SNW1

SNW1
Identifiers
Aliases	SNW1, Bx42, NCOA-62, PRPF45, Prp45, SKIIP, SKIP, SNW domain containing 1, SKIP1, FUN20
External IDs	OMIM: 603055; MGI: 1913604; HomoloGene: 56557; GeneCards: SNW1; OMA:SNW1 - orthologs
Gene location (Human) Chr. Chromosome 14 (human) Band 14q24.3 Start 77,717,599 bp End 77,761,207 bp
Gene location (Mouse) Chr. Chromosome 12 (mouse) Band 12|12 D2 Start 87,495,845 bp End 87,519,044 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in epithelium of nasopharynx parotid gland Achilles tendon amniotic fluid parietal pleura tendon of biceps brachii germinal epithelium trabecular bone tibia vena cava Top expressed in renal corpuscle Epithelium of choroid plexus retinal pigment epithelium medullary collecting duct ureter motor neuron maxillary prominence primitive streak ventricular zone genital tubercle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transcription corepressor activity transcription coactivator activity Notch binding protein binding retinoic acid receptor binding SMAD binding vitamin D receptor binding RNA binding enzyme binding androgen receptor binding Cellular component catalytic step 2 spliceosome nuclear matrix nucleoplasm cyclin/CDK positive transcription elongation factor complex spliceosomal complex nucleus nuclear body post-mRNA release spliceosomal complex nuclear speck U2-type catalytic step 2 spliceosome Biological process Notch signaling pathway cellular response to retinoic acid positive regulation of transforming growth factor beta receptor signaling pathway intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator regulation of transcription, DNA-templated positive regulation of mRNA splicing, via spliceosome regulation of retinoic acid receptor signaling pathway regulation of transcription by RNA polymerase II mRNA processing regulation of vitamin D receptor signaling pathway negative regulation of transcription by RNA polymerase II positive regulation of neurogenesis retinoic acid receptor signaling pathway positive regulation of histone H3-K4 methylation RNA splicing positive regulation of vitamin D receptor signaling pathway transcription initiation from RNA polymerase II promoter viral process negative regulation of transcription, DNA-templated positive regulation by host of viral transcription positive regulation of transcription by RNA polymerase II transcription, DNA-templated mRNA splicing, via spliceosome generation of catalytic spliceosome for second transesterification step positive regulation of transcription of Notch receptor target positive regulation of Notch signaling pathway Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 22938 66354 Ensembl ENSG00000100603 ENSMUSG00000021039 UniProt Q13573 Q9CSN1 RefSeq (mRNA) NM_012245 NM_001318844 NM_025507 RefSeq (protein) NP_001305773 NP_036377 NP_079783 Location (UCSC) Chr 14: 77.72 – 77.76 Mb Chr 12: 87.5 – 87.52 Mb PubMed search
Wikidata
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SNW domain-containing protein 1 is a protein that in humans is encoded by the SNW1 gene.

Function

This gene, a member of the SNW gene family, encodes a coactivator that enhances transcription from some Pol II promoters. This coactivator can bind to the ligand-binding domain of the vitamin D receptor and to retinoid receptors to enhance vitamin D-, retinoic acid-, estrogen-, and glucocorticoid-mediated gene expression. It can also function as a splicing factor by interacting with poly(A)-binding protein 2 to directly control the expression of muscle-specific genes at the transcriptional level. Finally, the protein may be involved in oncogenesis since it interacts with a region of SKI oncoproteins that is required for transforming activity.

Interactions

SNW1 has been shown to interact with:

• CIR,
• Calcitriol receptor,
• Histone deacetylase 2,
• Mothers against decapentaplegic homolog 2,
• Mothers against decapentaplegic homolog 3,
• NOTCH1
• Nuclear receptor co-repressor 2,
• Nuclear receptor coactivator 1,
• PABPN1,
• RBPJ,
• Retinoblastoma protein, and
• SKI protein.

