SAP18

Histone deacetylase complex subunit SAP18 is an enzyme that in humans is encoded by the SAP18 gene.[4][5]

SAP18
Available structures PDB Human UniProt search: PDBe RCSB List of PDB id codes 2HDE
Identifiers
Aliases	SAP18, 2HOR0202, SAP18P, Sin3A associated protein 18kDa, Sin3A associated protein 18
External IDs	OMIM: 602949 MGI: 3704317 HomoloGene: 4289 GeneCards: SAP18
Gene location (Human) Chr. Chromosome 13 (human)[1] Band 13q12.11 Start 21,140,514 bp[1] End 21,149,084 bp[1]
RNA expression pattern More reference expression data
Gene ontology Molecular function • GO:0001106 transcription corepressor activity • GO:0001948 protein binding • histone deacetylase activity • RNA binding Cellular component • histone deacetylase complex • nuclear speck • exon-exon junction complex • nucleoplasm • ASAP complex • cell nucleus • cytoplasm • cytosol • nuclear body Biological process • regulation of transcription, DNA-templated • regulation of transcription from RNA polymerase II promoter • mRNA processing • regulation of alternative mRNA splicing, via spliceosome • transcription, DNA-templated • negative regulation of mRNA splicing, via spliceosome • RNA splicing • positive regulation of apoptotic process • negative regulation of nucleic acid-templated transcription • histone deacetylation Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	10284	100041953
Ensembl	ENSG00000150459	n/a
UniProt	O00422	n/a
RefSeq (mRNA)	NM_005870 NM_001366643	NM_001142441
RefSeq (protein)	NP_005861 NP_001353572	n/a
Location (UCSC)	Chr 13: 21.14 – 21.15 Mb	n/a
PubMed search	[2]	[3]
Wikidata
View/Edit Human View/Edit Mouse

Function

Histone acetylation plays a key role in the regulation of eukaryotic gene expression. Histone acetylation and deacetylation are catalyzed by multisubunit complexes. The protein encoded by this gene is a component of the histone deacetylase complex, which includes SIN3, SAP30, HDAC1, HDAC2, RbAp46, RbAp48, and other polypeptides. This protein directly interacts with SIN3 and enhances SIN3-mediated transcriptional repression when tethered to the promoter.[5] Additionally, SAP18s splice variants are implicated in apoptotic cycles.[6]

Interactions

SAP18 has been shown to interact with

• POLE2,[7][8] and
• RGS10.[9]

References

1. GRCh38: Ensembl release 89: ENSG00000150459 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. Zhang Y, Iratni R, Erdjument-Bromage H, Tempst P, Reinberg D (May 1997). "Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex". Cell. 89 (3): 357–64. doi:10.1016/S0092-8674(00)80216-0. PMID 9150135.
5. "Entrez Gene: SAP18 Sin3A-associated protein, 18kDa".
6. Michelle L, Cloutier A, Toutant J, Shkreta L, Thibault P, Durand M, Garneau D, Gendron D, Lapointe E, Couture S, Le Hir H, Klinck R, Elela SA, Prinos P, Chabot B (March 2012). "Proteins associated with the exon junction complex also control the alternative splicing of apoptotic regulators". Molecular and Cellular Biology. 32 (5): 954–67. doi:10.1128/MCB.06130-11. PMC 3295189. PMID 22203037.
7. Wada M, Miyazawa H, Wang RS, Mizuno T, Sato A, Asashima M, Hanaoka F (March 2002). "The second largest subunit of mouse DNA polymerase epsilon, DPE2, interacts with SAP18 and recruits the Sin3 co-repressor protein to DNA". Journal of Biochemistry. 131 (3): 307–11. doi:10.1093/oxfordjournals.jbchem.a003104. PMID 11872158.
8. Cheng SY, Bishop JM (April 2002). "Suppressor of Fused represses Gli-mediated transcription by recruiting the SAP18-mSin3 corepressor complex". Proceedings of the National Academy of Sciences of the United States of America. 99 (8): 5442–7. doi:10.1073/pnas.082096999. PMC 122788. PMID 11960000.
9. Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

Further reading

• Koipally J, Renold A, Kim J, Georgopoulos K (June 1999). "Repression by Ikaros and Aiolos is mediated through histone deacetylase complexes". The EMBO Journal. 18 (11): 3090–100. doi:10.1093/emboj/18.11.3090. PMC 1171390. PMID 10357820.
• Wada M, Miyazawa H, Wang RS, Mizuno T, Sato A, Asashima M, Hanaoka F (March 2002). "The second largest subunit of mouse DNA polymerase epsilon, DPE2, interacts with SAP18 and recruits the Sin3 co-repressor protein to DNA". Journal of Biochemistry. 131 (3): 307–11. doi:10.1093/oxfordjournals.jbchem.a003104. PMID 11872158.
• Cheng SY, Bishop JM (April 2002). "Suppressor of Fused represses Gli-mediated transcription by recruiting the SAP18-mSin3 corepressor complex". Proceedings of the National Academy of Sciences of the United States of America. 99 (8): 5442–7. doi:10.1073/pnas.082096999. PMC 122788. PMID 11960000.
• Paces-Fessy M, Boucher D, Petit E, Paute-Briand S, Blanchet-Tournier MF (March 2004). "The negative regulator of Gli, Suppressor of fused (Sufu), interacts with SAP18, Galectin3 and other nuclear proteins". The Biochemical Journal. 378 (Pt 2): 353–62. doi:10.1042/BJ20030786. PMC 1223961. PMID 14611647.
• Andersen JS, Lam YW, Leung AK, Ong SE, Lyon CE, Lamond AI, Mann M (January 2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413.

External links

• SAP18 human gene location in the UCSC Genome Browser.
• SAP18 human gene details in the UCSC Genome Browser.