SKIL

For other uses, see Skil (disambiguation).

Ski-like protein is a protein that in humans is encoded by the SKIL gene.

SKIL
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3EQ5
Identifiers
Aliases	SKIL, SNO, SnoA, SnoI, SnoN, SKI-like proto-oncogene, SKI like proto-oncogene
External IDs	OMIM: 165340; MGI: 106203; HomoloGene: 3948; GeneCards: SKIL; OMA:SKIL - orthologs
Gene location (Human) Chr. Chromosome 3 (human) Band 3q26.2 Start 170,357,678 bp End 170,396,835 bp
Gene location (Mouse) Chr. Chromosome 3 (mouse) Band 3 A3|3 15.12 cM Start 31,149,207 bp End 31,176,726 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in tendon of biceps brachii mucosa of paranasal sinus jejunal mucosa Achilles tendon Skeletal muscle tissue of biceps brachii visceral pleura epithelium of nasopharynx epithelium of colon endothelial cell superficial temporal artery Top expressed in molar cumulus cell external carotid artery pineal gland tunica media of zone of aorta ciliary body body of femur mesenteric lymph nodes internal carotid artery umbilical cord More reference expression data BioGPS More reference expression data
Gene ontology Molecular function DNA binding transcription corepressor activity protein domain specific binding RNA polymerase II cis-regulatory region sequence-specific DNA binding DNA-binding transcription repressor activity, RNA polymerase II-specific protein binding SMAD binding chromatin binding DNA-binding transcription factor activity, RNA polymerase II-specific protein-containing complex binding Cellular component cytoplasm PML body nucleoplasm acrosomal vesicle nucleus protein-containing complex Biological process positive regulation of extrinsic apoptotic signaling pathway via death domain receptors response to cytokine lymphocyte homeostasis response to antibiotic negative regulation of transcription by RNA polymerase II blastocyst formation positive regulation of axonogenesis protein homotrimerization lens fiber cell differentiation positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage spermatogenesis protein heterotrimerization response to growth factor skeletal muscle tissue development negative regulation of BMP signaling pathway transforming growth factor beta receptor signaling pathway negative regulation of transforming growth factor beta receptor signaling pathway neuron development negative regulation of cell differentiation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 6498 20482 Ensembl ENSG00000136603 ENSMUSG00000027660 UniProt P12757 Q60665 RefSeq (mRNA) NM_001145097 NM_001145098 NM_001248008 NM_005414 NM_001039090 NM_001271772 NM_011386 NM_001398558 NM_001398559 NM_001398560 RefSeq (protein) NP_001138569 NP_001138570 NP_001234937 NP_005405 NP_001034179 NP_001258701 NP_035516 NP_001385487 NP_001385488 NP_001385489 Location (UCSC) Chr 3: 170.36 – 170.4 Mb Chr 3: 31.15 – 31.18 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Interactions

SKIL interacts with SKI protein, Mothers against decapentaplegic homolog 3 and Mothers against decapentaplegic homolog 2.

Protein Family

SKIL belongs to the Ski/Sno/Dac family, shared by SKI protein, Dachshund, and SKIDA1. Members of the Ski/Sno/Dac family share a domain that is roughly 100 amino acids long.