Further reading

• Dahl R, Wani B, Hayman MJ (Mar 1998). "The Ski oncoprotein interacts with Skip, the human homolog of Drosophila Bx42". Oncogene. 16 (12): 1579–86. doi:10.1038/sj.onc.1201687. PMID 9569025.
• Zhou S, Fujimuro M, Hsieh JJ, Chen L, Hayward SD (Feb 2000). "A role for SKIP in EBNA2 activation of CBF1-repressed promoters". Journal of Virology. 74 (4): 1939–47. doi:10.1128/JVI.74.4.1939-1947.2000. PMC 111672. PMID 10644367.
• Zhou S, Fujimuro M, Hsieh JJ, Chen L, Miyamoto A, Weinmaster G, Hayward SD (Apr 2000). "SKIP, a CBF1-associated protein, interacts with the ankyrin repeat domain of NotchIC To facilitate NotchIC function". Molecular and Cellular Biology. 20 (7): 2400–10. doi:10.1128/MCB.20.7.2400-2410.2000. PMC 85419. PMID 10713164.
• Leong GM, Subramaniam N, Figueroa J, Flanagan JL, Hayman MJ, Eisman JA, Kouzmenko AP (May 2001). "Ski-interacting protein interacts with Smad proteins to augment transforming growth factor-beta-dependent transcription". The Journal of Biological Chemistry. 276 (21): 18243–8. doi:10.1074/jbc.M010815200. PMID 11278756.
• Kim YJ, Noguchi S, Hayashi YK, Tsukahara T, Shimizu T, Arahata K (May 2001). "The product of an oculopharyngeal muscular dystrophy gene, poly(A)-binding protein 2, interacts with SKIP and stimulates muscle-specific gene expression". Human Molecular Genetics. 10 (11): 1129–39. doi:10.1093/hmg/10.11.1129. PMID 11371506.
• Beatus P, Lundkvist J, Oberg C, Pedersen K, Lendahl U (Jun 2001). "The origin of the ankyrin repeat region in Notch intracellular domains is critical for regulation of HES promoter activity". Mechanisms of Development. 104 (1–2): 3–20. doi:10.1016/S0925-4773(01)00373-2. PMID 11404076.
• Zhou S, Hayward SD (Sep 2001). "Nuclear localization of CBF1 is regulated by interactions with the SMRT corepressor complex". Molecular and Cellular Biology. 21 (18): 6222–32. doi:10.1128/MCB.21.18.6222-6232.2001. PMC 87339. PMID 11509665.
• Zhang C, Baudino TA, Dowd DR, Tokumaru H, Wang W, MacDonald PN (Nov 2001). "Ternary complexes and cooperative interplay between NCoA-62/Ski-interacting protein and steroid receptor coactivators in vitamin D receptor-mediated transcription". The Journal of Biological Chemistry. 276 (44): 40614–20. doi:10.1074/jbc.M106263200. PMID 11514567.
• Prathapam T, Kühne C, Hayman M, Banks L (Sep 2001). "Ski interacts with the evolutionarily conserved SNW domain of Skip". Nucleic Acids Research. 29 (17): 3469–76. doi:10.1093/nar/29.17.3469. PMC 55893. PMID 11522815.
• Jurica MS, Licklider LJ, Gygi SR, Grigorieff N, Moore MJ (Apr 2002). "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis". RNA. 8 (4): 426–39. doi:10.1017/S1355838202021088. PMC 1370266. PMID 11991638.
• Wardell SE, Boonyaratanakornkit V, Adelman JS, Aronheim A, Edwards DP (Aug 2002). "Jun dimerization protein 2 functions as a progesterone receptor N-terminal domain coactivator". Molecular and Cellular Biology. 22 (15): 5451–66. doi:10.1128/MCB.22.15.5451-5466.2002. PMC 133955. PMID 12101239.
• Prathapam T, Kühne C, Banks L (Dec 2002). "Skip interacts with the retinoblastoma tumor suppressor and inhibits its transcriptional repression activity". Nucleic Acids Research. 30 (23): 5261–8. doi:10.1093/nar/gkf658. PMC 137971. PMID 12466551.
• Petersen HH, Hilpert J, Militz D, Zandler V, Jacobsen C, Roebroek AJ, Willnow TE (Feb 2003). "Functional interaction of megalin with the megalinbinding protein (MegBP), a novel tetratrico peptide repeat-containing adaptor molecule". Journal of Cell Science. 116 (Pt 3): 453–61. doi:10.1242/jcs.00243. PMID 12508107.
• Barry JB, Leong GM, Church WB, Issa LL, Eisman JA, Gardiner EM (Mar 2003). "Interactions of SKIP/NCoA-62, TFIIB, and retinoid X receptor with vitamin D receptor helix H10 residues". The Journal of Biological Chemistry. 278 (10): 8224–8. doi:10.1074/jbc.C200712200. PMID 12529369.
• Zhang C, Dowd DR, Staal A, Gu C, Lian JB, van Wijnen AJ, Stein GS, MacDonald PN (Sep 2003). "Nuclear coactivator-62 kDa/Ski-interacting protein is a nuclear matrix-associated coactivator that may couple vitamin D receptor-mediated transcription and RNA splicing". The Journal of Biological Chemistry. 278 (37): 35325–36. doi:10.1074/jbc.M305191200. PMID 12840015.
• Leong GM, Subramaniam N, Issa LL, Barry JB, Kino T, Driggers PH, Hayman MJ, Eisman JA, Gardiner EM (Mar 2004). "Ski-interacting protein, a bifunctional nuclear receptor coregulator that interacts with N-CoR/SMRT and p300". Biochemical and Biophysical Research Communications. 315 (4): 1070–6. doi:10.1016/j.bbrc.2004.02.004. PMID 14985122.