific recombination". Genome Research 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
• Zapata JM, Pawlowski K, Haas E, Ware CF, Godzik A, Reed JC (Jun 2001). "A diverse family of proteins containing tumor necrosis factor receptor-associated factor domains". The Journal of Biological Chemistry 276 (26): 24242–52. doi:10.1074/jbc.M100354200. PMID 11279055.
• Takahashi I, Kameoka Y, Hashimoto K (Aug 2002). "MacroH2A1.2 binds the nuclear protein Spop". Biochimica Et Biophysica Acta 1591 (1-3): 63–8. doi:10.1016/S0167-4889(02)00249-5. PMID 12183056.
• Gilfillan S, Ho EL, Cella M, Yokoyama WM, Colonna M (Dec 2002). "NKG2D recruits two distinct adapters to trigger NK cell activation and costimulation". Nature Immunology 3 (12): 1150–5. doi:10.1038/ni857. PMID 12426564.
• Diefenbach A, Tomasello E, Lucas M, Jamieson AM, Hsia JK, Vivier E, Raulet DH (Dec 2002). "Selective associations with signaling proteins determine stimulatory versus costimulatory activity of NKG2D". Nature Immunology 3 (12): 1142–9. doi:10.1038/ni858. PMID 12426565.
• Billadeau DD, Upshaw JL, Schoon RA, Dick CJ, Leibson PJ (Jun 2003). "NKG2D-DAP10 triggers human NK cell-mediated killing via a Syk-independent regulatory pathway". Nature Immunology 4 (6): 557–64. doi:10.1038/ni929. PMID 12740575.
• Liu A, Desai BM, Stoffers DA (May 2004). "Identification of PCIF1, a POZ domain protein that inhibits PDX-1 (MODY4) transcriptional activity". Molecular and Cellular Biology 24 (10): 4372–83. doi:10.1128/MCB.24.10.4372-4383.2004. PMC 400448. PMID 15121856.
• La M, Kim K, Park J, Won J, Lee JH, Fu YM, Meadows GG, Joe CO (Jul 2004). "Daxx-mediated transcriptional repression of MMP1 gene is reversed by SPOP". Biochemical and Biophysical Research Communications 320 (3): 760–5. doi:10.1016/j.bbrc.2004.06.022. PMID 15240113.
• Wiemann S, Arlt D, Huber W, Wellenreuther R, Schleeger S, Mehrle A, Bechtel S, Sauermann M, Korf U, Pepperkok R, Sültmann H, Poustka A (Oct 2004). "From ORFeome to biology: a functional genomics pipeline". Genome Research 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMC 528930. PMID 15489336.
• Hernández-Muñoz I, Lund AH, van der Stoop P, Boutsma E, Muijrers I, Verhoeven E, Nusinow DA, Panning B, Marahrens Y, van Lohuizen M (May 2005). "Stable X chromosome inactivation involves the PRC1 Polycomb complex and requires histone MACROH2A1 and the CULLIN3/SPOP ubiquitin E3 ligase". Proceedings of the National Academy of Sciences of the United States of America 102 (21): 7635–40. doi:10.1073/pnas.0408918102. PMC 1140410. PMID 15897469.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
• Mehrle A, Rosenfelder H, Schupp I, del Val C, Arlt D, Hahne F, Bechtel S, Simpson J, Hofmann O, Hide W, Glatting KH, Huber W, Pepperkok R, Poustka A, Wiemann S (Jan 2006). "The LIFEdb database in 2006". Nucleic Acids Research 34 (Database issue): D415–8. doi:10.1093/nar/gkj139. PMC 1347501. PMID 16381901.