Further reading

• Pearson-White S (1993). "SnoI, a novel alternatively spliced isoform of the ski protooncogene homolog, sno". Nucleic Acids Res. 21 (19): 4632–8. doi:10.1093/nar/21.19.4632. PMC 311202. PMID 8233802.
• Pearson-White S; Crittenden R (1997). "Proto-oncogene Sno expression, alternative isoforms and immediate early serum response". Nucleic Acids Res. 25 (14): 2930–7. doi:10.1093/nar/25.14.2930. PMC 146803. PMID 9207045.
• Cohen SB; Zheng G; Heyman HC; Stavnezer E (1999). "Heterodimers of the SnoN and Ski oncoproteins form preferentially over homodimers and are more potent transforming agents". Nucleic Acids Res. 27 (4): 1006–14. doi:10.1093/nar/27.4.1006. PMC 148280. PMID 9927733.
• Stroschein SL, Wang W, Zhou S, et al. (1999). "Negative feedback regulation of TGF-beta signaling by the SnoN oncoprotein". Science. 286 (5440): 771–4. doi:10.1126/science.286.5440.771. PMID 10531062.
• Bonni S, Wang HR, Causing CG, et al. (2001). "TGF-beta induces assembly of a Smad2-Smurf2 ubiquitin ligase complex that targets SnoN for degradation". Nat. Cell Biol. 3 (6): 587–95. doi:10.1038/35078562. PMID 11389444. S2CID 23270947.
• Imoto I, Pimkhaokham A, Fukuda Y, et al. (2001). "SNO is a probable target for gene amplification at 3q26 in squamous-cell carcinomas of the esophagus". Biochem. Biophys. Res. Commun. 286 (3): 559–65. doi:10.1006/bbrc.2001.5428. PMID 11511096.
• Stroschein SL; Bonni S; Wrana JL; Luo K (2001). "Smad3 recruits the anaphase-promoting complex for ubiquitination and degradation of SnoN". Genes Dev. 15 (21): 2822–36. doi:10.1101/gad.912901. PMC 312804. PMID 11691834.
• Mizuide M, Hara T, Furuya T, et al. (2003). "Two short segments of Smad3 are important for specific interaction of Smad3 with c-Ski and SnoN". J. Biol. Chem. 278 (1): 531–6. doi:10.1074/jbc.C200596200. PMID 12426322.
• 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.
• Tomsig JL; Snyder SL; Creutz CE (2003). "Identification of targets for calcium signaling through the copine family of proteins. Characterization of a coiled-coil copine-binding motif". J. Biol. Chem. 278 (12): 10048–54. doi:10.1074/jbc.M212632200. PMID 12522145.
• He J, Tegen SB, Krawitz AR, et al. (2003). "The transforming activity of Ski and SnoN is dependent on their ability to repress the activity of Smad proteins" (PDF). J. Biol. Chem. 278 (33): 30540–7. doi:10.1074/jbc.M304016200. PMID 12764135. S2CID 31081406.
• 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.
• Sarker KP; Wilson SM; Bonni S (2005). "SnoN is a cell type-specific mediator of transforming growth factor-beta responses". J. Biol. Chem. 280 (13): 13037–46. doi:10.1074/jbc.M409367200. PMID 15677458.
• Barrios-Rodiles M, Brown KR, Ozdamar B, et al. (2005). "High-throughput mapping of a dynamic signaling network in mammalian cells". Science. 307 (5715): 1621–5. Bibcode:2005Sci...307.1621B. doi:10.1126/science.1105776. PMID 15761153. S2CID 39457788.
• Poser I, Rothhammer T, Dooley S, et al. (2005). "Characterization of Sno expression in malignant melanoma". Int. J. Oncol. 26 (5): 1411–7. doi:10.3892/ijo.26.5.1411. PMID 15809735.
• Krakowski AR, Laboureau J, Mauviel A, et al. (2005). "Cytoplasmic SnoN in normal tissues and nonmalignant cells antagonizes TGF-β signaling by sequestration of the Smad proteins". Proc. Natl. Acad. Sci. U.S.A. 102 (35): 12437–42. Bibcode:2005PNAS..10212437K. doi:10.1073/pnas.0504107102. PMC 1194926. PMID 16109768.
• Zhu Q; Pearson-White S; Luo K (2006). "Requirement for the SnoN Oncoprotein in Transforming Growth Factor β-Induced Oncogenic Transformation of Fibroblast Cells". Mol. Cell. Biol. 25 (24): 10731–44. doi:10.1128/MCB.25.24.10731-10744.2005. PMC 1316959. PMID 16314499.
• Briones-Orta MA, Sosa-Garrocho M, Moreno-Alvarez P, et al. (2006). "SnoN co-repressor binds and represses smad7 gene promoter". Biochem. Biophys. Res. Commun. 341 (3): 889–94. doi:10.1016/j.bbrc.2006.01.041. PMID 16442497.